Page last updated: 2024-11-12

calpain

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Description

Calpain: Cysteine proteinase found in many tissues. Hydrolyzes a variety of endogenous proteins including NEUROPEPTIDES; CYTOSKELETAL PROTEINS; proteins from SMOOTH MUSCLE; CARDIAC MUSCLE; liver; platelets; and erythrocytes. Two subclasses having high and low calcium sensitivity are known. Removes Z-discs and M-lines from myofibrils. Activates phosphorylase kinase and cyclic nucleotide-independent protein kinase. This enzyme was formerly listed as EC 3.4.22.4. [Medical Subject Headings (MeSH), National Library of Medicine, extracted Dec-2023]

Cross-References

ID SourceID
PubMed CID20086354
SCHEMBL ID8744665
MeSH IDM0003226

Synonyms (2)

Synonym
calpain
SCHEMBL8744665

Research Excerpts

Overview

Calpain is an important marker and mediator in the pathophysiology of neurodegeneration. Calpain 6 (CAPN6) is a non-classical calpain that has been reported to be overexpressed in CKD.

ExcerptReferenceRelevance
"Calpains are a family of Ca"( CAPN3: A muscle‑specific calpain with an important role in the pathogenesis of diseases (Review).
Chen, L; Gao, H; Li, X; Tang, F; Xiao, D; Zhang, X, 2021
)
2.37
"Calpain is an important marker and mediator in the pathophysiology of neurodegeneration."( Calpain Inhibitors as Potential Therapeutic Modulators in Neurodegenerative Diseases.
Garg, N; Kaur, A; Khan, H; Singh, TG; Thapa, K, 2022
)
2.89
"Calpains are a family of calcium-activated proteases involved in numerous disorders. "( Visualizing Cell Death in Live Retina: Using Calpain Activity Detection as a Biomarker for Retinal Degeneration.
Belhadj, S; Christensen, G; Hermann, NS; Paquet-Durand, F; Strasser, T; Zhu, Y, 2022
)
2.42
"Calpain-5 (CAPN5) is a member of the calpain family of calcium-activated neutral thiol proteases. "( S-acylation regulates the membrane association and activity of Calpain-5.
Bondada, V; Croall, DE; Gal, J; Geddes, JW; Mashburn, CB; Rodgers, DW, 2022
)
2.4
"Calpains are a family of calcium-dependent thiol proteases that participate in a wide variety of biological activities. "( Myeloid cell-specific deletion of Capns1 prevents macrophage polarization toward the M1 phenotype and reduces interstitial lung disease in the bleomycin model of systemic sclerosis.
Chen, R; Greer, PA; Li, Z; Peng, T; Wang, Q; Yan, Y; Yu, Y; Zhang, L; Zheng, D, 2022
)
2.16
"Calpain 6 (CAPN6) is a non-classical calpain that has been reported to be overexpressed in CKD."( Advanced glycation end products promote the progression of chronic kidney diseases by targeting calpain 6.
Han, H; Jiang, M; Qian, Y; Wang, Q; Zhang, Y, 2023
)
1.85
"Calpain-3 (CAPN3) is a muscle-specific member of the calpain family of Ca"( Calpain-3 Is Not a Sodium Dependent Protease and Simply Requires Calcium for Activation.
Lamb, GD; Murphy, RM; Wette, SG, 2023
)
3.8
"Calpain is an intracellular cysteine protease that cleaves its specific substrates in a limited region to modulate cellular function. "( Calpain-3 not only proteolyzes calpain-1 and -2 but also is a substrate for calpain-1 and -2.
Hata, S; Muroya, S; Ojima, K; Ono, Y; Shinkai-Ouchi, F, 2023
)
3.8
"Calpain 15 (CAPN15) is an intracellular cysteine protease belonging to the non-classical small optic lobe (SOL) family of calpains, which has an important role in development. "( Behavioral characterization of Capn15 conditional knockout mice.
Gamache, K; Hardt, OM; Sossin, WS; Zha, C, 2023
)
2.35
"Calpain 2 (CAPN2) is a Ca"( Regulation of calpain 2 expression by miR-223 and miR-145.
Fleming, I; Randriamboavonjy, V; Siuda, D, 2019
)
2.32
"Calpain is a Ca"( An unexpected co-crystal structure of the calpain PEF(S) domain with Hfq reveals a potential chaperone function of Hfq.
Allemann, RK; Cresser-Brown, J; Jin, Y; Miller, DJ; Rizkallah, P; Roth, C, 2020
)
2.27
"Calpain-2 is a Ca"( Calpain-2 activity promotes aberrant endoplasmic reticulum stress-related apoptosis in hepatocytes.
Cai, S; Chen, YS; Han, B; Hu, XX; Xie, RJ; Yang, Q; Yang, T; Yang, Y; Zheng, L, 2020
)
3.44
"Calpains are a well-known family of calcium-dependent cysteine proteases that regulate several processes, including cellular adhesion, proliferation, and migration, as well as inflammation and angiogenesis."( Targeted inhibition of endothelial calpain delays wound healing by reducing inflammation and angiogenesis.
Huang, H; Peng, G; Shen, Z; Teng, X; Wu, W; Yi, C; Zheng, D, 2020
)
1.56
"Calpain is a cytosolic proteinase that regulates of a wide range of physiological functions. "( An update on the therapeutic potential of calpain inhibitors: a patent review.
Donkor, IO, 2020
)
2.27
"Calpain 15 (CAPN15) is an intracellular cysteine protease belonging to the non-classical small optic lobe (SOL) family of calpains, an important class of developmental proteins, as yet uncharacterized in vertebrates."( Biallelic variants in the small optic lobe calpain CAPN15 are associated with congenital eye anomalies, deafness and other neurodevelopmental deficits.
Al-Abdi, L; Alkuraya, FS; Ceroni, F; Farah, CA; Helaby, R; Holt, RJ; Khan, AO; Kraus, A; Lévesque, S; Ragge, NK; Sossin, WS; Thuriot, F; Zha, C, 2020
)
1.54
"Calpain is a type of calcium-dependent cysteine protease that includes dozens of isoforms."( Calpain Activation and Organ Failure in Sepsis: Molecular Insights and Therapeutic Perspectives.
Huang, Y; Peng, T; Wang, G, 2021
)
2.79
"Calpains are a family of soluble calcium-dependent proteases that are involved in multiple regulatory pathways. "( Calpain-1 and Calpain-2 in the Brain: New Evidence for a Critical Role of Calpain-2 in Neuronal Death.
Baudry, M; Bi, X; Liu, Y; Wang, Y, 2020
)
3.44
"Calpains are a family of nonlysosomal cysteine proteases, which play important roles in numerous physiological and pathological processes. "( Effects of functionally diverse calpain system on immune cells.
Chen, Y; Liu, F; Su, Z, 2021
)
2.35
"Calpain is a family of stress-responsive intracellular proteases and is inducible in cancer and stromal cells during carcinogenesis."( Calpain-Associated Proteolytic Regulation of the Stromal Microenvironment in Cancer.
Akasu, R; Miyazaki, A; Miyazaki, T,
)
2.3
"Calpain I is a calcium-dependent cysteine protease which has dual effects on tissue inflammation depending on its cellular location. "( Intracellular versus extracellular inhibition of calpain I causes differential effects on pain in a rat model of joint inflammation.
McConnell, M; McDougall, JJ; Reid, AR,
)
1.83
"Calpain-2 (CAPN2) is a processing enzyme ubiquitously expressed in mammalian tissues whose pleiotropic functions depend on the role played by its cleaved-products. "( Cleavage and activation of LIM kinase 1 as a novel mechanism for calpain 2-mediated regulation of nuclear dynamics.
Company, S; García-Trevijano, ER; Rodríguez-Fernández, L; Viña, JR; Zaragozá, R, 2021
)
2.3
"Calpains are a family of calcium-dependent non-lysosomal cysteine proteases. "( Endothelial cell calpain as a critical modulator of angiogenesis.
Cai, H; Liu, NM; Wang, Y; Youn, JY; Zhang, Y, 2017
)
2.24
"Calpains are a family of ubiquitously expressed intracellular Ca"( ENaC activity is regulated by calpain-2 proteolysis of MARCKS proteins.
Al-Khalili, O; Alli, AA; Eaton, DC; Ghazi, ZM; Ma, HP; Montgomery, DS; Thai, TL; Yu, L, 2017
)
1.47
"Calpains are a family of Ca"( Targeting calpains: A novel immunomodulatory approach for microbial infections.
Ahmad, A; Kumar, V, 2017
)
2.3
"Calpains are a family of intracellular proteases defined by a conserved protease domain. "( Novel calpain families and novel mechanisms for calpain regulation in Aplysia.
Courchesne, C; Fan, X; Freibauer, A; Gong, K; Hastings, MH; Sossin, WS, 2017
)
2.38
"Calpain is a Ca"( Hippocampal calpain is required for the consolidation and reconsolidation but not extinction of contextual fear memory.
Isoda, K; Kida, S; Mamiya, N; Nagayoshi, T, 2017
)
1.56
"Calpain 3 (CAPN3) is a calcium dependent protease residing in the myofibrillar, cytosolic and triad fractions of skeletal muscle."( Calpain 3 and CaMKIIβ signaling are required to induce HSP70 necessary for adaptive muscle growth after atrophy.
Eskin, A; Kramerova, I; Nelson, SF; Spencer, MJ; Torres, JA, 2018
)
2.64
"Calpain-1 is a protease that is implicated in several pathological conditions that affect the heart."( Uric Acid Induces Cardiomyocyte Apoptosis via Activation of Calpain-1 and Endoplasmic Reticulum Stress.
Chen, K; He, L; Huang, D; Li, J; Li, S; Yan, M, 2018
)
1.44
"Calpains are a group of non-lysosomal Ca"( Calpains: Diverse Functions but Enigmatic.
Hosseini, M; Kahrizi, K; Najmabadi, H, 2018
)
3.37
"Calpainopathy is an autosomal recessive form of limb girdle muscular dystrophies (LGMDs) caused by mutations in the CAPN3 gene. "( Molecular genetic study of Calpainopathy in Iran.
Bagherian, H; Habibi, H; Khajeh, A; Mojbafan, M; Zeinali, S, 2018
)
2.22
"Calpain is a type of calcium-dependent protease that plays a critical role in memory consolidation and reconsolidation."( Basolateral amygdala calpain is required for extinction of contextual fear-memory.
Chen, H; Song, Z; Wu, S; Xu, W; Zhu, G, 2018
)
1.52
"Calpains (CAPNs) are a family of calcium-activated cysteine proteases. "( Redox Regulation of Calpains: Consequences on Vascular Function.
Fleming, I; Kyselova, A; Randriamboavonjy, V, 2019
)
2.28
"Calpains are a conserved family of calcium-dependent cysteine proteinases with ubiquitous or tissue-specific expression."( Evidence for calpains in cancer metastasis.
Chen, J; Fang, X; Hu, X; Wu, Y; Zhang, L, 2019
)
1.6
"Calpains are a 15-member class of calcium-activated nonlysosomal neutral proteases. "( In Vivo Monitoring of Calpain Activity by Forster Resonance Energy Transfer.
Lostal, W; Richard, I; Stockholm, D, 2019
)
2.27
"Calpains are a family of calcium-dependent intracellular cysteine proteases that regulate important physiological processes by substrate cleavage. "( Determining Temporal and Spatial Expression of Calpains in Amphibians.
Antoniades, I; Charalambous, A; Christodoulou, N; Skourides, PA; Zanardelli, S, 2019
)
2.21
"Calpains are a family of calcium-dependent intracellular cysteine proteases that regulate important physiological processes by substrate cleavage. "( Methods of Calpain Inhibition to Determine the Role of Calpains in Embryo Development in Amphibians.
Antoniades, I; Charalambous, A; Christodoulou, N; Skourides, PA; Zanardelli, S, 2019
)
2.35
"Calpain 1 is a proinflammatory calcium-activated cysteine protease, which can be partly externalized. "( Calpain 1 in bronchoalveolar lavage fluid is associated with poor prognosis in lepidic predominant pulmonary adenocarcinoma.
Antoine, M; Baud, L; Cadranel, J; Duruisseaux, M; Perez, J; Rabbe, N; Ruppert, AM; Vieira, T; Wislez, M, 2019
)
3.4
"Calpain-7 is a mammalian ortholog of a fungal non-classical calpain named PalB, which is an intracellular cysteine protease and functions in fungal alkaline adaptation in association with the endosomal sorting complex required for transport (ESCRT) system. "( Analysis of limited proteolytic activity of calpain-7 using non-physiological substrates in mammalian cells.
Kiso, S; Maemoto, Y; Maki, M; Shibata, H, 2013
)
2.09
"Calpain is an intracellular Ca²⁺-activated protease that is involved in numerous Ca²⁺ dependent regulation of protein function in many cell types. "( Calpain inhibition reduces amplitude and accelerates decay of the late sodium current in ventricular myocytes from dogs with chronic heart failure.
Maltsev, VA; Sabbah, HN; Undrovinas, A, 2013
)
3.28
"Calpain 10 expression is a potential prognostic marker in patients with esophageal squamous cell carcinoma."( Oncogene GAEC1 regulates CAPN10 expression which predicts survival in esophageal squamous cell carcinoma.
Chan, D; Chan, KW; Chan, SH; Chan, YP; Gopalan, V; Lam, AK; Law, SY; Liu, CD; Tang, JC; Tsoi, MY, 2013
)
1.11
"Calpains are a conserved family of calcium-dependent cysteine proteinases involved in various cellular functions. "( Calpains are required for invasive and metastatic potentials of human HCC cells.
Chen, B; Chen, ZN; Guo, YS; Jiang, JL; Li, Y; Tang, J, 2013
)
3.28
"m-calpain is a potential target for AD therapeutics."( Hypoxia-triggered m-calpain activation evokes endoplasmic reticulum stress and neuropathogenesis in a transgenic mouse model of Alzheimer's disease.
An, L; Cai, JH; Wang, CY; Wang, T; Wang, X; Wang, ZY; Xie, JW; Xu, Y; Zhao, BL, 2013
)
1.27
"Calpains are a family of Ca(2+)-dependent intracellular cysteine proteases, including the ubiquitously expressed μ-calpain (CANP1) and m-calpain (CANP2). "( Significant role of μ-calpain (CANP1) in proliferation/survival of bovine skeletal muscle satellite cells.
Inho, H; Van Ba, H, 2013
)
2.15
"Calpain-10 (CAPN10) is a cysteine protease that is activated by intracellular calcium (Ca(2+)) and known to be involved in diseases such as cancer, heart attack, and stroke. "( Analysis of the structure of calpain-10 and its interaction with the protease inhibitor SNJ-1715.
Alves, CN; da Silva, RC; de Alencar, NA; Lameira, J, 2013
)
2.12
"Calpains are a family of calcium-dependent intracellular cysteine proteases that regulate several physiological processes by limited cleavage of different substrates. "( Calpain2 protease: A new member of the Wnt/Ca(2+) pathway modulating convergent extension movements in Xenopus.
Christodoulou, N; Skourides, PA; Zanardelli, S, 2013
)
3.28
"Calpain is an up-stream regulator that regulates ROS-mediated GPIbα shedding."( The role of intraplatelet reactive oxygen species in the regulation of platelet glycoprotein Ibα ectodomain shedding.
Dai, J; Dai, K; Du, J; Liu, G; Wang, X; Yan, R; Zhang, F; Zhang, P; Zhang, Y; Zhao, L, 2013
)
1.11
"Calpain is a family of neutral cysteine proteinase involved in many physiological and pathological processes including virus replication, autophagy and apoptosis. "( Coxsackievirus B3-induced calpain activation facilitates the progeny virus replication via a likely mechanism related with both autophagy enhancement and apoptosis inhibition in the early phase of infection: an in vitro study in H9c2 cells.
Chen, R; Ge, J; Li, M; Peng, T; Wang, X; Xie, Y; Yu, Y; Zou, Y, 2014
)
2.15
"Calpain-1 is a calcium-activated cysteine protease that plays an important role in neutrophil motility."( Calpain-1 inhibitors for selective treatment of rheumatoid arthritis: what is the future?
Adams, SE; Allemann, RK; Hallett, MB; Miller, DJ, 2013
)
2.55
"Calpains are a family of calcium-dependent cysteine proteases that are ubiquitously expressed in mammals and play critical roles in neuronal death by catalyzing substrate proteolysis. "( Gel-based protease proteomics for identifying the novel calpain substrates in dopaminergic neuronal cell.
Baek, JY; Jeong, JY; Jin, BK; Ju, C; Kim, C; Kim, WK; Lee, YM; Oh, YJ; Song, HY; Youdim, MB; Yun, N, 2013
)
2.08
"Calpain 2 is an intracellular calcium-dependent proteolytic enzyme which cleaves numerous focal adhesion proteins."( Calpain 2 activity increases at the time of implantation in rat uterine luminal epithelial cells and administration of calpain inhibitor significantly reduces implantation sites.
Day, ML; Kaneko, Y; Murphy, CR, 2014
)
2.57
"The calpains are a superfamily of proteases with extensive relevance to human health and welfare. "( Characterization of the definitive classical calpain family of vertebrates using phylogenetic, evolutionary and expression analyses.
Macqueen, DJ; Wilcox, AH, 2014
)
1.22
"Calpain-10 is a ubiquitously expressed protease that serves as an intracellular calcium-dependent cysteine protease and is regarded to be one of the candidate genes for type 2 diabetes mellitus (T2DM). "( A case-control study on the association of common variants of CAPN10 gene and the risk of type 2 diabetes in an Iranian population.
Bakhtiyari, S; Haghani, K; Mahdieh, N; Mahmoodi, K; Maleki, F; Sayehmiri, K; Shokouhi, S, 2014
)
1.85
"Calpains are a family of cytoplasmic calcium-dependent proteinases with papain-like activity. "( [Calpains: general characteristics and role in various states of the organism].
Koval', SM; Samokhina, LM; Snigurs'ka, IO; Starodub, MF,
)
2.48
"Calpain 5 (CAPN5) is a non-classical member of the calpain family. "( Calpain 5 is highly expressed in the central nervous system (CNS), carries dual nuclear localization signals, and is associated with nuclear promyelocytic leukemia protein bodies.
Bondada, V; Brewer, MK; Geddes, JW; Graham, B; Lou, D; Mashburn, CB; Singh, R, 2014
)
3.29
"Calpain-3, or p94, is a skeletal muscle-specific isoform that is genetically linked to limb-girdle muscular dystrophy."( Crystal structure of calpain-3 penta-EF-hand (PEF) domain - a homodimerized PEF family member with calcium bound at the fifth EF-hand.
Allingham, JS; Campbell, RL; Davies, PL; Partha, SK; Ravulapalli, R, 2014
)
1.44
"Calpain-7 (CAPN7) is a unique intracellular cysteine protease that has a tandem repeat of microtubule interacting and trafficking (MIT) domains and lacks a penta-EF-hand domain. "( Involvement of calpain-7 in epidermal growth factor receptor degradation via the endosomal sorting pathway.
Kiso, S; Maemoto, Y; Maki, M; Ono, Y; Shibata, H; Sorimachi, H; Takahara, T, 2014
)
2.2
"Calpain-I is a Ca(2+)-dependent protease that plays a key role in the extravasation of neutrophils from the blood stream prior to causing damage within affected tissues."( The structural basis of differential inhibition of human calpain by indole and phenyl α-mercaptoacrylic acids.
Adams, SE; Allemann, RK; Hallett, MB; Miller, DJ; Rizkallah, PJ; Robinson, EJ, 2014
)
1.37
"Calpains are a complex family of ubiquitous or tissue-specific cysteine proteases that proteolyze a variety of substrates (leading to their degradation or functional modulation) and are implicated in several pathophysiological phenomena. "( Calpains and cancer: friends or enemies?
Allavena, G; Del Bello, B; Maellaro, E; Moretti, D, 2014
)
3.29
"Calpain is a family of cysteine proteases found in eukaryotes and a few bacteria. "( An updated patent review of calpain inhibitors (2012 - 2014).
Donkor, IO, 2015
)
2.15
"Calpain-3 is an intracellular cysteine protease, belonging to Calpain superfamily and predominantly expressed in skeletal muscle. "( Calpain-3 impairs cell proliferation and stimulates oxidative stress-mediated cell death in melanoma cells.
Allavena, G; Corti, A; Del Bello, B; Maellaro, E; Moretti, D; Signorini, C, 2015
)
3.3
"Calpain-3 (CAPN3) is a member of the calpain family of Ca(2+)-regulated cysteine proteases, which play an important role in sarcomere remodeling and mitochondrial protein turnover, and thus, regulating beef tenderness in cattle. "( Characterization of a novel CAPN3 transcript generated by alternative splicing in cattle.
Dai, LS; Gao, Y; Jiang, H; Liu, SY; Yuan, B; Zhang, JB, 2015
)
1.86
"Calpain is a family of cysteine proteases that has an important role in the initiation, regulation, and execution of cell death. "( Calpain inhibition decreases myocardial apoptosis in a swine model of chronic myocardial ischemia.
Abid, MR; Elmadhun, NY; Feng, J; Liu, Y; Mitchell, H; Potz, BA; Quesenberry, P; Sabe, AA; Sellke, FW, 2015
)
3.3
"The calpains are a family of intracellular cysteine proteases that function in a wide array of cellular activities, including cytoskeletal remodelling, survival and apoptosis. "( Calpain in Breast Cancer: Role in Disease Progression and Treatment Response.
Martin, SG; Pu, X; Storr, SJ; Thompson, N; Zhang, Y, 2015
)
2.42
"Calpain is a ubiquitous calcium-sensitive protease that is essential for normal physiologic function."( Role of the calpain on the development of diabetes mellitus and its chronic complications.
Li, XF; Li, YB; Su, Y; Sun, YM; Wan, TT, 2015
)
1.52
"Calpain 3 (CAPN3) is a tissue specific calpain, and its mRNA is the most expressed calpain isoform in skeletal muscles. "( Investigation of biochemical changes of the ovine calpain 3 exon-10 polymorphism.
Morton, J; Muto, Y; Palmer, D, 2015
)
2.11
"Calpains are a class of calcium-activated non-lysosomal cysteine proteases that serve as a proteolytic unit for cellular homeostasis."( Calpains and Coronary Vascular Disease.
Abid, MR; Potz, BA; Sabe, AA; Sellke, FW, 2016
)
2.6
"Calpain-1 is a ubiquitously expressed calcium-activated intracellular cysteine protease. "( Calpain-1 is associated with adverse relapse free survival in breast cancer: a confirmatory study.
Ahmad, NS; Boddy, A; Chan, SY; Cresti, N; Ellis, IO; Martin, SG; Moseley, PM; Pu, X; Storr, SJ; Televantou, D, 2016
)
3.32
"Calpain 1 (CPN1) is a ubiquitous cysteine protease that exists in both cytosol and cardiac mitochondria. "( Activation of mitochondrial calpain and increased cardiac injury: beyond AIF release.
Chen, Q; Hu, Y; Lesnefsky, EJ; Thompson, J, 2016
)
2.17
"Calpain3 is a calcium-dependent intracellular protease involved in an autosomal recessive form of muscular dystrophy known as limb-girdle muscular dystrophy type 2A. "( Report of limb girdle muscular dystrophy type 2a in 6 Iranian patients, one with a novel deletion in CAPN3 gene.
Akbari, MR; Beheshtian, M; Fadaee, M; Fattahi, Z; Godarzi, HR; Kahrizi, K; Kariminejad, A; Nafissi, S; Najmabadi, H; Vazehan, R,
)
1.57
"Calpain is a family of calcium-dependent nonlysosomal neutral cysteine endopeptidases. "( Calpain-2 activates Akt via TGF-β1-mTORC2 pathway in pulmonary artery smooth muscle cells.
Abeyrathna, P; Han, W; Kovacs, L; Su, Y, 2016
)
3.32
"Calpain is an intracellular Ca(2+)-regulated protease system whose substrates include proteins involved in proliferation, survival, migration, invasion, and sensitivity to therapeutic drugs. "( Calpain Genetic Disruption and HSP90 Inhibition Combine To Attenuate Mammary Tumorigenesis.
Gao, Y; Greer, PA; Grieve, S; Hall, C; Hu, J, 2016
)
3.32
"Calpain is a family of calcium-dependent endopeptidases, which plays an important role in ECM remodeling."( Activation of calpain by renin-angiotensin system in pleural mesothelial cells mediates tuberculous pleural fibrosis.
Cai, PC; Greer, PA; Li, FZ; Lu, YZ; Ma, WL; Shi, HZ; Su, Y; Xiang, F; Xin, JB; Xu, XX; Yang, J; Ye, H; Yu, F; Zhou, Q, 2016
)
1.52
"Calpainopathy is an autosomal recessive form of limb girdle muscular dystrophies which is caused by mutation in CAPN3 gene. "( Linkage Study Revealed Complex Haplotypes in a Multifamily due to Different Mutations in CAPN3 Gene in an Iranian Ethnic Group.
Abiri, M; Kianfar, S; Mojbafan, M; Nilipour, Y; Sarhadi, A; Tavakkoly-Bazzaz, J; Tonekaboni, SH; Zeinali, S, 2016
)
1.88
"Calpains are a group of Ca(2+)-dependent proteases that truncate specific proteins, and some of the cleavage products remain in the cell, although with a distinct function."( Calpains and neuronal damage in the ischemic brain: The swiss knife in synaptic injury.
Canzoniero, LM; Curcio, M; Duarte, CB; Mele, M; Salazar, IL, 2016
)
2.6
"The calpains are a family of intracellular cysteine proteases that function in a variety of important cellular functions, including cell signalling, motility, apoptosis and survival. "( The calpain system is associated with survival of breast cancer patients with large but operable inflammatory and non-inflammatory tumours treated with neoadjuvant chemotherapy.
Fatayer, H; Gahlaut, R; Lansdown, M; Martin, SG; Perren, T; Shaaban, A; Sharma, N; Storr, SJ; Zhang, S, 2016
)
1.55
"Calpain is an intracellular Ca(2+)-dependent protease, and the activation of calpain has been implicated in neurodegenerative diseases. "( Calpastatin overexpression reduces oxidative stress-induced mitochondrial impairment and cell death in human neuroblastoma SH-SY5Y cells by decreasing calpain and calcineurin activation, induction of mitochondrial fission and destruction of mitochondrial
Abubakar, Z; Chetsawang, B; Govitrapong, P; Kitiyanant, N; Leepiyasakulchai, C; Suwanjang, W; Tangmansakulchai, K, 2016
)
2.08
"Calpain-5 is a calcium-activated protease expressed in the retina. "( Small-angle X-ray scattering of calpain-5 reveals a highly open conformation among calpains.
Bassuk, AG; Gakhar, L; Khan, S; Mahajan, VB; Tsang, SH; Velez, G; Yang, J, 2016
)
2.16
"Calpain is a family of calcium-dependent endopeptidases, which plays an important role in ECM remodelling."( Calpain-activated mTORC2/Akt pathway mediates airway smooth muscle remodelling in asthma.
Cai, PC; Fang, J; Greer, PA; Li, FZ; Lin, YX; Liu, F; Ma, WL; Mu, Q; Rao, SS; Shi, HZ; Song, LJ; Su, Y; Xia, Y; Yang, J; Ye, H; Zeng, Y; Zhang, Q; Zhou, LL, 2017
)
2.62
"Calpains are a family of proteases that were scientifically recognized earlier than proteasomes and caspases, but remain enigmatic. "( Calpain research for drug discovery: challenges and potential.
Ono, Y; Saido, TC; Sorimachi, H, 2016
)
3.32
"Calpains are a family of intracellular, calcium-dependent cysteine proteases involved in a variety of regulatory processes, including cytoskeletal dynamics, cell-cycle progression, signal transduction, gene expression, and apoptosis. "( Calpain-14 and its association with eosinophilic esophagitis.
Kottyan, LC; Litosh, VA; Porollo, A; Rochman, M; Rothenberg, ME; Rymer, JK, 2017
)
3.34
"Calpain-3 (CAPN3) is a non-lysosomal cysteine protease that is necessary for normal muscle function, as mutations in CAPN3 result in an autosomal recessive form of limb girdle muscular dystrophy type 2A. "( Novel role of calpain-3 in the triad-associated protein complex regulating calcium release in skeletal muscle.
Granzier, H; Kramerova, I; Kudryashova, E; Ottenheijm, C; Spencer, MJ; Wu, B, 2008
)
2.15
"Calpain is a ubiquitous calcium-sensitive protease that is essential for normal physiologic neuronal function. "( Calpain-mediated signaling mechanisms in neuronal injury and neurodegeneration.
Brennan, CS; Chen, J; Vosler, PS, 2008
)
3.23
"Calpains are a family of calcium-dependent proteases with abundant expression in the CNS, and potent in cleaving some synaptic components. "( Calpain activity contributes to the control of SNAP-25 levels in neurons.
Antonucci, F; Berghuis, P; Bonanno, G; Caleo, M; Carmignoto, G; Dobszay, MB; Grumelli, C; Harkany, T; Matteoli, M; Pozzi, D; Verderio, C, 2008
)
3.23
"Calpain 3 is a member of the calpain family of calcium-dependent intracellular proteases. "( Calpain 3, the "gatekeeper" of proper sarcomere assembly, turnover and maintenance.
Beckmann, JS; Spencer, M, 2008
)
3.23
"Calpainopathy is an autosomal-recessive limb girdle muscular dystrophy (LGMD2A) characterized by selective atrophy and weakness of proximal limb girdle muscles. "( Phenotypic variability in siblings with calpainopathy (LGMD2A).
Bönnemann, CG; Kirschner, J; Korinthenberg, R; Lochmüller, H; Müller, CR; Schara, U; Schessl, J; Schreiber, G; Walter, MC, 2008
)
2.06
"Calpain is a ubiquitous protease found in different tissue types and in many organisms including mammals. "( Calpain and the glutamatergic synapse.
Doshi, S; Lynch, DR, 2009
)
3.24
"The calpain was found to be an arthropod M-class calpain homologue to Homarus americanus Calpain M (Ha-CalpM) and has thus been termed Nephrops norvegicus calpain M (Nn-CalpM)."( Molecular cloning and localization of a calpain-like protease from the abdominal muscle of Norway lobster Nephrops norvegicus.
Coombs, GH; Gornik, SG; Neil, DM; Westrop, GD, 2010
)
1.11
"Calpains are a ubiquitous cytoplasmic cysteine protease, the activity of which is absolutely dependent on calcium. "( A new SNP in the 3'UTR region of the bovine calpain small subunit (CAPNS1) gene.
Flisikowski, K; Juszczuk-Kubiak, E; Wicińska, K, 2010
)
2.06
"Calpain is a calcium ion-dependent cysteine protease, consisting of two primary isoforms (calpain1/calpain2) which mediate crucial cellular functions. "( Expression of typical calpains in mouse molar.
Matsunaga, T; Tachikawa, T; Yamamoto, G, 2009
)
2.11
"Calpains are a ubiquitous family of calcium-dependent cysteine proteases involved in a wide range of cell regulatory and differentiation processes. "( Expression and cellular localisation of calpain-like proteins in Trypanosoma brucei.
Apagyi, K; Ersfeld, K; Liu, W; McLeavy, L, 2010
)
2.07
"Calpains are a family of 14 calcium-regulated, intracellular cysteine proteases, which modulate cellular functions by limited, specific proteolysis."( Calpain inhibitor SNJ-1945 attenuates events prior to angiogenesis in cultured human retinal endothelial cells.
Azuma, M; Ma, H; Shearer, TR; Tochigi, A, 2009
)
2.52
"Calpain is a calcium-dependent protease that mediates cytoskeletal reorganization during cell migration."( Calpain inhibition impairs TNF-alpha-mediated neutrophil adhesion, arrest and oxidative burst.
Huttenlocher, A; Lokuta, MA; Surfus, JC; Wernimont, SA; Wiemer, AJ, 2010
)
2.52
"Calpain is a ubiquitous calcium-sensitive protease that is essential for normal physiologic neuronal function. "( Dysfunctional mitochondria uphold calpain activation: contribution to Parkinson's disease pathology.
Arduíno, DM; Cardoso, SM; Esteves, AR; Oliveira, CR; Swerdlow, RH, 2010
)
2.08
"Calpain is a calcium-dependent protease that plays a significant role in synaptic plasticity, cell motility, and neurodegeneration. "( Brain-derived neurotrophic factor and epidermal growth factor activate neuronal m-calpain via mitogen-activated protein kinase-dependent phosphorylation.
Baudry, M; Bi, X; Jourdi, H; Qin, Q; Rostamiani, K; Zadran, S, 2010
)
2.03
"Calpain 3 is a calcium-dependent cysteine protease that is primarily expressed in skeletal muscle and is implicated in limb girdle muscular dystrophy type 2A. "( Down-regulation of MyoD by calpain 3 promotes generation of reserve cells in C2C12 myoblasts.
Cottin, P; Dargelos, E; Lamarre, Y; Leibovitch, S; Poussard, S; Pouzoulet, F; Stuelsatz, P; Veschambre, P, 2010
)
2.1
"Calpain 3 (CAPN3) is a cysteine protease that when mutated causes Limb Girdle Muscular Dystrophy 2A. "( Calpain 3 is a rapid-action, unidirectional proteolytic switch central to muscle remodeling.
't Hoen, PA; de Galan, P; de Morrée, A; Frants, RR; Impagliazzo, A; Lutje Hulsik, D; van der Maarel, SM; van Haagen, HH; van Ommen, GB; van Remoortere, A, 2010
)
3.25
"Calpains are a family of intracellular calcium-dependent, non-lysosomal cysteine proteases that regulate cellular functions through proteolysis of numerous substrates."( Moderation of calpain activity promotes neovascular integration and lumen formation during VEGF-induced pathological angiogenesis.
Fox, JE; Hoang, MV; Nagy, JA; Senger, DR, 2010
)
1.44
"Calpains are a family of calcium-activated proteases involved in a number of cellular functions including cell death, proliferation and exocytosis. "( Impaired insulin secretion in transgenic mice over-expressing calpastatin in pancreatic β-cells.
Bell, GI; Johnson, JD; Otani, K; Polonsky, KS,
)
1.57
"Calpain is an intracellular Ca(2+)-activated protease and an important mediator of the actions of calcium. "( Physiologic and pathophysiologic role of calpain: implications for the occurrence of atrial fibrillation.
Bode-Böger, SM; Bukowska, A; Goette, A; Lendeckel, U, 2012
)
2.09
"The calpains are a family of cysteine proteases involved in some biological processes whose activities are highly dependent on Ca(2+). "( The PI3K-Akt pathway regulates calpain 6 expression, proliferation, and apoptosis.
Fan, J; Li, X; Li, Z; Liu, M; Liu, Y; Mei, C; Qiu, S; Shi, Y; Sun, L; Wang, L; Yin, P; Zha, X; Zhao, C, 2011
)
1.21
"Calpain is a cysteine protease that participates in normal signal transduction events, but deregulation of its action may result in pathologies such as neurological disorders, muscular dystrophies, cataract, cancer and diabetes. "( Calpain inhibitors: a survey of compounds reported in the patent and scientific literature.
Donkor, IO, 2011
)
3.25
"The calpains are a conserved family of cysteine proteinases that catalyse the controlled proteolysis of many specific substrates. "( The calpain system and cancer.
Carragher, NO; Frame, MC; Martin, SG; Parr, T; Storr, SJ, 2011
)
1.49
"Calpain is an intracellular Ca(2+)-dependent cysteine protease (EC 3.4.22.17; Clan CA, family C02) found in almost all eukaryotes."( Impact of genetic insights into calpain biology.
Hata, S; Ono, Y; Sorimachi, H, 2011
)
1.37
"Calpain 3 (CAPN3) is a muscle-specific, calcium-dependent proteinase that is mutated in Limb Girdle Muscle Dystrophy type 2A. "( Pathogenity of some limb girdle muscular dystrophy mutations can result from reduced anchorage to myofibrils and altered stability of calpain 3.
DiFranco, M; Ermolova, N; Kramerova, I; Kudryashova, E; Spencer, MJ; Vergara, J, 2011
)
2.02
"Calpain is an intracellular Ca2+-dependent cysteine protease (EC 3.4.22.17; Clan CA, family C02) discovered in 1964. "( Calpain chronicle--an enzyme family under multidisciplinary characterization.
Hata, S; Ono, Y; Sorimachi, H, 2011
)
3.25
"Calpain-3 is a skeletal muscle-specific protease and participates in the regulation of myogenesis. "( Characterization of the expression profile of calpain-3 (CAPN3) gene in chicken.
Du, HR; Jiang, XS; Liu, YP; Yao, YG; Zhang, ZR; Zhu, Q, 2012
)
2.08
"Calpain is an intracellular Ca(2+)-dependent cysteine protease (EC 3.4.22.17; Clan CA, family C02). "( Calpains: an elaborate proteolytic system.
Ono, Y; Sorimachi, H, 2012
)
3.26
"μ-Calpain is a Ca(2+)-activated protease abundant in mammalian tissues. "( μ-Calpain-mediated deregulation of cardiac, brain, and kidney NCX1 splice variants.
DeMoissac, D; Gilchrist, JS; Hnatowich, M; Hryshko, LV; Le, HD; Omelchenko, A; Ranson, K; Yurkov, V, 2012
)
1.82
"Calpains are a family of calcium-dependent proteases. "( Calpain 1 and -2 play opposite roles in cord formation of lymphatic endothelial cells via eNOS regulation.
Doki, Y; Jo, M; Koizumi, K; Park, JY; Prangsaengtong, O; Saiki, I; Sakurai, H; Senda, K; Shibahara, N, 2012
)
3.26
"Calpains are a 15-member family of Ca(2+)-activated cysteine proteases localized to the cytosol and mitochondria, and several have been shown to regulate apoptosis and necrosis."( Calpains, mitochondria, and apoptosis.
Schnellmann, RG; Smith, MA, 2012
)
2.54
"Calpain 10 is a ubiquitously expressed mitochondrial and cytosolic Ca(2+)-regulated cysteine protease in which overexpression or knockdown leads to mitochondrial dysfunction and cell death. "( Calpain 10 homology modeling with CYGAK and increased lipophilicity leads to greater potency and efficacy in cells.
Beeson, CC; Comer, RF; Lindsey, CC; McInnes, C; Schnellmann, RG; Smith, MA; Whitaker, RM, 2012
)
3.26
"Calpain is an important proteolytic enzyme in the myocardium."( Protective effects of adenosine on the diabetic myocardium against ischemia-reperfusion injury: role of calpain.
Duan, W; Jin, Z; Liu, J; Yan, J; Yang, Y; Yi, D; Zhang, J; Zhou, J, 2012
)
1.31
"Calpain is a Ca(2+)-sensitive cysteine protease that degrades intracellular substrates including cytoskeletal proteins, and participates in Ca(2+)-mediated intracellular processes."( Cooperation between proteolytic systems in cardiomyocyte recycling.
Otsu, K; Taneike, M; Yamaguchi, O, 2012
)
1.1
"Calpains are a family of complex multi-domain intracellular enzymes that share a calcium-dependent cysteine protease core. "( Structure-function relationships in calpains.
Campbell, RL; Davies, PL, 2012
)
2.1
"Calpain-1 is a nonlysosomal cysteine proteinase that modulates multiple cell functions through the selective cleavage of proteins."( Pharmacological inhibition of calpain-1 prevents red cell dehydration and reduces Gardos channel activity in a mouse model of sickle cell disease.
Bertoldi, M; Brugnara, C; Chishti, AH; De Franceschi, L; Franco, RS; Joiner, CH; Matté, A; Siciliano, A; Wieschhaus, AJ, 2013
)
1.4
"μ-Calpain is a calcium-dependent cysteine protease, which is activated by μM concentration of calcium in vitro. "( Effect of conjugated linoleic acid, μ-calpain inhibitor, on pathogenesis of Alzheimer's disease.
Baek, KH; Eom, JE; Jun, KY; Kim, HJ; Kim, HL; Kwon, Y; Lee, E; Lee, M; Mook-Jung, I, 2013
)
1.38
"The calpain system is a family of calcium activated proteases that degrade myofibrillar protein. "( The effect of early posthatch starvation on calpain mRNA levels.
Dibner, JJ; McCoy, DW; Mozdziak, PE, 2002
)
1.13
"Calpain is a Ca(2+)-dependent neutral protease which becomes activated following alterations in intracellular Ca(2+) homeostasis."( beta-Amyloid (1-40)-induced apoptosis of cultured cortical neurones involves calpain-mediated cleavage of poly-ADP-ribose polymerase.
Boland, B; Campbell, V,
)
1.08
"Calpain is a Ca(2+)-activated proteolytic enzyme involved in neurodegeneration in a variety of injuries and diseases of the central nervous system (CNS). "( Calpain and its involvement in the pathophysiology of CNS injuries and diseases: therapeutic potential of calpain inhibitors for prevention of neurodegeneration.
Banik, NL; Ray, SK, 2003
)
3.2
"Calpain is a calcium-activated protease and has two ubiquitously distributed mammalian isoforms, namely calpain 1 (calpain I, mu-calpain and CAPN1) and calpain 2 (calpain II, m-calpain and CAPN2). "( [Effect of calpain on the degradation of tau protein in rat brain cortex extracts].
Chen, ZY; Fang, ZY; Liu, R; Liu, SJ; Wang, JZ; Wang, Q; Wang, XC, 2003
)
2.15
"Calpain is a cytosolic "modulator protease" that modulates cellular functions in response to Ca2+. "( Heterogeneous nuclear ribonucleoprotein K interacts with and is proteolyzed by calpain in vivo.
Abe, K; Kimura, E; Sorimachi, H; Suzuki, K, 2003
)
1.99
"Calpains are a family of non-lysosomal cysteine proteases. "( Calpain facilitates GLUT4 vesicle translocation during insulin-stimulated glucose uptake in adipocytes.
Harmon, AW; Patel, YM; Paul, DS; Winston, CP, 2003
)
3.2
"Calpains are a family of calcium-dependent cysteine proteases under complex cellular regulation. "( The calpains in aging and aging-related diseases.
Nixon, RA, 2003
)
2.32
"p94/calpain 3 is an example of the latter, predominantly expressed in muscle."( Newly identified exons encoding novel variants of p94/calpain 3 are expressed ubiquitously and overlap the alpha-glucosidase C gene.
Abe, K; Hata, S; Ito, Y; Kawabata, Y; Ono, Y; Sorimachi, H; Suzuki, K, 2003
)
1.05
"Calpain I inhibitor is a potent antioxidant which is an effective inhibitor of NF-kappaB."( Calpain I inhibitor ameliorates the indices of disease severity in a murine model of cerulein-induced acute pancreatitis.
Cuzzocrea, S; Di Paola, R; Genovese, T; Mazzon, E; Serraino, I; Siriwardena, A; Thiemerman, C; Virlos, I, 2004
)
2.49
"Calpain3 (CAPN3, p94) is a muscle-specific nonlysosomal cysteine proteinase. "( Mutations in Czech LGMD2A patients revealed by analysis of calpain3 mRNA and their phenotypic outcome.
Chrobáková, T; Fajkusová, L; Havlová, M; Hermanová, M; Kroupová, I; Maríková, T; Mazanec, R; Stanek, J; Vondrácek, P; Zámecník, J, 2004
)
2.01
"The calpains are a family of cysteine proteases with closely related amino acid sequences, but a wide range of Ca(2+) requirements (K(d)). "( Activation of calpain by Ca2+: roles of the large subunit N-terminal and domain III-IV linker peptides.
Elce, JS; Hosfield, CM; Jia, Z, 2004
)
1.24
"Calpains are a large family of cytosolic cysteine proteases composed of at least fourteen distinct isoforms. "( [Calpains and cardiac diseases].
Perrin, C; Rochette, L; Vergely, C, 2004
)
2.68
"m-calpain is a calcium-dependent heterodimeric protease implicated in a number of pathological conditions. "( Investigations into the membrane interactions of m-calpain domain V.
Brandenburg, K; Dante, S; Dennison, SR; Harris, F; Hauss, T; Phoenix, DA, 2005
)
1.3
"Calpains are a family of 14 intracellular calcium-dependent proteases, which have been implicated in cardiovascular diseases. "( Down-regulation of calpain 9 is linked to hypertensive heart and kidney disease.
Busch, AE; Linz, W; Löhn, M; Markmann, A; Schäfer, S; Wohlfart, P, 2005
)
2.1
"Calpain is a calcium-dependent cystein protease, and the homologues of schistosome are known as one of vaccine candidate molecules against schistosomiasis. "( Establishment of Schistosoma japonicum calpain-specific mouse T cell hybridomas and identification of a T cell epitope that stimulates IFNgamma production.
Asahi, H; El-Malky, M; Hato, M; Kanazawa, T; Kumagai, T; Ohta, N; Osada, Y; Suzuki, T, 2005
)
2.04
"Calpains are a family of Ca(2+)-dependent cysteine proteases whose members are expressed ubiquitously or in a tissue-specific manner."( The expression of calpain 1 and calpain 2 in spermatogenic cells and spermatozoa of the mouse.
Ben-Aharon, I; Brown, PR; Eddy, EM; Etkovitz, N; Shalgi, R, 2005
)
1.38
"Calpain is a Ca(2+)-regulated cytosolic cysteine protease that exists mainly in two isoforms and mediates crucial cellular functions, including rearrangement of cytoskeletal proteins, transport of the glucose transporter GLUT4, and protein cleavage to activate various receptors and pro-enzymes. "( Calpain: a death protein that mediates progression of liver injury.
Limaye, PB; Mehendale, HM, 2005
)
3.21
"Calpains are a family of calcium-dependent endopeptidases, and their specific endogenous inhibitor is calpastatin."( Involvement of calpain-calpastatin in cigarette smoke-induced inhibition of lung endothelial nitric oxide synthase.
Antony, V; Block, ER; Cui, Z; Han, Z; Hu, H; Li, Z; Patel, JM; Su, Y, 2005
)
1.4
"Calpain-1 is a ubiquitous intracellular Ca2+-activated protease, which has been implicated in the pathogenesis of reversible myocardial depression (i.e. "( Calpain-1-sensitive myofibrillar proteins of the human myocardium.
Barta, J; Edes, I; Papp, JG; Papp, Z; Tóth, A; Varró, A; Vaszily, M, 2005
)
3.21
"Calpains are a family of calcium-dependent cysteine-proteases involved in cytoskeleton remodelling and muscle differentiation. "( Calpain 1-gamma filamin interaction in muscle cells: a possible in situ regulation by PKC-alpha.
Anne, M; Benyamin, Y; Carole, JN; Dieter, F; Fabrice, R; Fürst, D; Jond-Necand, C; Marcilhac, A; Raynaud, F; Yves, B, 2006
)
3.22
"Calpain is a nearly ubiquitous Ca2+-activated proteolytic enzyme whose precise physiological function is unknown. "( Molecular mode of action of a covalently inhibiting peptidomimetic on the human calpain protease core.
Hanzlik, RP; Li, Q; Schönbrunn, E; Weaver, RF, 2006
)
2
"m-Calpain is a protease implicated in the control of cell adhesion through focal adhesion disassembly. "( TRPM7 regulates cell adhesion by controlling the calcium-dependent protease calpain.
Agapito, MA; Habas, R; Huttenlocher, A; Li, M; Runnels, LW; Simonson, WT; Su, LT; Yue, L, 2006
)
1.28
"Calpain is a Ca2+-regulated cytosolic protease. "( Stomach-specific calpain, nCL-2, localizes in mucus cells and proteolyzes the beta-subunit of coatomer complex, beta-COP.
Abe, K; Doi, N; Hata, S; Kawahara, H; Koyama, S; Maeda, T; Sorimachi, H; Suzuki, K; Toyama-Sorimachi, N, 2006
)
2.12
"The calpains are a family of calcium-dependent thiol proteases involved in intracellular processing of proteins. "( Calpain 11 is unique to mouse spermatogenic cells.
Ben-Aharon, I; Brown, PR; Eddy, EM; Shalgi, R, 2006
)
2.33
"Calpains are a large family of Ca2+-dependent cysteine proteases that are ubiquitously distributed across most cell types and vertebrate species. "( Identification of calpain cleavage sites in the G1 cyclin-dependent kinase inhibitor p19(INK4d).
Ghosh, M; Gil-Parrado, S; Holak, TA; Jochum, M; Joy, J; Machleidt, W; Nalabothula, N; Popp, O, 2006
)
2.11
"p94/calpain 3 is a skeletal muscle-specific member of the Ca(2+)-regulated cytosolic cysteine protease family, the calpains. "( Suppressed disassembly of autolyzing p94/CAPN3 by N2A connectin/titin in a genetic reporter system.
Abe, K; Doi, N; Kawabata, Y; Labeit, D; Labeit, S; Maeda, T; Ojima, K; Ono, Y; Sorimachi, H; Suzuki, K; Torii, F; Yoshioka, K, 2006
)
0.89
"Calpains are a family of calcium-dependent cysteine proteases involved in a variety of cellular functions. "( Functional dissection of human protease mu-calpain in cell migration using RNAi.
Caron, A; Fan, J; Shen, SH; Whiteway, M; Wu, M; Yu, Z, 2006
)
2.04
"Calpain II is an calcium-dependent cysteine protease involved in essential regulatory or processing functions of the cell, mediated by physiological concentrations of Ca(2+). "( Altered expression, intracellular distribution and activity of lymphocyte calpain II in Duchenne muscular dystrophy.
Anandaraj, MP; Meena, AK; Mohana Rao, V; Shanmuga Sundaram, J, 2006
)
2.01
"Calpain is a class of Ca(2+)-dependent cysteine proteases and has been suggested to be involved in several important signaling cascades. "( Apoptosis induced by novel aldehyde calpain inhibitors in human tumor cell lines.
Dalton, JT; Donkor, IO; Guan, N; Hurh, E; Korukonda, R; Schmittgen, TD, 2006
)
2.05
"Calpain 3 is a 94-kDa calcium-dependent cysteine protease mainly expressed in skeletal muscle. "( Calpain 3: a key regulator of the sarcomere?
Bartoli, M; Duguez, S; Richard, I, 2006
)
3.22
"Calpain is a cytosolic cysteine endopeptidase that has been implicated in a number of disorders including cancer. "( Synthesis, calpain inhibitory activity, and cytotoxicity of P2-substituted proline and thiaproline peptidyl aldehydes and peptidyl alpha-ketoamides.
Dalton, JT; Donkor, IO; Guan, N; Korukonda, R; Liu, J, 2006
)
2.17
"Calpain (Cp) is a calcium (Ca(2+))-dependent cysteine protease. "( Subcellular mobility of the calpain/calpastatin network: an organelle transient.
Brooks, WH; Hood, JL; Roszman, TL, 2006
)
2.07
"Calpains are a family of calcium-dependent cysteine proteases involved in major cellular processes including cell death. "( Detection and localization of calpain 3-like protease in a neuronal cell line: possible regulation of apoptotic cell death through degradation of nuclear IkappaBalpha.
Benyamin, Y; Clerc, I; Marcilhac, A; Raynaud, F, 2006
)
2.07
"Mu-calpain is a myofibril-associated protease and is known to degrade TnT."( Selective deletion of the NH2-terminal variable region of cardiac troponin T in ischemia reperfusion by myofibril-associated mu-calpain cleavage.
Biesiadecki, BJ; Jin, JP; Zhang, Z, 2006
)
1.05
"The calpain family is a group of cysteine proteases unique in their dependency on calcium to attain functionally active forms. "( The therapeutic potential of the calpain family: new aspects.
Moron, FJ; Ramirez-Lorca, R; Ruiz, A; Saez, ME, 2006
)
1.17
"Calpain 3 (CAPN3) is a calcium-dependent protease, mutations in which cause limb girdle muscular dystrophy type 2A. "( Identification of putative in vivo substrates of calpain 3 by comparative proteomics of overexpressing transgenic and nontransgenic mice.
Anderson, LV; Beckmann, JS; Bushby, K; Cohen, N; Kramerova, I; Kudryashova, E; Spencer, MJ, 2006
)
2.03
"The calpains are a family of Ca(2+)-dependent cysteine proteases implicated in various biological processes. "( Calpain 6 is involved in microtubule stabilization and cytoskeletal organization.
Aburatani, H; Asano, T; Kurihara, H; Kurihara, Y; Tonami, K; Uchijima, Y, 2007
)
2.34
"p94/calpain 3 is a Ca(2+)-binding intracellular protease predominantly expressed in skeletal muscles. "( Myogenic stage, sarcomere length, and protease activity modulate localization of muscle-specific calpain.
Doi, N; Kawabata, Y; Labeit, S; Ojima, K; Ono, Y; Sorimachi, H; Yoshioka, K, 2007
)
1.12
"Calpains are a family of non-lysosomal cytoplasmatic cysteine proteases. "( Calpain inhibition impairs glycogen syntheses in HepG2 hepatoma cells without altering insulin signaling.
Drenckhan, M; Klein, HH; Kramer, J; Meier, M; Schütt, M, 2007
)
3.23
"Calpains are a super family of Ca2+ dependent proteases, which are involved in lens protein proteolysis and insolubilization."( Drevogenin D prevents selenite-induced oxidative stress and calpain activation in cultured rat lens.
Abraham, A; Biju, PG; Devi, VG; Lija, Y; Rooban, BN; Sahasranamam, V, 2007
)
1.3
"p94/calpain 3 is a skeletal muscle-specific Ca(2+)-regulated cysteine protease (calpain), and genetic loss of p94 protease activity causes muscular dystrophy (calpainopathy). "( Multiple molecular interactions implicate the connectin/titin N2A region as a modulating scaffold for p94/calpain 3 activity in skeletal muscle.
Arai, T; Doi, N; Hayashi, C; Hirner, S; Kitamura, F; Labeit, D; Labeit, S; Mineki, R; Ono, Y; Sorimachi, H; Tagami, M; Taguchi, H; Yanagida, M, 2008
)
1.12
"Calpain 2 is a calcium-dependent intracellular protease that regulates adhesion turnover and disassembly through the targeting of specific substrates such as talin."( Calpain 2 and PTP1B function in a novel pathway with Src to regulate invadopodia dynamics and breast cancer cell invasion.
Burton, NO; Chan, KT; Cortesio, CL; Huttenlocher, A; Perrin, BJ; Zhang, S; Zhang, ZY, 2008
)
2.51
"The calpains are a class of cellular cysteine proteases that require calcium and are functionally active at neutral pH. "( Calpain in the CNS: from synaptic function to neurotoxicity.
Liu, J; Liu, MC; Wang, KK, 2008
)
2.35
"Calpain-10 is a novel ubiquitous calpain family member that has been implicated as a susceptibility gene for type 2 diabetes. "( Characterization of endogenous and recombinant human calpain-10.
Dong, B; Liu, R, 2008
)
2.04
"Calpain-1 activation is a pivotal molecular event in the age-associated arterial Ang II/MMP2 signaling cascade that is linked to cytoskeleton protein restructuring, and VSMC migration. "( Increased aortic calpain-1 activity mediates age-associated angiotensin II signaling of vascular smooth muscle cells.
Jiang, L; Lakatta, EG; Monticone, RE; Pintus, G; Spinetti, G; Telljohann, R; Wang, M; Zhang, J, 2008
)
2.13
"Calpains (CANPs) are a family of calcium-dependent cysteine proteases under complex cellular regulation. "( Calcium-activated neutral proteinase (calpain) system in aging and Alzheimer's disease.
Beermann, M; Griffin, WR; Grynspan, F; Honda, T; Katayama, S; Mohan, PS; Nixon, RA; Saito, KI; Shea, TB, 1994
)
2
"Calpain is a calcium dependent cysteine protease consisting of a catalytic 80K subunit and a regulatory 30K subunit. "( Calpain dissociates into subunits in the presence of calcium ions.
Ishiura, S; Sorimachi, H; Suzuki, K; Tomioka, S; Yoshizawa, T, 1995
)
3.18
"mu-Calpain is a calcium-dependent neutral thiol protease activated by micromolar concentrations of calcium. "( 1,25-Dihydroxyvitamin D3 increases the cellular content of the calcium-activated neutral protease mu-calpain in renal cell carcinoma.
Garach-Jehoshua, O; Glaser, T; Koren, R; Liberman, UA; Ravid, A; Rotem, C, 1994
)
1.13
"Calpain I is a calcium-dependent cysteine proteinase that has been recently shown to degrade proteoglycan in vitro. "( Chemonucleolysis with calpain I in rabbits.
Nakagawa, Y; Shimizu, K; Suzuki, K; Wakita, S; Yamamoto, S; Yamamuro, T, 1993
)
2.04
"Calpain I is a heterodimeric protein that is part of a family of calcium-activated intracellular cysteine proteases presumed to play a role in mediating signals transduced by calcium. "( Biologically active monomeric and heterodimeric recombinant human calpain I produced using the baculovirus expression system.
Bihovsky, R; Bozyczko-Coyne, D; Kaywooya, JK; Lang, DM; Mallya, SK; Meyer, SL; Scott, RW; Siman, R; Spais, CM, 1996
)
1.97
"Calpain is inferred to be a calcium-dependent regulator for cytoskeletal reorganization."( Regulation of the calpain-calpastatin system by membranes (review).
Kawasaki, H; Kawashima, S,
)
1.19
"Calpains are a family of calcium-dependent thiol-proteases which are proposed to be involved in many physiological processes as well as pathological conditions. "( Calpains: intact and active?
Guttmann, RP; Johnson, GV, 1997
)
3.18
"Calpain is a ubiquitous calcium-dependent cysteine protease, whose cytoskeletal protein substrates suggest that it may be important in neuronal differentiation. "( Low levels of inorganic lead noncompetitively inhibit mu-calpain.
Audesirk, G; Audesirk, T; Kern, M; Pedersen, C, 1998
)
1.99
"Calpain is a ubiquitous neutral calcium-activated thiol protease that is implicated in various cellular functions including exocytosis, cell fusion, apoptosis and proliferation. "( Upregulation of the calcium-dependent protease, calpain, during keratinocyte differentiation.
Garach-Jehoshua, O; Glaser, T; Koren, R; Liberman, UA; Ravid, A; Reichrath, J, 1998
)
2
"Calpain 3 is a nonlysosomal cysteine protease whose biological functions remain unknown. "( Expression and functional characteristics of calpain 3 isoforms generated through tissue-specific transcriptional and posttranscriptional events.
Beckmann, JS; Beley, C; Fougerousse, F; Herasse, M; Kimura, E; Montarras, D; Ono, Y; Pinset, C; Richard, I; Sorimachi, H; Stockholm, D; Suzuki, K, 1999
)
2.01
"Calpains are a superfamily of related proteins, some of which have been shown to function as calcium-dependent cysteine proteases. "( CAPN11: A calpain with high mRNA levels in testis and located on chromosome 6.
Boehm, T; Dear, TN; Möller, A, 1999
)
2.15
"Calpains are a family of related proteins, originally classified on the basis of their calcium dependence and protease activity. "( Diverse mRNA expression patterns of the mouse calpain genes Capn5, Capn6 and Capn11 during development.
Boehm, T; Dear, TN, 1999
)
2
"Calpains are a ubiquitous, well-conserved family of calcium-dependent, cysteine proteases. "( Calpains and muscular dystrophies.
Spencer, MJ; Tidball, JG, 2000
)
3.19
"Calpain is a calcium dependent-protease and there are two isoforms, m-calpain and mu-calpain, which differ in the calcium concentration required for activation."( Molecular interactions between presenilin and calpain: inhibition of m-calpain protease activity by presenilin-1, 2 and cleavage of presenilin-1 by m-, mu-calpain.
Ishiura, S; Iwatsubo, T; Kametani, F; Maruyama, K; Mori, H; Saido, TC; Tomita, T; Usami, M, 2000
)
1.29
"m-Calpain is a heterodimeric, cytosolic, thiol protease, which is activated by Ca(2+)-binding to EF-hands in the C-terminal domains of both subunits. "( Roles of individual EF-hands in the activation of m-calpain by calcium.
Arthur, JS; Cygler, M; Dutt, P; Elce, JS; Grochulski, P, 2000
)
1.28
"Calpains are a family of Ca(2+)-dependent intracellular cysteine proteases, including the ubiquitously expressed micro- and m-calpains. "( Disruption of the murine calpain small subunit gene, Capn4: calpain is essential for embryonic development but not for cell growth and division.
Arthur, JS; Elce, JS; Greer, PA; Hegadorn, C; Williams, K, 2000
)
2.05
"If calpain autolysis is an intermolecular process, autolysis of a membrane-bound calpain would require selective participation of a second, cytosolic calpain, making it an inefficient process."( Autolysis of mu- and m-calpain from bovine skeletal muscle.
Cottin, P; Goll, DE; Sathe, SK; Szpacenko, A; Thompson, VF, 2001
)
1.14
"Calpain is a heterodimeric Ca(2+)-dependent cysteine protease consisting of a large (80 kDa) catalytic subunit and a small (28 kDa) regulatory subunit. "( Dissociation and aggregation of calpain in the presence of calcium.
Elce, JS; Jia, Z; Pal, GP, 2001
)
2.04
"Calpains are a family of related proteins, some of which have been shown to function as calcium-dependent cysteine proteases. "( Identification and characterization of two novel calpain large subunit genes.
Boehm, T; Dear, TN, 2001
)
2.01
"Calpain is a heterodimeric, intracellular Ca(2+)-dependent, "bio-modulator" that alters the properties of substrates through site-specific proteolysis. "( Dissociation of m-calpain subunits occurs after autolysis of the N-terminus of the catalytic subunit, and is not required for activation.
Masumoto, H; Nakagawa, K; Sorimachi, H; Suzuki, K, 2001
)
2.09
"Calpains are a large family of intracellular proteases whose precise and limited cleavage of specific proteins might be an integral regulatory aspect of signaling pathways. "( Cutting to the chase: calpain proteases in cell motility.
Glading, A; Lauffenburger, DA; Wells, A, 2002
)
2.07
"Calpain is a ubiquitous protease with potential involvement in apoptosis. "( Calpain-mediated Bid cleavage and calpain-independent Bak modulation: two separate pathways in cisplatin-induced apoptosis.
Hansson, J; Heiden, T; Linder, S; Mandic, A; Shoshan, MC; Strandberg, L; Viktorsson, K, 2002
)
3.2
"Calpain 10 is a member of a large family of intracellular proteases."( Homozygous combination of calpain 10 gene haplotypes is associated with type 2 diabetes mellitus in a Polish population.
Cyganek, K; Frey, J; Klupa, T; Malecki, MT; Moczulski, DK; Sieradzki, J; Wanic, K, 2002
)
1.34
"The calpains are a family of calcium-dependent proteases that play important roles in proteolysis of some proteins, and their possible participation in degradation of intracellular c-Myc was therefore investigated."( Evidence for involvement of calpain in c-Myc proteolysis in vivo.
Chou, TY; Dang, CV; Orlowski, RZ; Small, GW, 2002
)
1.09
"Calpain is a calcium-activated non lysosomal neutral thiol protease (EC 3.4.22.17) present in a wide variety of eukaryotic cells. "( Calpain function in the differentiation of mesenchymal stem cells.
Kawashima, S; Yajima, Y, 2002
)
3.2
"The calpain gene is a TPA-responsive gene and its expression is stimulated by activation of PKC."( Modulation of cellular signals by calpain.
Hirai, S; Saido, TC; Suzuki, K, 1992
)
1.04
"Calpain is a Ca2(+)-dependent cysteine proteinase that has neutral pH optima. "( Immunohistochemical and biochemical demonstration of calcium-dependent cysteine proteinase (calpain) in calcifying cartilage of rats.
Hamakubo, T; Hamamoto, T; Lee, WJ; Murachi, T; Nakagawa, Y; Shimizu, K; Suzuki, K; Yamamuro, T, 1991
)
1.94
"Calpain is a Ca2(+)-dependent cysteine endopeptidase and calpastatin is a calpain-specific endogenous inhibitor protein. "( [Calpain and calpastatin].
Murachi, T, 1990
)
2.63
"Calpain is a calcium-activated neutral protease that degrades a number of cytoskeletal proteins. "( Distribution of calcium-activated protease calpain in the rat brain.
Baudry, M; Gall, C; Lynch, G; Perlmutter, LS, 1990
)
1.98
"Calpain is a calcium-activated protease which has been implicated in degenerative phenomena in muscles and in peripheral nerves."( Lesions of entorhinal cortex produce a calpain-mediated degradation of brain spectrin in dentate gyrus. I. Biochemical studies.
Baudry, M; Ivy, G; Larson, J; Lee, J; Lynch, G; Seubert, P; Shahi, K, 1988
)
1.27

Effects

The calpain family has a well-established causal role in neuronal cell death following acute brain injury. Calpain activation has a putative role in ischaemia-reperfusion injury of cardiomyocytes. Cal pain has a degradative effect on proteoglycans, and is associated with chemonucleolytic action in the rabbit.

Calpain proteases have been implicated in cell death by necrosis and more recently by apoptosis. Calpains have been proposed to be activated following cardiac ischaemia and to contribute to myocyte damage after myocardial infarction (MI)

ExcerptReferenceRelevance
"Calpain activation has a putative role in ischaemia-reperfusion injury of cardiomyocytes. "( Contribution of calpain to myoglobin efflux from cardiomyocytes during ischaemia and after reperfusion in anaesthetized rats.
Akiyama, T; Du, CK; Shirai, M; Sonobe, T; Zhan, DY, 2014
)
2.19
"The calpain family has a well-established causal role in neuronal cell death following acute brain injury: their activation has been observed to progressively increase after either contusive or diffuse brain trauma in animals, suggesting calpain to be a mediator of early neuronal damage."( Introduction of calpain inhibitors in traumatic brain injury: a novel approach?
Bralic, M; Stemberga, V; Stifter, S, 2012
)
1.21
"Calpain has a degradative effect on proteoglycans, and as previously shown, it is associated with chemonucleolytic action in the rabbit. "( Calpain inhibition by cerebrospinal fluid and effects of calpain on intrathecal nerve tissue.
Akaike, A; Banno, Y; Kodama, H; Nonomura, Y; Oshita, H; Shimizu, K, 2002
)
3.2
"Calpains have been implicated in heart diseases. "( Sustained over-expression of calpain-2 induces age-dependent dilated cardiomyopathy in mice through aberrant autophagy.
Chakrabarti, S; Fan, GC; Hinton, A; Ji, XY; Ni, R; Peng, TQ; Shao, JQ; Song, LS; Su, ZL; Vue, Z; Wang, JX; Zheng, D, 2022
)
2.46
"Calpain activation has been implicated in various pathologies, including neurodegeneration. "( Selective Calpain Inhibition Improves Functional and Histopathological Outcomes in a Canine Spinal Cord Injury Model.
Ahmed, EA; Ahmed, MF; Al-Abbadi, HA; Hashem, MA; Helal, IE; Maaty, AI; Mahmoud, YK; Metwally, E, 2022
)
2.57
"Calpain 2 (CAPN2) has been suggested as a tumor marker linked to angiogenesis, cell proliferation, and migration in non-small cell lung cancer."( Noninvasive Early Detection of Calpain 2-Enriched Non-Small Cell Lung Cancer Using a Human Serum Albumin-Bounded Calpain 2 Nanosensor.
Choi, JH; Higaki, T; Kim, MW; Kwon, SH; Lee, G; Lee, R; Park, YI; Wi, T, 2020
)
1.57
"Calpain 1 (CAPN1) has been found to be a promoter of cancer progression. "( CAPN1 promotes malignant behavior and erlotinib resistance mediated by phosphorylation of c-Met and PIK3R2 via degrading PTPN1 in lung adenocarcinoma.
Chen, Y; Liu, F; Lu, T; Tang, J, 2020
)
2
"Calpain inhibition has been shown to reduce organ damage in various disease models."( Targeted inhibition of endothelial calpain delays wound healing by reducing inflammation and angiogenesis.
Huang, H; Peng, G; Shen, Z; Teng, X; Wu, W; Yi, C; Zheng, D, 2020
)
1.56
"Calpain inhibitors have been proposed as drug candidates for neurodegenerative disorders, with ABT-957 entering clinical trials for Alzheimer's disease and mild cognitive impairment. "( Synthesis of α-Ketoamide-Based Stereoselective Calpain-1 Inhibitors as Neuroprotective Agents.
Gaisina, IN; Jastaniah, A; Knopp, RC; Thatcher, GRJ, 2020
)
2.26
"Calpain has been proposed to play a critical role in the development of epilepsy. "( Calpain-2 activation in mouse hippocampus plays a critical role in seizure-induced neuropathology.
Baudry, M; Bi, X; Liu, Y; Quach, D; Wang, Y; Yahya, E, 2021
)
3.51
"Calpains have been shown to be involved in several physiological processes such as cell motility, proliferation, cell cycle, signal transduction, and apoptosis."( Redox-Dependent Calpain Signaling in Airway and Pulmonary Vascular Remodeling in COPD.
Kovacs, L; Su, Y, 2017
)
1.52
"Calpain expression has been shown to be increased in human malignant cells, but the contribution of the calpain/calpastatin system in tumorigenesis remains unclear."( The calpain/calpastatin system has opposing roles in growth and metastatic dissemination of melanoma.
Baud, L; Hanouna, G; Haymann, JP; Letavernier, E; Perez, J; Prignon, A; Raimbourg, Q; Vandermeersch, S, 2013
)
1.67
"Calpain proteases have been linked with tissue atrophy following ischaemia-reperfusion injury."( A randomised controlled trial of supervised exercise regimens and their impact on walking performance, skeletal muscle mass and calpain activity in patients with intermittent claudication.
Chataway, TK; Delaney, CL; Miller, MD; Spark, JI, 2014
)
1.33
"Calpain activity has been implicated in several cellular processes such as cell signaling, apoptosis, exocytosis, mitochondrial metabolism and cytoskeletal remodeling. "( Role of calpain-10 in the development of diabetes mellitus and its complications.
Burns, AL; Ostrosky-Wegman, P; Pánico, P; Salazar, AM, 2014
)
2.28
"Calpain has been associated with the pathophysiology of Alzheimer's disease (AD) and with apoptotic neuronal cell death leading to microparticles (MPs) formation."( Increased cerebrospinal fluid calpain activity and microparticle levels in Alzheimer's disease.
Fleming, I; Kempter, I; Laske, C; Maetzler, W; Randriamboavonjy, V; Stellos, K; Stransky, E, 2015
)
2.15
"Calpain has been implicated in the apparent expansion of neutrophil plasma membrane that accompanies cell spreading and phagocytosis. "( Active calpain in phagocytically competent human neutrophils: electroinjection of fluorogenic calpain substrate.
Campbell, JS; Hallett, MB, 2015
)
2.31
"Calpains have been implicated in some aspects of myogenesis in mammals, but whether they exert a conserved function during myoblast fusion has not been investigated."( A conserved role for calpains during myoblast fusion.
Araujo, H; Batista Possidonio, AC; Buffolo, M; Mermelstein, C, 2015
)
1.46
"Calpain has been shown to be involved in neurodegeneration, and in particular in retinal ganglion cell (RGC) death resulting from increased intraocular pressure (IOP) and ischemia. "( Calpain-1 and calpain-2 play opposite roles in retinal ganglion cell degeneration induced by retinal ischemia/reperfusion injury.
Baudry, M; Bi, X; Cameron, DJ; Davey, PG; Liu, Y; Lopez, D; Marquez, E; Nguyen, K; Tran, J; Wang, Y, 2016
)
3.32
"Calpains have been found to be involved in apoptosis of many cell systems."( Z-LLY-FMK can attenuate hepatocyte apoptosis after bile duct ligation in rat.
Eng, HL; Ho, HT; Hung, KS; Sheen-Chen, SM, 2008
)
1.07
"Calpains have been linked to the modulation of memory and are key to the pathogenesis of Alzheimer disease (AD)."( Inhibition of calpains improves memory and synaptic transmission in a mouse model of Alzheimer disease.
Arancio, O; Fa', M; Hidalgo, A; Liu, S; Mathews, PM; Nixon, RA; Schmidt, SD; Trinchese, F; Yamaguchi, H; Yoshii, N; Zhang, H, 2008
)
1.43
"Calpains have been implicated in the regulation of apoptosis. "( Calpain5 expression is decreased in endometriosis and regulated by HOXA10 in human endometrial cells.
Du, H; Ferriani, R; Penna, I; Taylor, HS, 2008
)
3.23
"Calpain-like proteins have been reported after in silico analysis of the Tritryps genome and are believed to play important roles in cell functions of trypanosomatids."( Trypanosoma cruzi: a stage-specific calpain-like protein is induced after various kinds of stress.
Dallagiovanna, B; Giese, V; Goldenberg, S; Krieger, MA; Marchini, FK; Pavoni, DP, 2008
)
1.34
"Calpain 10 has been localized to the mitochondria and is a key mediator of Ca(2+) induced mitochondrial dysfunction. "( Identification and optimization of a novel inhibitor of mitochondrial calpain 10.
Arrington, DD; Beeson, CC; Giguere, C; Odejinmi, S; Rasbach, KA; Schnellmann, RG, 2009
)
2.03
"Calpains have been detected in several studies during the embryonic and foetal stages."( Expression of typical calpains in mouse molar.
Matsunaga, T; Tachikawa, T; Yamamoto, G, 2009
)
1.39
"Calpain has been implicated in many inflammatory and neurodegenerative events that lead to disability in EAE and MS."( Calpeptin attenuated inflammation, cell death, and axonal damage in animal model of multiple sclerosis.
Banik, NL; Butler, JT; Das, A; Guyton, MK; Ray, SK; Samantaray, S; Wallace, GC, 2010
)
1.08
"Calpains have been implicated in many pathologies including muscular dystrophies, cancer, diabetes, Alzheimer's disease and multiple sclerosis."( Measuring calpain activity in fixed and living cells by flow cytometry.
Berger, S; Farr, C, 2010
)
1.48
"Calpain activation has been implicated in the disease pathology of Duchenne muscular dystrophy. "( Leupeptin-based inhibitors do not improve the mdx phenotype.
Acosta, P; Barton, E; Carver, T; Pendrak, K; Pham, J; Selsby, J; Sweeney, HL; Tian, Z; Zadel, M, 2010
)
1.8
"Calpains have been shown to be over-activated in alveolar rhabdomyosarcoma (ARMS)."( Investigation of peroxiredoxin IV as a calpain-regulated pathway in cancer.
Cottin, P; Dargelos, E; Gonthier-Maurin, L; Pires-Alves, A; Roumes, H, 2010
)
1.35
"Calpains have been implicated in both physiological and pathological cell death control, especially in various malignancies, but also in the immune system development and function."( Conventional calpains and programmed cell death.
Witkowski, JM; Łopatniuk, P, 2011
)
1.46
"Calpain inhibition has been shown to protect axons in rodent models of traumatic brain injury."( Short-duration treatment with the calpain inhibitor MDL-28170 does not protect axonal transport in an in vivo model of traumatic axonal injury.
Bull, DL; Li, L; Ma, M; Meaney, DF; Neumar, RW; Shofer, FS; Wang, X, 2012
)
1.38
"Calpain has been considered to be the most important protease involved in tenderization during the conversion of muscle into meat. "( Effects of inhibitors on the synergistic interaction between calpain and caspase-3 during post-mortem aging of chicken meat.
Chen, L; Feng, XC; Xu, XL; Zhang, WG; Zhou, GH, 2012
)
2.06
"Calpain has been implicated in acute myocardial injury after myocardial infarction (MI). "( Deficiency of Capn4 gene inhibits nuclear factor-κB (NF-κB) protein signaling/inflammation and reduces remodeling after myocardial infarction.
Fan, GC; Greer, PA; Karmazyn, M; Lacefield, JC; Li, J; Liu, W; Ma, J; Peng, T; Wang, H; Wang, Q; Wei, M, 2012
)
1.82
"Calpains have been shown to be involved in a number of physiological processes such as cell cycle progression, remodeling of cytoskeletal-cell membrane attachments, signal transduction, gene expression and apoptosis."( Implications of calpains in health and diseases.
Alam, MN; Chakraborti, S; Chakraborti, T; Paik, D; Shaikh, S, 2012
)
1.45
"The calpain system has been implicated in tumour progression and response to various anti-cancer therapies, and therefore expression of the system was determined in this tumour type."( Expression of the calpain system is associated with poor clinical outcome in gastro-oesophageal adenocarcinomas.
Davis, J; Lobo, D; Madhusudan, S; Martin, SG; Parsons, SL; Pu, X; Reece-Smith, AM; Storr, SJ, 2013
)
1.2
"The calpain protease has been shown to cleave p35."( Influence of phosphorylation of p35, an activator of cyclin-dependent kinase 5 (cdk5), on the proteolysis of p35.
Kerokoski, P; Pirttilä, T; Salminen, A; Soininen, H; Suuronen, T, 2002
)
0.8
"Many calpain homologs have been discovered."( Calpain and its involvement in the pathophysiology of CNS injuries and diseases: therapeutic potential of calpain inhibitors for prevention of neurodegeneration.
Banik, NL; Ray, SK, 2003
)
2.22
"Calpain activation has been implicated in various aging phenomena and diseases of late life, including cataract formation, erythrocyte senescence, diabetes mellitus type 2, hypertension, arthritis, and neurodegenerative disorders."( The calpains in aging and aging-related diseases.
Nixon, RA, 2003
)
1.6
"Calpain has been implicated in the pathophysiology of neurodegenerative diseases."( Immunofluorescent labeling of increased calpain expression and neuronal death in the spinal cord of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-treated mice.
Ali, SF; Banik, NL; Chera, B; Imam, SZ; Ray, SK; Rocchini, A; Schaecher, KE; Sribnick, EA, 2004
)
1.31
"Calpain activities have been shown to be increased in hearts experimentally subjected to ischemia reperfusion or during hypertrophy, but also in atrial tissue harvested from patients suffering from atrial fibrillations."( [Calpains and cardiac diseases].
Perrin, C; Rochette, L; Vergely, C, 2004
)
1.96
"Calpain has been implicated in excitotoxic neurode-generation, but its mechanism of action particularly in adult brains remains unclear. "( Calpain mediates excitotoxic DNA fragmentation via mitochondrial pathways in adult brains: evidence from calpastatin mutant mice.
Higuchi, M; Itohara, S; Iwata, N; Maki, M; Saido, TC; Takano, J; Tomioka, M; Tsubuki, S, 2005
)
3.21
"Calpain activation has been implicated in the development of ischemia-reperfusion (I-R) injury. "( Inhibitors of calpain activation (PD150606 and E-64) and renal ischemia-reperfusion injury.
Brown, PA; Chatterjee, PK; Cuzzocrea, S; Mazzon, E; Mota-Filipe, H; Sivarajah, A; Stewart, KN; Thiemermann, C; Todorovic, Z, 2005
)
2.13
"Calpain has been demonstrated to mediate specific Ca(2+)-dependent processes including cell fusion, mitosis and meiosis."( The expression of calpain 1 and calpain 2 in spermatogenic cells and spermatozoa of the mouse.
Ben-Aharon, I; Brown, PR; Eddy, EM; Etkovitz, N; Shalgi, R, 2005
)
1.38
"Calpain activation has been implicated in the pathogenesis of Alzheimer's disease. "( Calpain activation in okadaic-acid-induced neurodegeneration.
Choi, J; Huh, JW; Hwang, O; Kim, D; Yoon, S, 2006
)
3.22
"Calpain 3 has been shown to proteolytically cleave a wide variety of cytoskeletal and myofibrillar proteins and to act upstream of the ubiquitin-proteasome pathway."( Molecular and cellular basis of calpainopathy (limb girdle muscular dystrophy type 2A).
Beckmann, JS; Kramerova, I; Spencer, MJ, 2007
)
1.34
"Calpain-10 (CAPN10) has been identified as a diabetes susceptibility gene. "( Calpain facilitates actin reorganization during glucose-stimulated insulin secretion.
Aganna, E; Clark, A; Fulcher, FK; Hitman, GA; Jones, CV; Partridge, CJ; Patel, YM; Smith, BT; Turner, MD, 2007
)
3.23
"Calpains have been implicated in multiple models of human disease; for instance, calpain 1 is activated in the brains of individuals with Alzheimer's disease, and the digestive tract specific calpain 9 is down-regulated in gastric cancer cell lines."( The crystal structures of human calpains 1 and 9 imply diverse mechanisms of action and auto-inhibition.
Davis, TL; Dhe-Paganon, S; Finerty, PJ; Mackenzie, F; Newman, EM; Walker, JR, 2007
)
1.34
"Calpains have been proposed to be involved in the cytoskeletal remodeling and wasting of skeletal muscle. "( Differential localization of autolyzed calpains 1 and 2 in slow and fast skeletal muscles in the early phase of atrophy.
Astier, C; Cazorla, O; Lacampagne, A; Mercier, J; Raynaud, F; Sirvent, P; Vermaelen, M, 2007
)
2.05
"Calpain-10 (CAPN10) has been identified as a susceptibility gene in type 2 diabetes mellitus (T2DM) and insulin resistance. "( Variations in the calpain-10 gene are associated with the risk of type 2 diabetes and hypertension in northern Han Chinese population.
Chen, SF; Gu, DF; Huang, JF; Lu, XF; Yan, WL, 2007
)
2.12
"Calpain activity has been implicated in various aging phenomena, including cataract formation and erythrocyte senescence."( Calcium-activated neutral proteinase (calpain) system in aging and Alzheimer's disease.
Beermann, M; Griffin, WR; Grynspan, F; Honda, T; Katayama, S; Mohan, PS; Nixon, RA; Saito, KI; Shea, TB, 1994
)
1.28
"Calpain has been identified as the intracellular proteinase that catalyzes the selective down-regulation of protein kinase C (PKC) isoforms, occurring in the early stages of commitment to terminal erythroid differentiation of murine erythroleukemia (MEL) cells induced by hexamethylenebisacetamide. "( Modulation of the intracellular Ca(2+)-dependent proteolytic system is critically correlated with the kinetics of differentiation of murine erythroleukemia cells.
Melloni, E; Passalacqua, M; Patrone, M; Pessino, A; Pontremoli, S; Sparatore, B, 1994
)
1.73
"Calpains have been previously shown to regulate AMPA receptor properties by producing partial truncation of the C-terminal domains of several receptor subunits. "( Calpain-mediated regulation of NMDA receptor structure and function.
Baudry, M; Bi, X; Chen, J; Dang, S; Rong, Y; Wang, Z, 1998
)
3.19
"Calpain test has been informative in a large group of patients and carriers tested so far."( Deletion analysis & calpain status for carrier detection in a family with Duchenne muscular dystrophy.
Anandaraj, MP; Devi, NG; Hussain, T; Kumari, CK, 1998
)
1.34
"Calpain proteases have been implicated in cell death by necrosis and more recently by apoptosis. "( Calpain mediates ischemic injury of the liver through modulation of apoptosis and necrosis.
Bentley, RC; Clavien, PA; Kohli, V; Madden, JF, 1999
)
3.19
"Calpains have been identified in the cochlea and are active during ischemic injury."( Calpain inhibitors protect auditory sensory cells from hypoxia and neurotrophin-withdrawal induced apoptosis.
Cheng, AG; Huang, T; Kim, A; Lefebvre, PP; Liu, W; Malgrange, B; Schulman, A; Stracher, A; Van de Water, TR, 1999
)
2.47
"Calpain isoforms also have been found in nuclear, cytosolic, and plasma membrane-associated compartments in a variety of cell types."( Membrane proximal ERK signaling is required for M-calpain activation downstream of epidermal growth factor receptor signaling.
Glading, A; Keyse, SM; Lauffenburger, DA; Uberall, F; Wells, A, 2001
)
1.29
"Calpains have been implicated in basic cellular processes including cell proliferation, apoptosis and differentiation."( Calpain.
Huttenlocher, A; Perrin, BJ, 2002
)
2.48
"The calpains have been proposed to be activated following cardiac ischaemia and to contribute to myocyte damage after myocardial infarction (MI)."( Activity profile of calpains I and II in chronically infarcted rat myocardium--influence of the calpain inhibitor CAL 9961.
Prenzel, F; Sandmann, S; Schauer, R; Shaw, L; Unger, T, 2002
)
1.12
"Calpain has been implicated in the differentiation of myoblasts through the turnover of glycoproteins."( Calpain function in the differentiation of mesenchymal stem cells.
Kawashima, S; Yajima, Y, 2002
)
2.48
"Calpain activity has been associated with cleavages that alter regulation of various enzyme activities, with remodeling or disassembly of the cell cytoskeleton, and with cleavages of hormone receptors."( Is calpain activity regulated by membranes and autolysis or by calcium and calpastatin?
Goll, DE; Taylor, RG; Thompson, VF; Zalewska, T, 1992
)
1.63
"Calpains have been implicated previously as the protease responsible for the observed necrosis in dystrophin-deficient human muscle."( Calpain concentration is elevated although net calcium-dependent proteolysis is suppressed in dystrophin-deficient muscle.
Spencer, MJ; Tidball, JG, 1992
)
2.45
"Calpains have been reported to appear in myoblasts at around the time of fusion."( [Calpains, protein kinase c and development of muscle tissue].
Belamri, M; Ducastaing, A; Pallet, V; Savart, M, 1988
)
1.91

Actions

Calpain plays dual roles of facilitating CVB3 replication and inflammation promotion. Calpain plays a critical role in cardiomyopathic changes in type 1 diabetes (T1D) Calpain 10 plays a role in insulin secretion, action and susceptibility to type 2 diabetes.

ExcerptReferenceRelevance
"Calpain plays a significant role in the cleavage and aggregation of toxic α-synuclein (α-syn), a presynaptic neural protein, and other organelles, contributing to mitochondrial dysfunction and oxidative stress."( Calpain activation and progression of inflammatory cycles in Parkinson's disease.
Banik, NL; Gao, A; Haque, A; McCoy, HM; Shields, DC; Zaman, V, 2022
)
2.89
"Calpains activate during myocardial ischemia-reperfusion and contribute to reperfusion injury. "( Delayed, oral pharmacological inhibition of calpains attenuates adverse post-infarction remodelling.
Aluja, D; Garcia-Dorado, D; Hernando, V; Inserte, J; Poncelas, M; Vilardosa, U, 2017
)
2.16
"Calpain 10 plays a role in insulin secretion, action and susceptibility to type 2 diabetes. "( Molecular signatures of Calpain 10 isoforms sequences, envisage functional similarity and therapeutic potential.
Chaudhry, B; Hanif, F; Saboohi, K, 2019
)
2.26
"Calpain-p25-mediated increase in cdk5 expression leading to dopaminergic neuronal death has been demonstrated in human PD and MPTP-PD models."( Downregulation of miR-124 in MPTP-treated mouse model of Parkinson's disease and MPP iodide-treated MN9D cells modulates the expression of the calpain/cdk5 pathway proteins.
Beiping, H; Dheen, ST; Kanagaraj, N; Tay, SS, 2014
)
1.32
"Calpain activity was lower in the HT + αT group than in HT and Control + αT and superoxide dismutase (SOD) activity was higher in the HT + αT group than in the Control + αT."( Reactive oxygen species play a role in muscle wasting during thyrotoxicosis.
Armani, A; Bernardes, SS; Cecchini, AL; Cecchini, R; Guarnier, FA; Marinello, PC; Simão, AN, 2014
)
1.12
"Calpain plays a critical role in causing neurodegenerative diseases."( Calpain Inhibition Improves Erectile Function in a Rat Model of Cavernous Nerve Injury.
Chen, L; Guo, YL; Li, GH; Li, WZ; Wan, ZH, 2015
)
2.58
"Calpain plays an important role in the pathophysiology of neurological and cardiovascular complications, but its functional association in diabetic neuropathy is not yet elucidated. "( Calpain inhibitor, MDL 28170 confer electrophysiological, nociceptive and biochemical improvement in diabetic neuropathy.
Kharatmal, SB; Sharma, SS; Singh, JN, 2015
)
3.3
"Calpain plays an important role in myocardial ischemia/reperfusion (I/R) injury. "( PD150606 protects against ischemia/reperfusion injury by preventing μ-calpain-induced mitochondrial apoptosis.
Hu, H; Li, K; Luo, T; Xu, L; Yiu, KH; Yu, Z; Yue, R; Zhang, S; Zhou, Z, 2015
)
2.09
"Calpain plays a critical role in cardiomyopathic changes in type 1 diabetes (T1D). "( Mitochondrial Calpain-1 Disrupts ATP Synthase and Induces Superoxide Generation in Type 1 Diabetic Hearts: A Novel Mechanism Contributing to Diabetic Cardiomyopathy.
Abel, ED; Fan, GC; Gardiner, RB; Greer, PA; Hill, DJ; Lu, Y; Ni, R; Peng, T; Sun, T; Xiong, S; Zheng, D, 2016
)
2.24
"Calpain plays dual roles of facilitating CVB3 replication and inflammation promotion. "( Dual roles of calpain in facilitating Coxsackievirus B3 replication and prompting inflammation in acute myocarditis.
Chen, R; Ge, J; Li, M; Su, Y; Wang, X; Yu, Y; Zou, Y, 2016
)
2.24
"Calpain 3 plays different roles in muscular cells, but little is known about its functions or in vivo substrates."( Gene expression profiling in limb-girdle muscular dystrophy 2A.
Alzualde, A; Armañanzas, R; Azpitarte, M; Cabello, A; Corcuera, J; De la Herran, G; De la Torre, C; Gallardo, E; García-Bragado, F; Illa, I; Inza, I; Leturcq, F; López de Munain, A; Navarro, C; Sáenz, A, 2008
)
1.07
"Calpain A knockdowns increase Cactus levels, shifting the Dorsal gradient and dorsal-ventral patterning."( The Ca2+-dependent protease Calpain A regulates Cactus/I kappaB levels during Drosophila development in response to maternal Dpp signals.
Agrellos, R; Araujo, H; Carneiro, K; Fontenele, M; Machado, E; Negreiros, E; Oliveira, D; Oliveira-Silva, A; Vieira, V,
)
1.15
"The calpain system plays an important role in many processes including apoptosis, necrosis, ischaemia and exocytosis."( Immunhistochemical analysis for expression of calpain 1, calpain 2 and calpastatin in endometrial cancer.
Bauerschlag, D; Bohle, RM; Dohmen, B; Friedrich, M; Fromberg, I; Georg, T; Haugk, C; Maass, N; Salehin, D, 2010
)
1.1
"m-Calpain plays a critical role in cell migration enabling rear de-adhesion of adherent cells by cleaving structural components of the adhesion plaques. "( m-Calpain activation is regulated by its membrane localization and by its binding to phosphatidylinositol 4,5-bisphosphate.
Bae, YH; Deasy, B; Leloup, L; Roy, P; Shao, H; Stolz, D; Wells, A, 2010
)
1.8
"The calpain system plays an important role in many processes including apoptosis, necrosis, ischemia formation and exocytosis."( Immunhistochemical analysis for expression of calpain 1, calpain 2 and calpastatin in ovarian cancer.
Bauerschlag, D; Bohle, RM; Dohmen, B; Friedrich, M; Fromberg, I; Georg, T; Haugk, C; Salehin, D; Thill, M, 2011
)
1.11
"The calpains activity increase in the lungs, heart, liver and kidneys was revealed after 2 h cobalt chloride action."( [Activity of Ca(2+)-dependent neutral proteinases in rat organs under cobalt and mercury chloride injection].
Kaliman, PA; Samokhin, AA; Samokhina, LM,
)
0.61
"Calpain activity was lower in two different areas tested, 29% in the medulla oblongata and 26% in the lateral prefrontal cortex, and was 18% higher in the midbrain."( Alteration of protease levels in different brain areas of suicide victims.
Banay-Schwartz, M; DeGuzman, T; Faludi, G; Lajtha, A; Palkovits, M, 1998
)
1.02
"Calpain seems to produce neuronal damage by degrading neuronal cytoskeleton."( Calpain inhibitor entrapped in liposome rescues ischemic neuronal damage.
Hori, S; Nakagaki, I; Saido, TC; Tani, E; Tsubuki, S; Yamaura, I; Yokota, M, 1999
)
2.47

Treatment

Calpain I treatment of recombinant dicer or immunopurified brain dicer caused a marked increase in RNAse III activity. Calpain treatment weakens the PR72-core enzyme interaction, activates basal PP2A(T72) phosphatase activity and dramatically increases its sensitivity for and activation by polycations.

ExcerptReferenceRelevance
"Calpain inhibitor-1 treatment normalized the loss rate of surface NMDARs in YAC128 MSNs to that of wild type, and significantly increased surface NMDAR expression in YAC128, but not in wild type or YAC72."( Polyglutamine-modulated striatal calpain activity in YAC transgenic huntington disease mouse model: impact on NMDA receptor function and toxicity.
Cowan, CM; Fan, J; Fan, MM; Graham, RK; Hayden, MR; Raymond, LA; Shehadeh, J; Zhang, LY, 2008
)
1.35
"Mild calpain treatment of myofibrils released filaments that had a polypeptide composition and were ultrastructurally similar to ERMs."( Properties of easily releasable myofilaments: are they the first step in myofibrillar protein turnover?
Goll, DE; Neti, G; Novak, SM; Thompson, VF, 2009
)
0.81
"Calpain treatment weakens the PR72-core enzyme interaction, activates basal PP2A(T72) phosphatase activity and dramatically increases its sensitivity for and activation by polycations."( Specific regulation of protein phosphatase 2A PR72/B'' subunits by calpain.
Derua, R; Goris, J; Janssens, V; Waelkens, E; Zwaenepoel, K, 2009
)
1.31
"Calpain I treatment of recombinant dicer or immunopurified brain dicer caused a marked increase in RNAse III activity."( Dicer and eIF2c are enriched at postsynaptic densities in adult mouse brain and are modified by neuronal activity in a calpain-dependent manner.
Jones, Y; Larson, J; Lugli, G; Martone, ME; Smalheiser, NR, 2005
)
1.26
"Mu-calpain treatment of the cardiac myofibril and troponin complex specifically reproduced cTnT-ND."( Selective deletion of the NH2-terminal variable region of cardiac troponin T in ischemia reperfusion by myofibril-associated mu-calpain cleavage.
Biesiadecki, BJ; Jin, JP; Zhang, Z, 2006
)
1.05
"Calpain treatment had the reverse effect."( Activation of TGF-beta within cultured hepatocytes and in liver injury leads to intracrine signaling with expression of connective tissue growth factor.
Gressner, AM; Gressner, OA; Herrmann, J; Lahme, B; Rehbein, K; Siluschek, M; Weiskirchen, R, 2008
)
1.07
"Calpain treatment in vitro caused a large decrease in the activity of carnosine synthetase which is involved in the synthesis of the putative antioxidant carnosine."( Effects of calpain on antioxidant enzyme activities.
Hammer, JL; Johnson, P, 1994
)
1.4
"Calpain treatment of synaptic membranes resulted in a large decrease in the GluR1 band (105 kDa) labeled with C-Ab and in the formation of a doublet band labeled with N-Ab due to the appearance of a new species of GluR1 (98 kDa)."( Characterization of calpain-mediated proteolysis of GluR1 subunits of alpha-amino-3-hydroxy-5-methylisoxazole-4-propionate receptors in rat brain.
Baudry, M; Bi, X; Chen, J; Dang, S; Tocco, G; Wenthold, RJ, 1997
)
1.34
"Calpain treatment potentiated the activity of guanosine 5'-[gamma-thio]triphosphate (GTP[S]), but did not attenuate MnCl(2) action on adenylate cyclase, suggesting that calpain acted at the G-protein level, rather than directly on adenylate cyclase."( Persistent activation of Gsalpha through limited proteolysis by calpain.
Kawashima, S; Sato-Kusubata, K; Yajima, Y, 2000
)
1.27
"Calpain treatment of rabbit skinned muscle fibers resulted in proteolysis of junctional foot protein or Ca2+ release channel of the sarcoplasmic reticulum. "( Enhancement of Ca2+-induced Ca2+ release in calpain treated rabbit skinned muscle fibers.
Endo, M; Iino, M; Kawana, Y; Takano-Ohmuro, H, 1992
)
1.99
"In calpain-treated membrane, the 240 and 36 kDa bands were retained in the blotting, though the other bands disappeared dose-dependently with respect to calpain."( Characterization of calpain I-binding proteins in human erythrocyte plasma membrane.
Ishii, H; Kazama, M; Kuboki, M, 1990
)
1.12
"Treatment with calpain inhibitors reduced TUG cleavage, resulting in impaired GLUT4 translocation without altering Akt phosphorylation."( TUG is a calpain-10 substrate involved in the translocation of GLUT4 in adipocytes.
Hiriart, M; Ostrosky-Wegman, P; Pánico, P; Salazar, AM, 2020
)
1.31
"Treatment with calpain inhibitor III specifically inhibited calpain-1/-2 activities, mitigated the degree of proteinuria and glomerulosclerosis, and led to a striking increase in survival in the Gak-KO mice."( Inhibiting calpain 1 and 2 in cyclin G associated kinase-knockout mice mitigates podocyte injury.
Ebenezer, K; Greene, L; Greer, P; Groener, M; Inoue, K; Ishibe, S; Li, W; Liebermann, DA; Moledina, DG; Parikh, CR; Pedigo, CE; Sperati, CJ; Tian, X; Wang, Y; Yan, M; Zhang, Y; Zhang, Z; Zhao, T, 2020
)
1.29
"Co-treatment with calpain inhibitor ALLN and EEPM had a synergistic effect on neuronal death and contributed to blockade of activation of both ERK and p38 with increased activation of CREB."( Neuroprotective effects of Polygonum multiflorum extract against glutamate-induced oxidative toxicity in HT22 hippocampal cells.
Baek, JU; Choi, BT; Choi, YH; Choi, YW; Hong, JW; Jang, JY; Kim, HN; Kim, YR; Shin, HK, 2013
)
0.71
"Treatment with calpain inhibitors also ameliorated cachexia-associated negative effects in metabolic profiles and increased survival time in most of the tumor-bearing mice compared with the cachexia controls."( Calpain inhibitors ameliorate muscle wasting in a cachectic mouse model bearing CT26 colorectal adenocarcinoma.
Chen, SZ; Lin, XY, 2017
)
2.24
"Treating calpain-induced apoptosis with this agent may be a feasible therapeutic strategy for patients with spinal cord injury."( Therapeutic efficacy of SJA6017, a calpain inhibitor, in rat spinal cord injury.
Akdemir, O; Barut, S; Bilguvar, K; Cirakoğlu, B; Colak, A; Karaoğlan, A; Sağmanligil, A; Sahan, E; Uçankale, M, 2008
)
1.01
"Treatment of calpain-1 with iso [4]LGE(2) in vitro results in covalent modification, inactivation, and resistance to protease digestion."( Neuroprotection in glaucoma using calpain-1 inhibitors: regional differences in calpain-1 activity in the trabecular meshwork, optic nerve and implications for therapeutics.
Bhattacharya, SK; Govindarajan, B; Laird, J; Salomon, RG; Sherman, R, 2008
)
0.98
"Pretreatment with calpain inhibitor prevented the reduction of phosphorylated ERK but had no significant effect on phosphorylated AKT."( Dual effect of 17β-estradiol on NMDA-induced neuronal death: involvement of metabotropic glutamate receptor 1.
Battaglia, G; Bruno, V; Merlo, S; Molinaro, G; Nicoletti, F; Sortino, MA; Spampinato, SF, 2012
)
0.7
"Co-treatment with calpain inhibitors resulted in preservation of titin, reduction in myofibrillar disarray, and attenuation of cardiomyocyte necrosis but not apoptosis."( Anthracyclines induce calpain-dependent titin proteolysis and necrosis in cardiomyocytes.
Eppenberger, HM; Guo, X; Helmes, M; Kuster, GM; Liao, R; Lim, CC; Sawyer, DB; Suter, TM; Zuppinger, C, 2004
)
0.96
"Pretreatment with calpain inhibitor decreased lactate dehydrogenase release by 20% and increased average dendritic branch length by 50% compared with neurons treated with okadaic acid alone."( Calpain activation in okadaic-acid-induced neurodegeneration.
Choi, J; Huh, JW; Hwang, O; Kim, D; Yoon, S, 2006
)
2.1
"Treatment with calpain inhibitor, calpeptin, decreased Th1 cytokines in PBMCs from MS patients."( Increased calpain correlates with Th1 cytokine profile in PBMCs from MS patients.
Banik, NL; Guyton, MK; Haque, A; Imam, SA; Ray, SK; Tyor, WR; Vandenbark, A, 2007
)
1.08
"Treatment with calpain inhibitors resulted in a two- to three-fold increase in the half-life of total AChRs."( Involvement of calpains in the destabilization of the acetylcholine receptor clusters in rat myotubes.
Kim, S; Nelson, PG, 2000
)
1
"Co-treatment with calpain and serine/threonine phosphatase inhibitors restored pCREB levels and rescued neurons."( Oxidative stress induces neuronal death by recruiting a protease and phosphatase-gated mechanism.
Loeffler, JP; Sée, V, 2001
)
0.63
"Treatment with calpain I or calpain II did not produce a conversion from XD to XO nor did it result in partial proteolysis of the enzyme."( Proteolytic conversion of xanthine dehydrogenase to xanthine oxidase: evidence against a role for calcium-activated protease (calpain).
Baudry, M; Lynch, G; Seubert, P; Stark, K, 1989
)
0.82

Toxicity

Cardiomyocyte-specific up-regulation of calpain-2 did not induce any adverse cardiac phenotypes under physiological conditions by age 3 months. The deletions did not appreciably compromise globular domain antibody binding, suggesting that the flexible tail is required to transmit toxic signals.

ExcerptReferenceRelevance
" Among various processes that have been thought to mediate the toxic effects of glutamate are activation of the Ca(2+)-dependent proteases calpain I and II and the activation of nitric oxide synthase."( Delayed antagonism of calpain reduces excitotoxicity in cultured neurons.
Brorson, JR; Marcuccilli, CJ; Miller, RJ, 1995
)
0.81
" This inhibitor also limited the toxicity, even when applied at times up to 1 hour after the onset of the toxic exposure."( Delayed antagonism of calpain reduces excitotoxicity in cultured neurons.
Brorson, JR; Marcuccilli, CJ; Miller, RJ, 1995
)
0.61
"We examined the mechanism by which capsaicin produces its toxic effects on cultures of rat sensory neurons."( Capsaicin-induced neurotoxicity in cultured dorsal root ganglion neurons: involvement of calcium-activated proteases.
Bleakman, D; Chard, PS; Miller, RJ; Savidge, JR, 1995
)
0.29
" The results indicate that, contrary to current hypotheses, the toxic mode of Al is not through an interaction with enzymatic catalytic metal binding sites but may be through the interaction with specific membrane lipids."( Aluminum interaction with plasma membrane lipids and enzyme metal binding sites and its potential role in Al cytotoxicity.
Jones, DL; Kochian, LV, 1997
)
0.3
" Accordingly, sensitive spectrin breakdown assays now are utilized to identify potential toxic side-effects of compounds and to develop calpain inhibitors for a wide range of indications including stroke, cerebral vasospasm, and kidney failure."( The pathogenic activation of calpain: a marker and mediator of cellular toxicity and disease states.
Bahr, BA; Vanderklish, PW, 2000
)
0.8
" The results presented here, indicate that the toxic effects of aluminium could be mediated through modifications in the intracellular calcium homeostasis, which may lead to impaired neuronal function."( Disruption of neuronal calcium homeostasis after chronic aluminium toxicity in rats.
Gill, KD; Kaur, A, 2005
)
0.33
" Moreover, NMDAR involvement causes the fatal activation of calpain, which, in turn, degrades tau protein into a 17-kDa peptide and possibly other highly toxic N-terminal peptides."( NMDA receptor mediates tau-induced neurotoxicity by calpain and ERK/MAPK activation.
Amadoro, G; Calissano, P; Canu, N; Cestari, V; Ciotti, MT; Costanzi, M, 2006
)
0.83
" Since the metabolic product of PLA(2) signaling, PGE(2), which augments toxic effect of NMDA, is known to stimulate cAMP, the effect of adenyl cyclase activator (forskolin plus IBMX) and inhibitor (MDL12,300) on NMDA-induced DPYSL3 degradation was tested."( PLA(2) signaling is involved in calpain-mediated degradation of synaptic dihydropyrimidinase-like 3 protein in response to NMDA excitotoxicity.
Chakravarthy, B; Kowara, R; Moraleja, KL, 2008
)
0.63
" Our experimental results suggest that the altered expression of calpain proteins may contribute to the adverse effects of NSAIDs on intestinal epithelial restitution."( Drug-induced alterations to gene and protein expression in intestinal epithelial cell 6 cells suggest a role for calpains in the gastrointestinal toxicity of nonsteroidal anti-inflammatory agents.
Freeman, LC; Ganta, S; Lillich, JD; Narvaez, D; Raveendran, NN; Silver, K; Weng, K, 2008
)
0.79
" The peptide is toxic to neurons, possibly by causing initial synaptic dysfunction and neuronal membrane dystrophy, promoted by increased cellular Ca(2+)."( Amyloid beta peptide toxicity in differentiated PC12 cells: calpain-calpastatin, caspase, and membrane damage.
Barnoy, S; Elkind, E; Kosower, NS; Vaisid, T, 2008
)
0.59
"Apoptosis is a tightly regulated physiological process, which can be initiated by toxic stimuli, such as cadmium (Cd2+)."( Novel roles for ceramides, calpains and caspases in kidney proximal tubule cell apoptosis: lessons from in vitro cadmium toxicity studies.
Lee, WK; Thévenod, F, 2008
)
0.64
" Abeta is toxic to neurons, possibly through causing initial synaptic dysfunction and neuronal membrane dystrophy, promoted by increased cellular Ca(2+)."( Calpastatin overexpression attenuates amyloid-beta-peptide toxicity in differentiated PC12 cells.
Barnoy, S; Kosower, NS; Vaisid, T, 2008
)
0.35
" Recently, we reported safe clamping associated with least ischemia-reperfusion injury as assessed by calpain-p in a rat model."( A safe protocol of intermittent hilar vascular clamping for hepatic resection in cirrhosis.
Doki, Y; Eguchi, H; Kishimoto, S; Kobayashi, S; Marubashi, S; Monden, M; Mori, M; Nagano, H; Noda, T; Sakon, M; Takeda, Y; Tanemura, M; Tomimaru, Y; Umeshita, K,
)
0.35
"Our results indicated that repeated 10-min hepatic vascular clamping interrupted by 5-min reperfusion is a safe protocol as it does not cause ischemia-reperfusion injury."( A safe protocol of intermittent hilar vascular clamping for hepatic resection in cirrhosis.
Doki, Y; Eguchi, H; Kishimoto, S; Kobayashi, S; Marubashi, S; Monden, M; Mori, M; Nagano, H; Noda, T; Sakon, M; Takeda, Y; Tanemura, M; Tomimaru, Y; Umeshita, K,
)
0.13
" Proteases activation is responsible for triggering deadly cascades during cell damage in toxic models."( Time-course correlation of early toxic events in three models of striatal damage: modulation by proteases inhibition.
Ali, SF; Carrillo-Mora, P; Chánez-Cárdenas, ME; Elinos-Calderón, D; Konigsberg, M; Morán, J; Pérez-De La Cruz, G; Pérez-De La Cruz, V; Santamaría, A; Silva-Adaya, D,
)
0.13
" Mutations in the gene encoding Cu/Zn superoxide dismutase (SOD1) cause ALS through a gain of toxic function."( Calpastatin reduces toxicity of SOD1G93A in a culture model of amyotrophic lateral sclerosis.
Durham, HD; Tradewell, ML, 2010
)
0.36
" Collectively, these results suggest that A-1254 exerts its toxic effect via REST by down-regulating synapsin 1 and decreasing H3 and H4 acetylation."( The repressor element 1-silencing transcription factor is a novel molecular target for the neurotoxic effect of the polychlorinated biphenyl mixture aroclor 1254 in neuroblastoma SH-SY5Y cells.
Canzoniero, LM; Cocco, S; Di Renzo, G; Formisano, L; Guida, N; Paturzo, F; Secondo, A; Sirabella, R; Ulianich, L, 2011
)
0.37
" Although this mutation was the first ever reported in the human APP gene, little is known about the molecular mechanisms underlying the direct toxic effects of this mutated Aβ on central neurons."( β-Amyloid carrying the Dutch mutation has diverse effects on calpain-mediated toxicity in hippocampal neurons.
Ferreira, A; Nicholson, AM; Walsh, DM; Wold, LA, 2012
)
0.62
" Supplementation of cells with exogenous calpastatin was able to reverse the toxic effect of METH on reduction in cell viability and tyrosine hydroxylase phosphorylation."( Calpastatin reduces calpain and caspase activation in methamphetamine-induced toxicity in human neuroblastoma SH-SY5Y cultured cells.
Chetsawang, B; Govitrapong, P; Phansuwan-Pujito, P; Suwanjang, W, 2012
)
0.7
" These deletions did not appreciably compromise globular domain antibody binding, suggesting that the flexible tail is required to transmit toxic signals that originate from the globular domain and trigger oxidative stress and calpain activation."( The toxicity of antiprion antibodies is mediated by the flexible tail of the prion protein.
Aguzzi, A; Baral, PK; Das, D; Falsig, J; Herrmann, US; Hornemann, S; James, MN; Kav, N; Li, B; Liberski, PP; O'Connor, T; Rahman, MH; Reimann, RR; Riek, R; Sonati, T; Swayampakula, M; Wieland, B; Yaganoglu, S, 2013
)
0.57
"Cardiotoxicity is a well-recognized side effect induced by chemotherapeutic drugs such as anthracycline and trastuzumab through different mechanisms."( Cardiac protective effects of dexrazoxane on animal cardiotoxicity model induced by anthracycline combined with trastuzumab is associated with upregulation of calpain-2.
Liu, J; Meng, T; Zhang, J; Zhang, S; Zhang, X, 2015
)
0.61
" This abnormal proteolysis leads to the accumulation of cleaved fragments, which have been identified as toxic and further they act as a seed for more aggregate formation, thereby increasing toxicity in neuronal cells."( n-Butylidenephthalide exhibits protection against neurotoxicity through regulation of tryptophan 2, 3 dioxygenase in spinocerebellar ataxia type 3.
Chiang, IT; Chiou, TW; Harn, HJ; Hsieh, DK; Lin, SY; Lin, SZ; Liu, JW; Rajamani, K; Wu, CH; You, DH, 2017
)
0.46
" Across all trials, the incidence of treatment-emergent adverse events was similar in the placebo and alicapistat groups."( Pharmacokinetics, Safety, Tolerability, and Pharmacodynamics of Alicapistat, a Selective Inhibitor of Human Calpains 1 and 2 for the Treatment of Alzheimer Disease: An Overview of Phase 1 Studies.
Goss, S; Jin, Z; Locke, C; Lon, HK; Mendonca, N; Othman, AA; Rendenbach-Mueller, B, 2019
)
0.73
" Cardiomyocyte-specific up-regulation of calpain-2 did not induce any adverse cardiac phenotypes under physiological conditions by age 3 months, but significantly reduced myocardial injury and improved myocardial function in doxorubicin-treated mice."( Calpain-2 promotes MKP-1 expression protecting cardiomyocytes in both in vitro and in vivo mouse models of doxorubicin-induced cardiotoxicity.
Fan, GC; Li, J; Ni, R; Peng, T; Robbins, J; Song, LS; Su, Z; Zhang, Y; Zheng, D, 2019
)
2.22
" However, ototoxicity is a major side effect of CDDP, and there is an associated risk of irreversible hearing loss."( Ursolic acid protects against cisplatin‑induced ototoxicity by inhibiting oxidative stress and TRPV1‑mediated Ca2+‑signaling.
Bao, D; Di, Y; Lin, Y; Liu, S; Ma, T; Qu, D; Tian, Y; Wang, A; Wang, Y; Xu, T; Yu, L, 2020
)
0.56

Pharmacokinetics

ExcerptReferenceRelevance
" Maximum alicapistat plasma concentrations were reached in 2 to 5 hours; half-life was 7 to 12 hours postdose."( Pharmacokinetics, Safety, Tolerability, and Pharmacodynamics of Alicapistat, a Selective Inhibitor of Human Calpains 1 and 2 for the Treatment of Alzheimer Disease: An Overview of Phase 1 Studies.
Goss, S; Jin, Z; Locke, C; Lon, HK; Mendonca, N; Othman, AA; Rendenbach-Mueller, B, 2019
)
0.73

Compound-Compound Interactions

ExcerptReferenceRelevance
" In this study, we investigated whether dexrzoxane could reduce cardiotoxicity in the treatment of anthracycline combined with trastuzumab."( Cardiac protective effects of dexrazoxane on animal cardiotoxicity model induced by anthracycline combined with trastuzumab is associated with upregulation of calpain-2.
Liu, J; Meng, T; Zhang, J; Zhang, S; Zhang, X, 2015
)
0.61

Bioavailability

The previously reported calpain inhibitor SJA6017 (1) showed oral efficacy in a retinal pharmacological model. Its oral bioavailability was low due to the metabolic lability and low water-solubility. Therapeutic strategies targeting malfunctions of calpains have been developed.

ExcerptReferenceRelevance
" In particular, these calpain inhibitors showed oral bioavailability in rats as demonstrated by N-(1-benzyl-2-carbamoyl-2-oxoethyl)-2-[E-2-(4-diethylaminomethylphenyl)ethen-1-yl]benzamide (5d)."( Benzoylalanine-derived ketoamides carrying vinylbenzyl amino residues: discovery of potent water-soluble calpain inhibitors with oral bioavailability.
Beckenbach, E; Bopp, S; Hofmann, HP; Kartal, A; Kästel, C; Lindner, T; Lubisch, W; Metz-Garrecht, M; Möller, A; Reeb, J; Regner, F; Vierling, M, 2003
)
0.85
" The previously reported calpain inhibitor SJA6017 (1) showed oral efficacy in a retinal pharmacological model, but its oral bioavailability was low due to the metabolic lability and low water-solubility."( Exploration of orally available calpain inhibitors. Part 3: Dipeptidyl alpha-ketoamide derivatives containing pyridine moiety.
Miyashita, H; Shirasaki, Y; Yamaguchi, M, 2006
)
0.92
"We previously reported a potent calpain inhibitor 1 (SJA6017, N-(4-fluorophenyl)-l-valyl-l-leucinal), which displayed relatively low oral bioavailability (BA)."( Exploration of orally available calpain inhibitors 2: peptidyl hemiacetal derivatives.
Inoue, J; Miyashita, H; Nakamura, M; Sakai, O; Shirasaki, Y; Yamaguchi, M, 2006
)
0.9
" The orally bioavailable inhibitors, hemiacetal 3 (SNJ-1715), amphipathic ketoamide 5 (SNJ-1945), and pyridine ketoamide 6 (SNJ-2008), were evaluated for their retinal pharmacokinetic (PK) profiles."( Retinal penetration of calpain inhibitors in rats after oral administration.
Miyashita, H; Shirasaki, Y; Yamaguchi, M, 2006
)
0.64
" Improved bioavailability is needed and solution of their precise mode of action should prompt the development of specific calpain-1 screens for novel classes of inhibitors."( Calpain-1 inhibitors for selective treatment of rheumatoid arthritis: what is the future?
Adams, SE; Allemann, RK; Hallett, MB; Miller, DJ, 2013
)
2.04
" NO is consumed by superoxide to form peroxynitrite, leading to decreased NO bioavailability for S-nitrosoglutathione (GSNO) synthesis and regulation of neuroprotective pathways."( Targeting the nNOS/peroxynitrite/calpain system to confer neuroprotection and aid functional recovery in a mouse model of TBI.
Annamalai, B; Dhammu, TS; Dhindsa, TS; Khan, M; Matsuda, F; Singh, AK; Singh, I, 2016
)
0.72
" Therapeutic strategies targeting malfunctions of calpains have been developed, driven primarily by improvements in the specificity and bioavailability of calpain inhibitors."( Calpain research for drug discovery: challenges and potential.
Ono, Y; Saido, TC; Sorimachi, H, 2016
)
2.13
" Nevertheless other compounds as lipids or sugars should be valorized along with polyphenols to improve their bioavailability into highly protected organs as brain or eye."( Characterization, anti-oxidative effect of grape seed powder and in silico affinity profiling of polyphenolic and extra-phenolic compounds for calpain inhibition.
Aouani, E; El Ayed, M; Elkahoui, S; Kadri, S; Limam, F; Mabrouk, M; Mokni, M, 2019
)
0.71

Dosage Studied

Calpain activity in brain increased by 40% in TOCP hens compared to the control group when measured 24h after dosing. Dose-response and time course studies revealed that mu-cal pain was more sensitive to PDBu than m-calpain.

ExcerptRelevanceReference
" In addition, the Ca2+ dose-response curves of both activities in intact platelets, obtained by stimulation with A23187 in the presence of Ca2+/HEDTA-buffers, were compared."( Correlation between calpain-mediated cytoskeletal degradation and expression of platelet procoagulant activity. A role for the platelet membrane-skeleton in the regulation of membrane lipid asymmetry?
Bevers, EM; Comfurius, P; Verhallen, PF; Zwaal, RF, 1987
)
0.6
" Results of a controlled, dose-response study indicated that leupeptin was absorbed into plasma by the oral route of administration."( Neuromuscular recovery after peripheral nerve repair: effects of an orally-administered peptide in a primate model.
Badalamente, MA; Hurst, LC; Stracher, A, 1995
)
0.29
"An ex vivo brain protease inhibition assay established pharmacodynamic dosing parameters for MDL 28,170."( Six-hour window of opportunity for calpain inhibition in focal cerebral ischemia in rats.
Chmielewski, PA; Johnson, MP; Koehl, JR; Linnik, MD; Markgraf, CG; McCarty, DR; Medhi, S; Velayo, NL, 1998
)
0.58
" The activity of apopain (CPP32), an interleukin 1beta converting enzyme (ICE)-like cysteine protease specifically associated with apoptosis, was increased following dosing with aluminum."( Elevation of cerebral proteases after systemic administration of aluminum.
Bondy, SC; Guo-Ross, S; Yang, E, 1998
)
0.3
" DNA samples of these members were analysed to ascertain the carrier status, by PCR followed by dosage analysis by densitometry."( Deletion analysis & calpain status for carrier detection in a family with Duchenne muscular dystrophy.
Anandaraj, MP; Devi, NG; Hussain, T; Kumari, CK, 1998
)
0.62
"" While investigators continue to examine the best dosing paradigms for gentamicin in the treatment of Ménière's disease and for steroids in the treatment of hearing loss, they have also begun to focus on the use of other agents."( Sustained-release delivery of leupeptin in the chinchilla: hearing results.
Balough, BJ; Finley, JC; Gottshall, KR; Hoffer, ME; Killian, P; Shulman, A; Wester, D, 2003
)
0.32
" Dose-response and time course studies revealed that mu-calpain was more sensitive to PDBu than m-calpain and the temporal course of the mu-calpain change coincides better with that of APPs release."( Mu-calpain is functionally required for alpha-processing of Alzheimer's beta-amyloid precursor protein.
Chen, M; Fernandez, HL, 2005
)
1.2
" Cows receiving 25-OH D3 or DCAD+25-OH D3 were dosed with 125 mg of 25-OH D3 6 d before slaughter."( Effects of 25-hydroxyvitamin D3 and manipulated dietary cation-anion difference on the tenderness of beef from cull native Korean cows.
Cho, YM; Choi, H; Hwang, IH; Kim, YK; Myung, KH, 2006
)
0.33
" Identical tempol dosing maintained respiratory function and attenuated 3NT in isolated cortical mitochondria at 12 h after injury, the peak of mitochondrial dysfunction."( Neuroprotective effects of tempol, a catalytic scavenger of peroxynitrite-derived free radicals, in a mouse traumatic brain injury model.
Carrico, KM; Deng-Bryant, Y; Hall, ED; Singh, IN, 2008
)
0.35
" However, a therapeutic window analysis showed that the axonal cytoskeletal protective effects require tempol dosing within the first hour after injury."( Pharmacological evidence for a role of peroxynitrite in the pathophysiology of spinal cord injury.
Hall, ED; Xiong, Y, 2009
)
0.35
" We found that chronic treatment of neurons with a low dosage of two CNS-permeable statins (lovastatin and simvastatin) selectively reduced NMDA-induced cell death but not the caspase-mediated apoptosis."( Statin's excitoprotection is mediated by sAPP and the subsequent attenuation of calpain-induced truncation events, likely via rho-ROCK signaling.
Kwak, YD; Liao, FF; Luo, Z; Ma, T; Thompson, R; Xu, H; Yang, Z; Zhao, Y, 2009
)
0.58
" Thus responses to NMDA receptor activity follow a classical hormetic dose-response curve: both too much and too little can be harmful."( Coupling of the NMDA receptor to neuroprotective and neurodestructive events.
Hardingham, GE, 2009
)
0.35
"In a dose-response study, a 60 mg/kg bolus followed by 30 mg/kg infusion was required to reduce postischemic brain calpain activity measured by Western blot of hippocampal homogenates at 48 hrs after injury."( Neuroprotection with delayed calpain inhibition after transient forebrain ischemia.
Bevers, MB; Chen, Z; Frederick, JR; Ingleton, LP; Ma, M; Neumar, RW, 2008
)
0.85
" This was preceded by a dose-response and pharmacodynamic evaluation of IV or IP doses of MDL-28170 with regard to ex vivo inhibition of calpain 2 activity in harvested brain homogenates."( A pharmacological analysis of the neuroprotective efficacy of the brain- and cell-permeable calpain inhibitor MDL-28170 in the mouse controlled cortical impact traumatic brain injury model.
Bains, M; Carrico, KM; Hall, ED; Mustafa, AG; Thompson, SN, 2010
)
0.78
" Based upon this preservation of a major Ca(2+) homeostatic mechanism, we have now performed dose-response and therapeutic window analyses of the ability of U-83836E to reduce post-traumatic calpain-mediated cytoskeletal (α-spectrin) proteolysis in ipsilateral cortical homogenates at its 24 h post-TBI peak."( Pharmacological inhibition of lipid peroxidation attenuates calpain-mediated cytoskeletal degradation after traumatic brain injury.
Carrico, KM; Hall, ED; Mustafa, AG; Wang, JA, 2011
)
0.8
"The current Organisation for Economic Co-operation and Development (OECD) guidelines for evaluating organophosphorus-induced delayed neuropathy (OPIDN) require the observation of dosed animals over several days and the sacrifice of 48 hens."( Comparative in vitro study of the inhibition of human and hen esterases by methamidophos enantiomers.
DeOliveira, GH; Ehrich, M; Emerick, GL; Oliveira, RV, 2012
)
0.38
" Adult hens were treated with a dose of 750mg/kg TOCP by gavage, or injected subcutaneously with 60mg/kg phenylmethanesulfonyl fluoride (PMSF) dissolved in DMSO 24h earlier and subsequently treated with TOCP, then sacrificed on the time-points of 0, 1, 5, 10, and 21 days after dosing of TOCP respectively."( Changes in beclin-1 and micro-calpain expression in tri-ortho-cresyl phosphate-induced delayed neuropathy.
Han, X; Song, F; Xie, K; Zeng, T; Zhang, C; Zou, C, 2012
)
0.67
" Calpain activity in brain increased by 40% in TOCP hens compared to the control group when measured 24h after dosing and remained high (18% over control) 21 days after dosing."( Biochemical, histopathological and clinical evaluation of delayed effects caused by methamidophos isoforms and TOCP in hens: ameliorative effects using control of calcium homeostasis.
Deoliveira, GH; Ehrich, M; Emerick, GL; Jortner, BS; Oliveira, RV, 2012
)
1.29
" The effect of SNJ-1945 on α-spectrin degradation exhibited a U-shaped dose-response curve when treatment was initiated 15 min post-TBI."( Pharmacological analysis of the cortical neuronal cytoskeletal protective efficacy of the calpain inhibitor SNJ-1945 in a mouse traumatic brain injury model.
Bains, M; Barnes, CC; Cebak, JE; Geddes, JW; Gilmer, LK; Hall, ED; Thompson, SN, 2013
)
0.61
" Here, we show that oral dosing with SNJ-1945, a novel water-soluble calpain inhibitor, reduces experimental autoimmune encephalomyelitis clinical scores in vivo and has a two pronged effect via anti-inflammation and protection against neurodegeneration."( Effects of a novel orally administered calpain inhibitor SNJ-1945 on immunomodulation and neurodegeneration in a murine model of multiple sclerosis.
Azuma, M; Banik, NL; Beeson, C; Haque, A; Inoue, J; Smith, A; Trager, N; Wallace Iv, G, 2014
)
0.91
" Using prenatal transient systemic hypoxia-ischemia (TSHI) in rats to mimic CNS injury from extreme preterm birth, and postnatal EPO treatment with a clinically relevant dosing regimen, we found sustained postnatal excess cortical calpain activation following prenatal TSHI, as shown by the cleavage of alpha II-spectrin (αII-spectrin) into 145-kDa αII-spectrin degradation products (αII-SDPs) and p35 into p25."( Erythropoietin Modulates Cerebral and Serum Degradation Products from Excess Calpain Activation following Prenatal Hypoxia-Ischemia.
Corbett, CJ; Jantzie, LL; Robinson, S; Winer, JL, 2016
)
0.85
" Systemic injection of C2I 30 min before training in the fear-conditioning paradigm resulted in a biphasic dose-response curve, with low doses enhancing and high doses inhibiting freezing behavior."( A calpain-2 selective inhibitor enhances learning & memory by prolonging ERK activation.
Baudry, M; Bi, X; Liu, Y; Sun, J; Wang, Y; Zhu, G, 2016
)
1.16
" C57BL/6J mice infected with the Daniel's strain of Theiler's murine encephalomyelitis virus were treated with the FDA-approved drug ritonavir using a dosing regimen that resulted in plasma concentrations within the therapeutic range for calpain inhibition."( Neuroprotection mediated by inhibition of calpain during acute viral encephalitis.
Buenz, EJ; Howe, CL; LaFrance-Corey, RG; McGovern, RM; Mirchia, K; Reid, JM; Sauer, BM, 2016
)
0.88
"PL mice with myelin basic protein on Days 0 and 2, and mice received twice daily oral dosing of SNJ 1945 from Day 9 until sacrificing (Day 26)."( Calpain inhibition reduces structural and functional impairment of retinal ganglion cells in experimental optic neuritis.
Azuma, M; Banik, NL; Inoue, J; Ray, SK; Rohrer, B; Samantaray, S; Smith, AW; Wheless, L, 2016
)
1.88
" UPDs can cause clinical abnormalities owing to the aberrant dosage of genes regulated by epigenetic imprinting or homozygosity of variants for recessive phenotypes."( Obesity and developmental delay in a patient with uniparental disomy of chromosome 2.
Chang, G; Chen, Y; Ding, Y; Li, J; Li, N; Liu, R; Shen, Y; Wang, J; Wang, X; Yu, T, 2016
)
0.43
[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (6,872)

TimeframeStudies, This Drug (%)All Drugs %
pre-1990532 (7.74)18.7374
1990's1287 (18.73)18.2507
2000's2376 (34.58)29.6817
2010's2232 (32.48)24.3611
2020's445 (6.48)2.80
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Market Indicators

Research Demand Index: 53.66

According to the monthly volume, diversity, and competition of internet searches for this compound, as well the volume and growth of publications, there is estimated to be very strong demand-to-supply ratio for research on this compound.

MetricThis Compound (vs All)
Research Demand Index53.66 (24.57)
Research Supply Index8.86 (2.92)
Research Growth Index4.87 (4.65)
Search Engine Demand Index93.56 (26.88)
Search Engine Supply Index2.00 (0.95)

This Compound (53.66)

All Compounds (24.57)

Study Types

Publication TypeThis drug (%)All Drugs (%)
Trials25 (0.36%)5.53%
Reviews563 (8.02%)6.00%
Case Studies73 (1.04%)4.05%
Observational3 (0.04%)0.25%
Other6,355 (90.54%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]