Page last updated: 2024-08-07 19:45:17

Disintegrin and metalloproteinase domain-containing protein 8

A disintegrin and metalloproteinase domain-containing protein 8 that is encoded in the genome of human. [PRO:WCB, UniProtKB:P78325]

Synonyms

ADAM 8;
EC 3.4.24.-;
Cell surface antigen MS2

Research

Bioassay Publications (1)

TimeframeStudies on this Protein(%)All Drugs %
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's1 (100.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Compounds (1)

Drugs with Inhibition Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
incb3619Homo sapiens (human)IC501.000011

Enables

This protein enables 9 target(s):

TargetCategoryDefinition
serine-type endopeptidase activitymolecular functionCatalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). [GOC:mah, https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE]
calcium ion bindingmolecular functionBinding to a calcium ion (Ca2+). [GOC:ai]
protein bindingmolecular functionBinding to a protein. [GOC:go_curators]
metallopeptidase activitymolecular functionCatalysis of the hydrolysis of peptide bonds by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. [GOC:mah, https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE]
zinc ion bindingmolecular functionBinding to a zinc ion (Zn). [GOC:ai]
tumor necrosis factor receptor superfamily bindingmolecular functionBinding to a member of the tumor necrosis factor receptor superfamily. [GOC:add]
immunoglobulin receptor bindingmolecular functionBinding to one or more specific sites on an immunoglobulin receptor molecule. [GOC:BHF, GOC:vk]
metalloendopeptidase activitymolecular functionCatalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. [GOC:mah, https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE, https://www.ebi.ac.uk/merops/about/glossary.shtml#ENDOPEPTIDASE]
cell adhesion molecule bindingmolecular functionBinding to a cell adhesion molecule. [GOC:ai]

Located In

This protein is located in 11 target(s):

TargetCategoryDefinition
podosomecellular componentAn actin-rich adhesion structure characterized by formation upon cell substrate contact and localization at the substrate-attached part of the cell, contain an F-actin-rich core surrounded by a ring structure containing proteins such as vinculin and talin, and have a diameter of 0.5 mm. [PMID:12837608, PMID:15890982]
cytoplasmcellular componentThe contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684]
plasma membranecellular componentThe membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. [ISBN:0716731363]
cell surfacecellular componentThe external part of the cell wall and/or plasma membrane. [GOC:jl, GOC:mtg_sensu, GOC:sm]
phagolysosomecellular componentA membrane-bounded intracellular vesicle formed by maturation of an early phagosome following the ingestion of particulate material by phagocytosis; during maturation, phagosomes acquire markers of late endosomes and lysosomes. [GOC:mah, PMID:12388753, PMID:14733906]
dense core granule membranecellular componentThe lipid bilayer surrounding a dense core granule. [GOC:mah]
specific granule membranecellular componentThe lipid bilayer surrounding a specific granule, a granule with a membranous, tubular internal structure, found primarily in mature neutrophil cells. Most are released into the extracellular fluid. Specific granules contain lactoferrin, lysozyme, vitamin B12 binding protein and elastase. [GOC:bf, PMID:7334549]
specific granulecellular componentGranule with a membranous, tubular internal structure, found primarily in mature neutrophil cells. Most are released into the extracellular fluid. Specific granules contain lactoferrin, lysozyme, vitamin B12 binding protein and elastase. [GOC:jl, ISBN:0721662544, PMID:7334549]
tertiary granulecellular componentA secretory granule that contains cathepsin and gelatinase and is readily exocytosed upon cell activation; found primarily in mature neutrophil cells. [GOC:BHF, GOC:mah, GOC:rl, PMID:12070036]
tertiary granule membranecellular componentThe lipid bilayer surrounding a tertiary granule. [GOC:BHF, GOC:mah, GOC:rl, PMID:12070036]
ficolin-1-rich granule membranecellular componentThe lipid bilayer surrounding a ficolin-1-rich granule. [GOC:mec, PMID:23650620]

Part Of

This protein is part of 1 target(s):

TargetCategoryDefinition
alpha9-beta1 integrin-ADAM8 complexcellular componentA protein complex that consists of an alpha9-beta1 integrin complex bound to the transmembrane metallopeptidase ADAM8. [PMID:16995821]

Involved In

This protein is involved in 30 target(s):

TargetCategoryDefinition
cell morphogenesisbiological processThe developmental process in which the size or shape of a cell is generated and organized. [GOC:clt, GOC:dph, GOC:go_curators, GOC:tb]
angiogenesisbiological processBlood vessel formation when new vessels emerge from the proliferation of pre-existing blood vessels. [ISBN:0878932453]
leukocyte migration involved in inflammatory responsebiological processThe movement of a leukocyte within or between different tissues and organs of the body contributing to an inflammatory response. [GOC:add, ISBN:0781735149, PMID:14680625, PMID:14708592, PMID:7507411, PMID:8600538]
positive regulation of acute inflammatory responsebiological processAny process that activates or increases the frequency, rate, or extent of an acute inflammatory response. [GOC:add]
inflammatory responsebiological processThe immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. [GO_REF:0000022, ISBN:0198506732]
canonical NF-kappaB signal transductionbiological processAn intracellular signaling cassette characterized by the I-kappaB-kinase (IKK)-dependent activation of NF-kappaB, also known as the canonical NF-kappaB signaling cascade. The cascade begins with activation of a trimeric IKK complex (consisting of catalytic kinase subunits IKKalpha and/or IKKbeta, and the regulatory scaffold protein NEMO) and ends with the regulation of transcription of target genes by NF-kappaB. In a resting state, NF-kappaB dimers are bound to I-kappaB proteins, sequestering NF-kappaB in the cytoplasm. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing the NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription. The canonical NF-kappaB pathway is mainly stimulated by proinflammatory cytokines such as IL-1beta, tumor necrosis factor (TNF)-alpha, antigen ligands, and toll-like receptors (TLRs). [GOC:bf, PMID:12773372, PMID:34659217]
positive regulation of epithelial to mesenchymal transitionbiological processAny process that increases the rate, frequency, or extent of epithelial to mesenchymal transition. Epithelial to mesenchymal transition is where an epithelial cell loses apical/basolateral polarity, severs intercellular adhesive junctions, degrades basement membrane components and becomes a migratory mesenchymal cell. [GOC:BHF, GOC:dph, GOC:tb]
positive regulation of protein processingbiological processAny process that increases the rate, frequency or extent of protein maturation by peptide bond cleavage. [GOC:dph, GOC:mah, GOC:tb]
regulation of cell-cell adhesionbiological processAny process that modulates the frequency, rate or extent of attachment of a cell to another cell. [GOC:isa_complete]
extracellular matrix disassemblybiological processA process that results in the breakdown of the extracellular matrix. [GOC:jid]
signal releasebiological processThe process in which a signal is secreted or discharged into the extracellular medium from a cellular source. [GOC:mtg_signal]
positive regulation of T cell differentiation in thymusbiological processAny process that activates or increases the frequency, rate or extent of T cell differentiation in the thymus. [GOC:add, GOC:mah]
positive regulation of MAPK cascadebiological processAny process that activates or increases the frequency, rate or extent of signal transduction mediated by the MAPK cascade. [GOC:go_curators]
negative regulation of neuron apoptotic processbiological processAny process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process in neurons. [GOC:go_curators, GOC:mtg_apoptosis]
positive regulation of innate immune responsebiological processAny process that activates or increases the frequency, rate or extent of the innate immune response, the organism's first line of defense against infection. [GOC:ebc]
positive regulation of bone resorptionbiological processAny process that activates or increases the frequency, rate or extent of bone resorption. [GOC:go_curators]
positive regulation of cell adhesionbiological processAny process that activates or increases the frequency, rate or extent of cell adhesion. [GOC:go_curators]
lymphocyte chemotaxisbiological processThe directed movement of a lymphocyte in response to an external stimulus. [GOC:hjd, GOC:jid, PMID:12391252]
positive regulation of protein secretionbiological processAny process that activates or increases the frequency, rate or extent of the controlled release of a protein from a cell. [GOC:ai]
positive regulation of membrane protein ectodomain proteolysisbiological processAny process that activates or increases the frequency, rate or extent of membrane protein ectodomain peptidolysis. [GOC:ai]
positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transductionbiological processAny process that activates or increases the frequency, rate or extent of phosphatidylinositol 3-kinase/protein kinase B signal transduction. [GOC:ai]
positive regulation of thymocyte apoptotic processbiological processAny process that activates or increases the frequency, rate or extent of thymocyte death by apoptotic process. [GOC:add, GOC:mtg_apoptosis, ISBN:0781765196]
cellular response to hypoxiabiological processAny process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level. [GOC:mah]
cell-cell adhesionbiological processThe attachment of one cell to another cell via adhesion molecules. [GOC:dos]
positive regulation of tumor necrosis factor (ligand) superfamily member 11 productionbiological processAny process that activates or increases the frequency, rate or extent of tumor necrosis factor (ligand) superfamily member 11 production. [GOC:BHF, GOC:mah]
positive regulation of neutrophil extravasationbiological processAny process that activates or increases the frequency, rate or extent of neutrophil extravasation. [GOC:BHF, GOC:mah]
positive regulation of fibronectin-dependent thymocyte migrationbiological processAny process that activates or increases the frequency, rate or extent of fibronectin-dependent thymocyte migration. [GOC:BHF, GOC:mah]
positive regulation of eosinophil migrationbiological processAny process that activates or increases the frequency, rate or extent of eosinophil migration. [GOC:mah]
positive regulation of cellular extravasationbiological processAny process that activates or increases the frequency, rate, or extent of cellular extravasation. [GOC:add]
proteolysisbiological processThe hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. [GOC:bf, GOC:mah]