piperidines has been researched along with Hemolysis* in 21 studies
1 review(s) available for piperidines and Hemolysis
1 trial(s) available for piperidines and Hemolysis
20 other study(ies) available for piperidines and Hemolysis
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Alectinib induces marked red cell spheroacanthocytosis in a near-ubiquitous fashion and is associated with reduced eosin-5-maleimide binding.
We reviewed haematological investigations for 43 patients treated at a single centre with alectinib, an inhibitor of anaplastic lymphoma kinase (ALK) which is considered standard first-line treatment for patients with ALK-rearranged advanced non-small cell lung cancer. Ninety-five percent of patients developed marked acanthocytosis, echinocytosis and/or spheroacanthocytosis, not observable with prior treatment with other ALK-inhibitors. Anaemia developed in 73% of patients (38% <100 g/L, 8% <80 g/L), though definite new haemolysis was present in only 11%. Eosin-5-maleimide binding was reduced in all assessed patients, and increased membrane cholesterol was identified in one patient assessed with lattice light sheet microscopy. We have identified a previously undescribed phenomenon whereby alectinib induces red cell membrane abnormalities in nearly all patients through an unclear, but likely ALK-independent, mechanism, resulting in mild anaemia without universal haemolysis. Topics: Abetalipoproteinemia; Anaplastic Lymphoma Kinase; Anemia; Carbazoles; Carcinoma, Non-Small-Cell Lung; Hemolysis; Humans; Lung Neoplasms; Maleimides; Piperidines; Protein Kinase Inhibitors; Retrospective Studies | 2021 |
Two cases of marked red cell anisopoikilocytosis and haemolysis with alectinib, an anaplastic lymphoma kinase inhibitor.
Topics: Aged; Anaplastic Lymphoma Kinase; Brain Neoplasms; Carbazoles; Erythrocytes; Female; Hemolysis; Humans; Lung Neoplasms; Male; Piperidines; Protein Kinase Inhibitors | 2020 |
Severe hemolysis and transfusion reactions after treatment with BGB-3111 and PD-1 antibody for Waldenström macroglobulinemia.
Topics: Antibodies, Monoclonal; Antineoplastic Agents; Blood Transfusion; Female; Hemolysis; Humans; Middle Aged; Piperidines; Prognosis; Programmed Cell Death 1 Receptor; Pyrazoles; Pyrimidines; Transfusion Reaction; Waldenstrom Macroglobulinemia | 2018 |
Acetamide Derivatives of Chromen-2-ones as Potent Cholinesterase Inhibitors.
Alzheimer's disease (AD), a neurodegenerative disorder, is a serious medical issue worldwide with drastic social consequences. Inhibition of cholinesterase is one of the rational and effective approaches to retard the symptoms of AD and, hence, consistent efforts are being made to develop efficient anti-cholinesterase agents. In pursuit of this, a series of 19 acetamide derivatives of chromen-2-ones were synthesized and evaluated for their acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) inhibitory potential. All the synthesized compounds exhibited significant anti-AChE and anti-BChE activity, with IC Topics: Acetylcholinesterase; Alzheimer Disease; Animals; Blood-Brain Barrier; Butyrylcholinesterase; Cholinesterase Inhibitors; Chromones; Donepezil; Electrophorus; Erythrocytes; Hemolysis; Humans; Indans; Inhibitory Concentration 50; Neuroblastoma; Piperidines | 2017 |
Potential Implications for Designing Drugs Against the Brown Spider Venom Phospholipase-D.
Loxoscelism refers to the clinical symptoms that develop after brown spider bites. Brown spider venoms contain several phospholipase-D isoforms, which are the main toxins responsible for both the cutaneous and systemic effects of loxoscelism. Understanding of the phospholipase-D catalytic mechanism is crucial for the development of specific treatment that could reverse the toxic effects caused by the spider bite. Based on enzymatic, biological, structural, and thermodynamic tests, we show some features suitable for designing drugs against loxoscelism. Firstly, through molecular docking and molecular dynamics predictions, we found three different molecules (Suramin, Vu0155056, and Vu0359595) that were able to bind the enzyme's catalytic site and interact with catalytically important residues (His12 or His47) and with the Mg Topics: Animals; Arthropod Proteins; Benzimidazoles; Brown Recluse Spider; Drug Design; Drug Evaluation, Preclinical; Enzyme Inhibitors; Hemolysis; Humans; Kinetics; Ligands; Molecular Docking Simulation; Molecular Dynamics Simulation; Necrosis; Phospholipase D; Phosphoric Diester Hydrolases; Piperidines; Rabbits; Recombinant Proteins; Skin; Spider Bites; Spider Venoms; Suramin | 2017 |
A supported liquid extraction LC-MS/MS method for determination of concentrations of GDC-0425, a small molecule Checkpoint kinase 1 inhibitor, in human plasma.
A liquid chromatography-tandem mass spectrometry (LC-MS/MS) method for the determination of GDC-0425 concentrations in human plasma has been developed and validated. Supported liquid extraction was used to extract plasma samples (50 μL) and the resulting samples were analyzed using reverse-phase chromatography and mass spectrometry coupled with a turbo-ionspray interface. The mass analysis of GDC-0425 was performed using multiple reaction monitoring transitions in positive ionization mode. The method was validated over the calibration curve range of 1.00-1000 ng/mL using linear regression and 1/x Topics: Checkpoint Kinase 1; Chromatography, Liquid; Hemolysis; Heterocyclic Compounds, 3-Ring; Humans; Limit of Detection; Piperidines; Protein Kinase Inhibitors; Reference Standards; Reproducibility of Results; Tandem Mass Spectrometry | 2016 |
Suicidal inactivation of methemoglobin by generation of thiyl radical: insight into NAC mediated protection in RBC.
N-acetyl-L-cysteine (NAC) improves antioxidant potentials of RBCs to provide protection against oxidative stress induced hemolysis. The antioxidant mechanism of NAC to reduce oxidative stress in RBC, studied through inactivation of pro-oxidant MetHb. NAC causes irreversible inactivation of the MetHb in an H2O2 dependent manner, and the inactivation follows the pseudo- first- order kinetics. The kinetic constants are ki = 8.5μM, kinact = 0.706 min(-1) and t1/2 = 0.9 min. Spectroscopic studies indicate that MetHb accepts NAC as a substrate and oxidizes through a single electron transfer mechanism to the NACox. The single e- oxidation product of NAC has been identified as the 5, 5'- dimethyl-1- pyrroline N- oxide (DMPO) adduct of the sulfur centered radical (a(N) = 15.2 G and a(H)=16.78 G). Binding studies indicate that NACox interacts at the heme moiety and NAC oxidation through MetHb is essential for NAC binding. Heme-NAC adduct dissociated from MetHb and identified (m/z 1011.19) as 2:1 ratio of NAC/heme in the adduct. TEMPO and PBN treatment reduces NAC binding to MetHb and protects against inactivation confirms the role of thiyl radical in the inactivation process. Furthermore, scavenging thiyl radicals by TEMPO abolish the protective effect of NAC in hemolysis. Current work highlights antioxidant mechanism of NAC through NAC thiyl radical generation, and MetHb inactivation to exhibit protection in RBC against oxidative stress induced hemolysis. Topics: Acetylcysteine; Cytoprotection; Erythrocytes; Free Radicals; Heme; Hemolysis; Humans; Hydrogen Peroxide; Kinetics; Methemoglobin; Oxidation-Reduction; Oxidative Stress; Peroxidase; Piperidines; Protective Agents; Spectrometry, Mass, Electrospray Ionization | 2013 |
Inhibition of intermediate-conductance Ca2+-activated K+ channel and cytoprotective properties of 4-piperidinomethyl-2-isopropyl-5-methylphenol.
The ionic mechanisms and cytoprotective activities of 4-piperidinomethyl-2-isopropyl-5-methylphenol (THPI), an analogue of thymol, were investigated in HL-60 granulocytes and in human erythrocytes, respectively. THPI inhibited K+ outward current (I(K)) in a concentration-dependent manner in HL-60 leukocytes, with an IC50 value of 4 microM. Neither iberiotoxin (200 nM) nor paxilline (1 microM) suppressed the amplitude of I(K), whereas clotrimazole (5 microM) significantly inhibited it. In the inside-out configuration of single channel recordings, application of THPI (5 microM) into the bath medium did not alter the single-channel conductance of intermediate-conductance Ca2+-activated K+ (IK(Ca)) channels (i.e K(Ca)3.1 channels), but it suppressed the channel activity significantly. THPI-induced inhibition of IK(Ca) channels was reversed by a further application of 1-ethyl-2-benzimidazolinone (10 microM). THPI-induced reduction in IK(Ca)-channel activity in these cells was primarily due to a decrease in mean open time. These results provide direct evidence that THPI is capable of suppressing the activity of IK(Ca) channels in HL-60 cells. The antioxidant action of THPI also revealed a beneficial cytoprotective effect against mitomycin C-mediated haemolytic effect in human erythrocytes. The results of this study suggest that blockade of IK(Ca) channels and the membrane-protecting activity of THPI would combine to have beneficial effects in lessening the severity of haemolytic crisis and reducing anaemia in sickle cell disease. Topics: Antioxidants; Cells, Cultured; Dose-Response Relationship, Drug; Electric Conductivity; Electrophysiology; Erythrocytes; Granulocytes; Hemolysis; Humans; Inhibitory Concentration 50; Intermediate-Conductance Calcium-Activated Potassium Channels; Mitomycin; Phenols; Piperidines | 2007 |
The relationship between structure and antioxidative activity of piperidine nitroxides.
We have investigated the relationship between structure and antioxidative activity of piperidine nitroxides which were substituted by different groups at the 4-position. All of the tested piperidine nitroxides inhibited malondialdehyde (MDA) generation caused either spontaneously or by a hydroxyl free radical generation system (Fe2+-ascorbic acid) in homogenates of liver, heart and kidney of rats, and antagonized H2O2-induced haemolysis from rat erythrocytes in a concentration-dependent manner. The same rank was followed: Bis-(4-amino-2,2,6,6-tetramethyl piperidinooxyl) (4-BIS-Tempo) and 4-azido-2,2,6,6-tetramethyl piperidinooxyl (4-N(3)-Tempo) > 4-isothiocyanate-2,2,6,6-tetramethyl piperidinooxyl (4-ISO-Tempo), 4-2', 4'-dinitrophenylhy-drazone-2,2,6,6-tetramethyl piperidinooxyl (4-D-Tempo), 4-sulfonate-2,2,6,6-tetramethyl piperidinooxyl (4-S-Tempo) and 4-amino-2,2,6,6-tetramethyl piperidinooxyl (4-NH(2)-Tempo) > 4-acetate ester-2,2,6,6-tetramethyl piperidinooxyl (4-A-Tempo) and 4-benzoate-2,2,6,6-tetramethyl piperidinooxyl (4-B-Tempo). With the exception of 4-A-Tempo and 4-D-Tempo, the tested piperidine nitroxides inhibited superoxide anion (O(2*-)) release from neutrophils stimulated by zymosan. The concentration required for inhibiting O(2*-) release was higher than that of inhibiting MDA formation and haemolysis. However, 4-amino-2,2,6,6-tetramethyl piperidine (4-NH2-TempH) and other 4-position substitutes, such as NaN3 and isothiocyanate, had no effects on MDA formation, haemolysis or O(2*-) release. The results indicated that nitroxides have a wide range of scavenging reactive oxygen species (ROS) actions. The nitroxide moiety was the essential group while the 4-position substitutes could influence the activity of nitroxides on scavenging ROS. Topics: Animals; Antioxidants; Cyclic N-Oxides; Dose-Response Relationship, Drug; Erythrocytes; Female; Heart; Hemolysis; In Vitro Techniques; Kidney; Leukocytes; Liver; Male; Malondialdehyde; Mice; Myocardium; Oxidants; Piperidines; Rats; Rats, Wistar; Structure-Activity Relationship | 2006 |
Effects of the anti-allergics astemizole and norastemizole on Fc epsilon RI receptor-mediated signal transduction processes.
The non-sedating anti-allergic drug astemizole, apart from its potential to antagonise H1 receptors, inhibits the release of inflammation mediators from mast cells. To study the mechanism of this inhibition, we investigated the effects of astemizole and one of its active metabolites, norastemizole, on different phases of Fc epsilon RI (the high affinity receptor for the immunoglobulin IgE) receptor-activated signal transduction in rat basophilic leukemia cells (RBL-2H3), leading to exocytosis. Cells were stimulated either through antigen, or thapsigargin, or synergistic combinations of Fc epsilon RI receptor activation with either adenosine A3 receptors or integrins, activated by fibronectin adherence. The effects of the drugs on mediator release, inositol 1,4,5-trisphosphate formation, tyrosine phosphorylation of cellular proteins and Ca2+ fluxes were investigated. Inositol 1,4,5-trisphosphate levels are not affected. Astemizole increased tyrosine phosphorylation in resting cells, especially a 96-kDa protein band. Particularly tyrosine phosphorylation related to post Ca2+ processes is changed after cell triggering in the presence of astemizole. Both drugs inhibit the influx of 45Ca2+, with similar dose response curves as for the inhibition of exocytosis. Astemizole but not norastemizole, when used in resting cells, released Ca2+ from intracellular stores. Astemizole (> 15 microM) also induced exocytosis in resting cells. It did not induce additional changes in its inhibiting effect when cells were triggered with synergistic combinations of Fc epsilon RI receptor activation with either adenosine A3 receptors or integrins. Effects on haemolysis of erythrocytes and differential scanning calorimetry in liposomes showed clear differences in membrane perturbation between astemizole and norastemizole. The observed differences, and the role of membrane perturbation in the action on Ca2+ fluxes, are discussed. Topics: Animals; Anti-Allergic Agents; Astemizole; Benzimidazoles; Calcium; Cell Adhesion; Cell Line; Erythrocyte Membrane; Exocytosis; Fibronectins; Hemolysis; Hypotonic Solutions; Inosine Triphosphate; Piperidines; Protein Tyrosine Phosphatases; Rats; Receptors, IgE; Signal Transduction | 1997 |
Haemagglutinin of influenza A virus is a target for the antiviral effect of Norakin.
The anticholinergic anti-parkinsonism drug Norakin is an inhibitor of influenza virus multiplication. By crossing a Norakin-resistant variant of fowl plague virus (FPV) strain Weybridge with the sensitive FPV/Rostock/34 wild-type virus, Norakin-resistant recombinants were obtained. Analyses of the gene composition showed that all Norakin-resistant recombinants had inherited their haemagglutinin gene from the Norakin-resistant parent strain. The majority of the recombinants had received all the other gene segments from the sensitive parent strain. Norakin was shown to inhibit red blood cell lysis induced either by purified virions or by the haemagglutinin of a sensitive FPV strain at low pH, but failed to affect the Norakin-resistant FPV variant. No aggregation of autoliposomes containing the haemagglutinin of a sensitive FPV strain or digestion of the HA1 subunit of haemagglutinin by trypsin occurred in the presence of Norakin at acid pH. The data suggest that the haemagglutinin of FPV is the target for the antiviral activity of Norakin, which acts by inhibiting the conformational change in the haemagglutinin at acid pH important for lysis. Topics: Animals; Cells, Cultured; Chick Embryo; Drug Resistance, Microbial; Genes, Viral; Hemagglutination; Hemagglutinins, Viral; Hemolysis; Hydrogen-Ion Concentration; In Vitro Techniques; Influenza A virus; Liposomes; Membrane Fusion; Piperidines; Recombination, Genetic; Trypsin; Virus Replication | 1986 |
The anticholinergic anti-Parkinson drug Norakin selectively inhibits influenza virus replication.
Topics: Amantadine; Animals; Antiviral Agents; Biperiden; Cell Line; Chick Embryo; Drug Interactions; Drug Resistance, Microbial; Genes, Viral; Hemagglutination, Viral; Hemolysis; Influenza A virus; Interferon Type I; Interferons; Measles virus; Mutation; Piperidines; Virus Replication | 1985 |
Anticonvulsant activity and monoamine oxidase inhibitory and antihemolytic properties of some newer 4-phenylpiperidino carbamides.
Six 1-[N-acetyl(4-phenylpiperidino)]-3-aryl carbamides were synthesized, characterized and evaluated for their anticonvulsant, monoamine oxidase inhibitory and antihemolytic properties. These compounds (100 mg/kg, i.p.) provided 10--80% protection against pentylenetetrazol-induced seizures in mice. All carbamides (1 mM) inhibited (34--82%) in vitro activity of rat brain monoamine oxidase and provided 18--51% protection against in vitro hypoosmotic hemolysis of human red blood cells at a final concentration of 1 mM. Low toxicity of these carbamides was reflected by their high approximate LD50 values. Topics: Animals; Anticonvulsants; Female; Hemolysis; Humans; In Vitro Techniques; Lethal Dose 50; Male; Membranes; Mice; Monoamine Oxidase Inhibitors; Piperidines; Rats | 1978 |
Porphyrin biosynthesis from prophobilinogen by duck blood hemolysate.
The formation of porphyrins from porphobilinogen by a duck blood hemolysate was examined. The system was found to form mainly protoporphyrin IX and hemin, and accumulated lesser amounts of uroporphyrins, hepatacarboxylic porphyrin, and coproporphyrins. By storage at -20 degrees the accumulation of uroporphyrins and heptacarboxylic porphyrin was increased. Both porphyrins were mainly the type III isomers. By addition of dithiothreitol the porphyrin pattern reversed to the original one formed by the fresh hemolysate. Addition of a number of amines also inhibited the decarboxylating system without affecting the original isomer distribution among the porphyrins. Addition of Fe2+ (3mM) did not affect the porphyrin pattern or the isomer distribution. Addition of Pb2+ (2.5 mM) partially inhibited the decarboxylating system, whereas at higher concentrations (4 mM) it increased the decarboxylation rate of the heptacarboxylic porphyrin. The obtained results are discussed in relation to porphyrin accumulation in porphyria cutanea tarda and in acquired hepatic porphyrias. Topics: Ammonium Chloride; Animals; Cyclohexylamines; Dithiothreitol; Ducks; Erythrocytes; Freezing; Hemolysis; Hydroxylamines; Imidazoles; Piperidines; Porphobilinogen; Porphyrins | 1977 |
Permeation of a spin-label phosphate into the human erythrocyte.
The reduction of spin-labels by human erythrocytes can be used to follow their penetration into these cells. The neutral spin-label alcohol Tempol (4-hydroxy-2,2,6,6-tetramethylpiperidinyl-1-oxyl) diffuses through the membrane very quickly. The membrane is virtually impermeable to the positively charged spin-label Tempo-choline (N,N-dimethyl-N-(2',2',6',6'-tetramethyl-4'-piperidinyl-1-oxyl)-2-hydroxyethylammonium chloride). The negatively charged spin-label Tempo phosphate (4-phospho-2,2,6,6-tetramethylpiperidinyl-l-oxyl) is reduced at 37 degrees, with a half-time of about 1 hr. The reduction occurs internally following the rate-limiting transport of the label across the erythrocyte membrane. Reduction of this spin-label is greatly diminished by the specific inhibitor of anion transport, 4-acetamido-4'-isothiocyanostilbene-2,2'-disulfonic acid (SITS). The rate of transport depends strongly on the transmembrane electrical potential. Topics: Adult; Biological Transport; Cell Membrane Permeability; Cyclic N-Oxides; Electron Spin Resonance Spectroscopy; Erythrocytes; Hemolysis; Humans; Membrane Potentials; Oxidation-Reduction; Phosphates; Piperidines; Spin Labels; Temperature; Time Factors | 1975 |
A new method for the preparation of EAC14 cell with human or guinea-pig serum.
Topics: Acetates; Animals; Calcium; Complement System Proteins; Erythrocytes; Guinea Pigs; Hemolysis; Humans; Immunologic Techniques; Magnesium; Piperidines; Quaternary Ammonium Compounds; Sheep; Temperature | 1974 |
Structure-activity relationships in membrane-perturbing agents. Hemolytic, narcotic, and antibacterial compounds.
Topics: Alcohols; Amides; Animals; Anti-Bacterial Agents; Axons; Benzene Derivatives; Carbamates; Cattle; Cell Membrane; Chemical Phenomena; Chemistry; Depression, Chemical; Dogs; Erythrocytes; Esters; Fatty Acids; Glycerides; Hemolysis; Humans; Hydrogen-Ion Concentration; Indoles; Mathematics; Membrane Potentials; Molecular Biology; Naphthalenes; Narcotics; Phenols; Piperidines; Pyridines; Quaternary Ammonium Compounds; Rabbits; Staphylococcus; Sulfates; Temperature; Thermodynamics | 1971 |
Structure-activity relationships of noreperidine congeners on cholinesterase systems in vitro and analgesia in vivo.
Topics: Analgesia; Analgesics; Animals; Binding Sites; Carboxylic Acids; Chemical Phenomena; Chemistry; Chemistry, Physical; Cholinesterase Inhibitors; Chromatography, Thin Layer; Eels; Erythrocytes; Esters; Hemolysis; Humans; In Vitro Techniques; Kinetics; Mathematics; Mice; Piperidines; Receptors, Drug; Structure-Activity Relationship; Thermodynamics | 1971 |
Detection of chlorpromazine and thioridazine metabolites in human erythrocytes.
Topics: Chlorpromazine; Chromatography, Thin Layer; Erythrocytes; Hemolysis; Humans; Indicators and Reagents; Methods; Phenothiazines; Piperidines; Plasma; Silicon Dioxide; Sulfoxides; Thioridazine; Time Factors | 1969 |
Inactivation of hemolytic activities of serum complement by phenothiazines.
Topics: Animals; Chemical Phenomena; Chemistry; Complement System Proteins; Depression, Chemical; Guinea Pigs; Hemolysis; Humans; Phenothiazines; Piperazines; Piperidines; Promazine; Sheep | 1969 |