A mechanism of erythrocyte lysis by lysophosphatidylcholine.
Lysophosphatidylcholine micelles liberate several cell surface polypeptides from erythrocyte membranes, inducing a sodium-selective permeability defect which leads to colloid osmotic lysis. Evidence is presented to support the hypothesis that at the lowest lytic lysophospholipid concentrations, selective disruption of membrane protein function, rather than gross structural reorganization of the membrane, is the primary lytic mechanism.
D000110:Acetylcholinesterase / Q000097:blood; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000648:ultrastructure*; D004912:Erythrocytes / Q000201:enzymology / Q000648:ultrastructure*; D006461:Hemolysis / Q000187:drug effects*; D006801:Humans; D007700:Kinetics; D008244:Lysophosphatidylcholines / Q000494:pharmacology*; D008565:Membrane Proteins / Q000097:blood; D008823:Micelles; D013395:Sucrose / Q000494:pharmacology; D013779:Tetrodotoxin / Q000494:pharmacology
D008244:Lysophosphatidylcholines; D008565:Membrane Proteins; D008823:Micelles; D013779:Tetrodotoxin; D013395:Sucrose; D000110:Acetylcholinesterase