title: Chemical modification of cytoskeletal proteins of human blood platelets by diamide.
abstract: Incubation of human blood platelets with diamide (azo-dicarboxylic acid-bis-dimethylamide, DIA) influences the aggregation behaviour considerably. Depending on concentration and incubation time DIA induces a reversible aggregation or brings about complete inhibition. The effect is reversible and may be due to the regeneration of reduced glutathione (GSH) which will be oxidized to GSSG by DIA. DIA causes disulfide-linked polymer formation of certain cytoskeletal proteins. At least three polymer families (Pa, Pb, Pc) with different molecular weights are formed depending on dosage and incubation time of DIA. The appearance of a double band in Pa correlates with reversible aggregation, the formation of Pc is always accompanied by a complete inhibition of aggregation. A disturbance of cytoskeleton-membrane interaction by polymer formation can be assumed. GSH serves as a reductant of disulfide-linked polymers whereby a direct link between the maintenance of SH/SS status of platelets and GSH can be established.
mesh_terms: D001391:Azo Compounds / Q000494:pharmacology*; D001792:Blood Platelets / Q000187:drug effects* / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000097:blood*; D003958:Diamide / Q000494:pharmacology*; D004220:Disulfides / Q000097:blood; D005978:Glutathione / Q000097:blood; D006801:Humans; D066298:In Vitro Techniques; D010974:Platelet Aggregation / Q000187:drug effects; D011108:Polymers / Q000378:metabolism
chemical_list: D001391:Azo Compounds; D003598:Cytoskeletal Proteins; D004220:Disulfides; D011108:Polymers; D003958:Diamide; D005978:Glutathione