Platelet affinity for burro aorta collagen.
Despite ingenious concepts, there are no unequivocal clues as to what, when, and how some undefined biochemical factor(s) or constituent(s) that localizes in the arterial wall can precipitate a thromboatheromatous lesion or arterial disease. The present study focused on the extraction, partial purification, and characterization of a collagen-active platelet stimulator from the aortas of aged burros. The aggregator moiety in the aorta extracts invariably had a higher affinity for platelets in citrated platelet-rich plasma of human beings than for platelets of homologous burros. The platelet-aggregating factor(s) in the aorta extract was retained by incubation with alpha-chymotrypsin. Platelet-aggregating activity was rapidldy abolished after incubation with collagenase, as determined by plateletaggregometry tests. Evidence based on light microscope and polysaccharide histochemical reactions indicates a probability that the intracellular amorphous matrix (PAS-positive) and filamentous components (PTAH-positive) expelled from smooth muscle cells disrupted during homogenization of the aorta may be a principle source of a precursor collagen species which is a potent inducer of platelet aggregation.
D000818:Animals; D001013:Aorta, Thoracic / Q000032:analysis* / Q000033:anatomy & histology; D002918:Chymotrypsin / Q000378:metabolism; D003094:Collagen / Q000302:isolation & purification / Q000494:pharmacology*; D006736:Horses; D006801:Humans; D003012:Microbial Collagenase / Q000378:metabolism; D010527:Perissodactyla / Q000378:metabolism*; D010974:Platelet Aggregation / Q000187:drug effects*
D003094:Collagen; D002918:Chymotrypsin; D003012:Microbial Collagenase