Comparison of fibrinogen association with normal and thrombasthenic platelets on exposure to ADP or chymotrypsin.
Although 125I-fibrinogen becomes associated with washed platelets from normal human subjects during ADP-induced shape change and aggregation, 125I-fibrinogen did not become associated with washed plateletes from a thrombasthenic subject during ADP-induced shape change and the platelets did not aggregate. Platelets from control and thrombasthenic subjects were treated with chymotrypsin, which is known to degrade platelet membrane glycoproteins. More 125I-fibrinogen became associated with chymotrypsin-pretreated platelets from normal subejcts than with untreated platelets, and fibrinogen caused the enzyme-treated platelets to aggregate. 125I-fibrinogen did not become associated with chymotrypsin-pretreated thromobasthenic platelets, and fibrinogen did not aggregate them. Thus, there appears to be a defect in thrombasthenic platelets that prevents the association of fibrinogen with them.
D000244:Adenosine Diphosphate / Q000494:pharmacology*; D001791:Blood Platelet Disorders / Q000503:physiopathology*; D001792:Blood Platelets / Q000502:physiology*; D002918:Chymotrypsin / Q000494:pharmacology*; D003094:Collagen / Q000494:pharmacology; D005340:Fibrinogen / Q000378:metabolism; D006801:Humans; D007457:Iodine Radioisotopes; D010974:Platelet Aggregation; D012701:Serotonin / Q000378:metabolism; D013917:Thrombin / Q000494:pharmacology
D007457:Iodine Radioisotopes; D012701:Serotonin; D000244:Adenosine Diphosphate; D005340:Fibrinogen; D003094:Collagen; D002918:Chymotrypsin; D013917:Thrombin