Alterations of blood platelet function induced by neutral proteases from human leukocytes.
Washed human platelets are damaged by two neutral proteases from human leukocytes (elastase-like protease, ELP and chymotrypsin-like protease, CLP). The damage is manifested as inhibited aggregation by ristocetin and collagen, and enhanced aggregation by ADP in the presence of fibrinogen. Similarly to alpha-chymotrypsin (alpha-CT), CLP also increases binding of 125I-fibrinogen to platelets and renders platelets aggregable by human fibrinogen. ELP is less effective in this respect possibly due to damage to platelet receptors for fibrinogen. In the plasma medium platelets are not sensitive to leukocytic proteases added at concentrations that provoke some prolongation of the time of plasma clotting by thrombin.
D000244:Adenosine Diphosphate / Q000494:pharmacology; D001792:Blood Platelets / Q000187:drug effects*; D002918:Chymotrypsin / Q000494:pharmacology; D003094:Collagen / Q000494:pharmacology; D005340:Fibrinogen / Q000494:pharmacology; D006801:Humans; D066298:In Vitro Techniques; D007962:Leukocytes / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000494:pharmacology; D010447:Peptide Hydrolases / Q000097:blood / Q000494:pharmacology*; D010974:Platelet Aggregation / Q000187:drug effects; D012310:Ristocetin / Q000494:pharmacology
D012310:Ristocetin; D000244:Adenosine Diphosphate; D005340:Fibrinogen; D003094:Collagen; D010447:Peptide Hydrolases; D002918:Chymotrypsin; D010196:Pancreatic Elastase