Human neutrophil elastase modulates platelet function by limited proteolysis of membrane glycoproteins.
نویسندگان
چکیده
منابع مشابه
Human Neutrophil Elastase Modulates Platelet Function
During blood coagulation human polymorphonuclear leukocytes release elastase in amounts that can exceed 100 nmol/liter. We therefore studied the effect of elastase on platelet structure and function. Physiologic concentrations of elastase specifically inhibited thrombin-induced platelet aggregation and ristocetininduced agglutination of washed platelets in a timeand dosedependent manner. This w...
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Human neutrophil and Pseudomonas aeruginosa elastases were compared for their ability to degrade hog gastric mucin, which was used as a model substrate. P. aeruginosa elastase was more active than neutrophil elastase, and 2 to 10 peptide bonds were hydrolyzed within 5 min. The results demonstrate that both elastases degrade mucins actively at concentrations comparable to physiological levels of...
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During blood coagulation. polymorphonuclear leukocytes release elastase in amounts that can exceed 100 nmol/L. We therefore studied the interaction between human leukocyte elastase and human a-thrombin. Elastase cleaved the thrombin B chain (Ala 1 50-Asn 1 51 ) near the “y-cleavage site, resulting in two fragments held together by noncovalent interactions. The NH2-terminal fragment (Fl). mol wt...
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Glycoproteins I Ib / I I Ia form a Ca2+-dependent complex that functions as the fibrinogen receptor on human platelets (1). Several reports have indicated that this fibrinogen receptor is also expressed on the surface of human monocytes (2-4). Of three monoclonal antibodies directed against platelet I Ib/ I I Ia , two were reported to give a positive reaction with monocytes as well (4). Other i...
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Inflammatory mouse peritoneal macrophages secrete a metalloproteinase that is not inhibited by alpha 1-proteinase inhibitor. This proteinase, macrophage elastase, recognizes alpha 1-proteinase inhibitor with macrophage elastase does not involve a stable proteinase-inhibitor complex and results in the proteolytic removal of a peptide of apparent molecular weight 4,000-5,000 from the inhibitor. A...
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ژورنال
عنوان ژورنال: Journal of Clinical Investigation
سال: 1985
ISSN: 0021-9738
DOI: 10.1172/jci111744