High molecular weight kininogen binds to unstimulated platelets.
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چکیده
منابع مشابه
High molecular weight kininogen binds to unstimulated platelets.
Studies were performed to determine if the unstimulated platelet membrane has a site for high molecular weight kininogen (HMWK) binding. 125I-HMWK bound to unstimulated platelets. Zn++ was required for 125I-HMWK binding to unstimulated platelets and binding was maximal at 50 microM Zn++. Neither Mg++ nor Ca++ substituted for Zn++ in supporting 125I-HMWK binding to unstimulated platelets, and ne...
متن کاملHigh Molecular Weight Kininogen : Localization in the Unstimulated and Activated Platelet
High mol wt kininogen (HMWK), the major cofactorsubstrate of the contact phase of coagulation, is contained within and secreted by platelets. Studies have been performed to localize platelet HMWK in both the unstimulated and activated platelet and to ascertain the effect of platelet enzymes on HMWK itself. On platelet subcellular fractionation, platelet HMWK was localized to a-granules, and pla...
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Fibrinogen inhibited ~25I-high molecular weight kininogen (HMWK) binding and displaced bound J25I-HMWK from neutrophils. Studies were performed to determine whether fibrinogen could bind to human neutrophils and to describe the HMWK-fibrinogen interaction on cellular surfaces. At 4°C, the binding of ~2H-fibrinogen to neutrophils reached a plateau by 30 min and did not decrease. At 23 and 37°C, ...
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Fibrinogen inhibited 125I-high molecular weight kininogen (HMWK) binding and displaced bound 125I-HMWK from neutrophils. Studies were performed to determine whether fibrinogen could bind to human neutrophils and to describe the HMWK-fibrinogen interaction on cellular surfaces. At 4 degrees C, the binding of 125I-fibrinogen to neutrophils reached a plateau by 30 min and did not decrease. At 23 a...
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ژورنال
عنوان ژورنال: Journal of Clinical Investigation
سال: 1986
ISSN: 0021-9738
DOI: 10.1172/jci112567