Platelet Activation Through Membrane Glycoprotein VI
نویسندگان
چکیده
منابع مشابه
Variation in human platelet glycoprotein VI content modulates glycoprotein VI-specific prothrombinase activity.
- Glycoprotein VI (GPVI) is a platelet-specific receptor for collagen that figures prominently in signal transduction. An addition to binding to type I and III collagens, GPVI is also bound specifically by collagen-related peptide and convulxin (CVX), a snake venom protein. We developed a quantitative assay of platelet GPVI in which biotin-conjugated CVX binds selectively to GPVI in separated t...
متن کاملLigand binding rapidly induces disulfide-dependent dimerization of glycoprotein VI on the platelet plasma membrane.
Thrombus formation in hemostasis or thrombotic disease is initiated by adhesion of circulating platelets to damaged blood vessel walls. Exposed subendothelial collagen interacting with platelet glycoprotein (GP) VI leads to platelet activation and integrin alpha(IIb)beta(3)-mediated aggregation. We previously showed that ligand binding to GPVI also induces metalloproteinase-dependent shedding, ...
متن کاملNovel platelet membrane glycoprotein VI dimorphism is a risk factor for myocardial infarction.
BACKGROUND Glycoprotein (GP) VI plays a crucial role in platelet activation and aggregation. We investigated whether polymorphic variation at the GP VI locus confers an increased risk of myocardial infarction (MI). METHODS AND RESULTS Coding and 5' and 3' non-coding regions of the GP VI gene were analyzed by polymerase chain reaction and conformation sensitive gel electrophoresis in 21 health...
متن کاملChanges in the platelet membrane glycoprotein IIb.IIIa complex during platelet activation.
Platelet activation is accompanied by the appearance on the platelet surface of approximately 45,000 receptor sites for fibrinogen. The binding of fibrinogen to these receptors is required for platelet aggregation. Although it is established that the fibrinogen receptor is localized to a heterodimer complex of the membrane glycoproteins, IIb and IIIa, little is known about the changes in this c...
متن کاملEvidence of a role for SHP-1 in platelet activation by the collagen receptor glycoprotein VI.
The Src homology (SH)2 domain-containing protein-tyrosine phosphatase SHP-1 is tyrosine phosphorylated in platelets in response to the glycoprotein VI (GPVI)-selective agonist collagen-related peptide (CRP), collagen, and thrombin. Two major unidentified tyrosine-phosphorylated bands of 28 and 32 kDa and a minor band of 130 kDa coprecipitate with SHP-1 in response to all three agonists. Additio...
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ژورنال
عنوان ژورنال: Japanese Journal of Thrombosis and Hemostasis
سال: 1996
ISSN: 1880-8808,0915-7441
DOI: 10.2491/jjsth.7.251