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• W1567677323 endingPage "66" @default.
• W1567677323 startingPage "31" @default.
• W1567677323 abstract "This chapter explores the platelet surface receptors involved in adhesion and their structure/function relationships. Platelets contain a wide variety of membrane glycoproteins many of that are critical for adhesion or aggregation. Studies have pointed to the importance of the von Willebrand factor (vWf)/GPIb axis as critical for platelet adhesion at high shear as found in capillaries or in larger vessels under atherosclerotic conditions. The glycoprotein (GP) Ib-V-IX complex consists of four chains each coded by separate genes present on different chromosomes. GPIb contains GPIba and GPIbP linked by a disulfide bond while GPIX is strongly non-covalently associated in a 1:1 ratio and GPV weakly non-covalently associated with the complex in a 1 :2 ratio. The structure of vWf is also broadly known although many of the details remain to be determined. It has been known for some time that the A1 domain contains sites for GPIb, collagen, and heparin interactions and more recent studies of sequence mutants, Type IIb von Willebrand's disease, the effects of glycosylation and differences with animal vWf have narrowed down the GPIb binding site to a disulfide loop formed by a cysteine bridge and neighboring sequences. The fact that a collagen-binding site is in close proximity supports the idea that conformational changes in the GPIb-binding site are probably induced by collagen-binding." @default.
• W1567677323 created "2016-06-24" @default.
• W1567677323 creator A5006904490 @default.
• W1567677323 date "1997-01-01" @default.
• W1567677323 modified "2023-09-26" @default.
• W1567677323 title "Platelet Adhesion Receptors" @default.
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