Abstract
The physiological collagen receptors integrili α2β1 (previously known as GP Ia/IIa) (α2β1) and glycoprotein VI (GPVI) were identified by analyzing patients’ platelets deficient in one of these proteins. Stimulant-induced platelet activation converts α2β1 to its active form, which can bind tightly to its ligand collagen. Collagen interacts with α2β1 mainly through a Glu residue (part of the receptor-binding sequence GFOGER) that interacts with the MIDAS (metal ion-dependent motif) coordinated divalent cation (Mg2+, physiologically), located in the I domain of the α-subunit of this integrin. GPVI binds more weakly to collagen than activated α2β1, but this interaction is sufficient to initiate a strong signaling cascade to transduce signals, among which tyrosine phosphorylation is the most important, resulting in full platelet activation. GPVI recognizes repeats of the Gly-Pro-hydroxyPro (GPO) sequence in collagen and crosslinking of GPVI induces the initial signaling reaction. Analysis of platelet adhesion and aggregation to a collagen surface under blood flow, which approximates physiological conditions, indicates that α2β1 mainly contributes to the initial adhesion to collagen, and GPVI contributes to large aggregate formation after the initial adhesion. Thus, α2β1 and GPVI have different properties as collagen receptors, and both contribute to physiological platelet plug formation.
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Jung, S.M., Moroi, M. (2008). Platelet Collagen Receptors. In: Tanaka, K., Davie, E.W., Ikeda, Y., Iwanaga, S., Saito, H., Sueishi, K. (eds) Recent Advances in Thrombosis and Hemostasis 2008. Springer, Tokyo. https://doi.org/10.1007/978-4-431-78847-8_15
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DOI: https://doi.org/10.1007/978-4-431-78847-8_15
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