Sentence examples for major platelet integrin from inspiring English sources
PKCδ is tyrosine phosphorylated at two distinct sites, Tyr311 and 565, in response to activation of GPVI and PAR receptors, but not by the major platelet integrin, αIIbβ3 [11], [12], [13], [13].
The levels of the two collagen receptors, GPVI and α2β1, and the major platelet integrin, αIIbβ3, were similar in the PKCε-null and litter-matched control platelets (Fig 5C).
(2) CD148 plays a critical role in signaling through GPVI and the major platelet integrin, αIIbβ3.
αIIb exclusively associates with β3 to form the major platelet integrin αIIbβ3 (gpIIb/IIIa or CD41/CD61).
These similar phenotypes appear to be due to impaired signalling by the major platelet integrin αIIbβ3, but their weak nature suggests functional redundancy between tetraspanins.
Platelet activation by thrombin induces increased cell-surface expression of the major platelet integrin αIIbβ3, which binds and assembles FN via a fibrin-independent mechanism [ 38- 44].
Therefore it seems unlikely that the major platelet glycoproteins, such as integrin αIIbβ3 (80000 copies) [ 35] or GPIb-IX-V (25000 copies) [ 36], would be direct binding partners for Tspan9.
This is comparable with the level of the collagen receptor integrin, α2β1, and approximately 75% of that of GPVI, measured using the same assay, but is substantially lower than integrin αIIbβ3, the major platelet glycoprotein at more than 80 000 copies.
The major platelet receptors involved in this process are the von Willebrand factor (vWF) receptor GP glycoprotein Ib/IX/V, the collagen integrin receptor α2β1, and the fibrinogen integrin receptor αIIBβ3 (Fig. 1a).
The glycosaminoglycan heparin has been shown to bind to platelet integrin αIIbβ3 and induce platelet activation and aggregation, although the relationship between binding and activation is unclear.
Vesicles bearing reconstituted blood platelet integrin receptors αIIbβ3 were spread on ultrathin films of cellulose, forming continuous supported membranes.
