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- W2015713712 abstract "Platelets function by secreting components necessary for primary clot formation. This report describes an in vitro assay that measures α-granule secretion. Using permeabilized platelets, it is possible to recreate Ca2+-stimulated release of platelet factor 4 (PF4) that is ATP- and temperature-dependent. Though other divalent cations can replace Ca2+ (i.e., Sr2+, Mn2+, Zn2+), there is no effect of Ba2+. Analysis by electron microscopy indicates that the in vitro assay also mimics the cytoskeletal rearrangements and granule centralization that occurs upon platelet activation in vivo. Antibody inhibition studies show that PF4 release requires the general membrane fusion protein N-ethylmaleimide-sensitive factor (NSF) and well as the target membrane SNAP receptors (t-SNAREs), syntaxin 2, 4, and SNAP-23. As shown by electron microscopy, the anti-t-SNARE antibodies block granule to target membrane fusion. This finding is unique in that it is the first report of a role for two syntaxins in the same exocytosis event." @default.
- W2015713712 created "2016-06-24" @default.
- W2015713712 creator A5028622382 @default.
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- W2015713712 date "2000-01-01" @default.
- W2015713712 modified "2023-09-28" @default.
- W2015713712 title "Molecular Mechanisms of Platelet Exocytosis: Requirements for α-Granule Release" @default.
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- W2015713712 doi "https://doi.org/10.1006/bbrc.1999.2039" @default.
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