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A more recent version of this article appeared on January 1, 2007 Originally published as MBC in Press, 10.1091/mbc.E06-09-0785 on October 25, 2006
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Submitted on September 5, 2006
Revised on October 5, 2006
Accepted on October 16, 2006
*Department of Molecular and Cellular Biochemistry, University of Kentucky College of Medicine, Lexington, KY 40536; Membrane Biology Laboratory, Institute of Molecular and Cellular Biology, Proteos, Singapore 138673, Singapore
Monitoring Editor: Sean Munro
Platelet secretion is critical to hemostasis. Release of granular cargo is mediated by Soluble NSF Attachment Protein Receptors (SNAREs); but, despite consensus on t-SNAREs usage, it is unclear which Vesicle Associated Membrane Protein (VAMPs: synaptobrevin/VAMP-2, cellubrevin/VAMP-3, TI-VAMP/VAMP-7, and endobrevin/VAMP-8) is required. We demonstrate that VAMP-8 is required for release from dense core granules, alpha granules, and lysosomes. Platelets from VAMP-8-/- mice have a significant defect in agonist-induced secretion, though signaling, morphology, and cargo levels appear normal. In contrast, VAMP-2+/-, VAMP-3-/-, and VAMP-2+/-/VAMP-3-/- platelets showed no defect. Consistently, Tetanus toxin had no effect on secretion from permeabilized mouse VAMP-3-/- platelets or human platelets, despite cleavage of VAMP-2 and/or -3. Tetanus toxin does block the residual release from permeabilized VAMP-8-/- platelets suggesting a secondary role for VAMP-2 and/or -3. These data imply a ranked redundancy of v-SNARE usage in platelets and suggest that VAMP-8-/- mice will be a useful in vivo model to study platelet exocytosis in hemostasis and vascular inflammation.
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