{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ren Q"],"funding":["NHLBI NIH HHS"],"pagination":["24-33"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC1751319"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["18(1)"],"pubmed_abstract":["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, "],"journal":["Molecular biology of the cell"],"pubmed_title":["Endobrevin/VAMP-8 is the primary v-SNARE for the platelet release reaction."],"pmcid":["PMC1751319"],"funding_grant_id":["R01 HL056652","R01 HL091893"],"pubmed_authors":["Karim ZA","Zhao C","Choi W","Crawford GL","Hong W","Barber HK","Wang CC","Ren Q","Whiteheart SW"],"additional_accession":[]},"is_claimable":false,"name":"Endobrevin/VAMP-8 is the primary v-SNARE for the platelet release reaction.","description":"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, ","dates":{"release":"2007-01-01T00:00:00Z","publication":"2007 Jan","modification":"2025-04-07T00:08:05.035Z","creation":"2019-03-27T02:03:09Z"},"accession":"S-EPMC1751319","cross_references":{"pubmed":["17065550"],"doi":["10.1091/mbc.e06-09-0785"]}}