SNAP23 Regulates Endothelial Exocytosis of von Willebrand Factor
Endothelial exocytosis regulates vascular thrombosis and inflammation. The trafficking and release of endothelial vesicles is mediated by SNARE (Soluble NSF Attachment protein REceptors) molecules, but the exact identity of endothelial SNAREs has been unclear. Three SNARE molecules form a ternary co...
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description | Endothelial exocytosis regulates vascular thrombosis and inflammation. The trafficking and release of endothelial vesicles is mediated by SNARE (Soluble NSF Attachment protein REceptors) molecules, but the exact identity of endothelial SNAREs has been unclear. Three SNARE molecules form a ternary complex, including isoforms of the syntaxin (STX), vesicle-associated membrane protein (VAMP), and synaptosomal-associated protein (SNAP) families. We now identify SNAP23 as the predominant endothelial SNAP isoform that mediates endothelial exocytosis of von Willebrand Factor (VWF). SNAP23 was localized to the plasma membrane. Knockdown of SNAP23 decreased endothelial exocytosis, suggesting it is important for endothelial exocytosis. SNAP23 interacted with the endothelial exocytic machinery, and formed complexes with other known endothelial SNARE molecules. Taken together, these data suggest that SNAP23 is a key component of the endothelial SNARE machinery that mediates endothelial exocytosis. |
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The trafficking and release of endothelial vesicles is mediated by SNARE (Soluble NSF Attachment protein REceptors) molecules, but the exact identity of endothelial SNAREs has been unclear. Three SNARE molecules form a ternary complex, including isoforms of the syntaxin (STX), vesicle-associated membrane protein (VAMP), and synaptosomal-associated protein (SNAP) families. We now identify SNAP23 as the predominant endothelial SNAP isoform that mediates endothelial exocytosis of von Willebrand Factor (VWF). SNAP23 was localized to the plasma membrane. Knockdown of SNAP23 decreased endothelial exocytosis, suggesting it is important for endothelial exocytosis. SNAP23 interacted with the endothelial exocytic machinery, and formed complexes with other known endothelial SNARE molecules. Taken together, these data suggest that SNAP23 is a key component of the endothelial SNARE machinery that mediates endothelial exocytosis.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0118737</identifier><identifier>PMID: 26266817</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Animals ; Autophagy ; Cell death ; Cell Membrane - metabolism ; Endothelial Cells - metabolism ; Endothelium ; Exocytosis ; Gene Expression ; Human Umbilical Vein Endothelial Cells ; Humans ; Isoforms ; Laboratory animals ; Machinery and equipment ; Medicine ; Membrane proteins ; Mice ; Molecular chains ; Neurosciences ; Plasma ; Polyclonal antibodies ; Protein Binding ; Protein Transport ; Proteins ; Proteomics ; Qb-SNARE Proteins - genetics ; Qb-SNARE Proteins - metabolism ; Qc-SNARE Proteins - genetics ; Qc-SNARE Proteins - metabolism ; Receptors ; SNAP receptors ; Syntaxin ; Thromboembolism ; Thrombosis ; Von Willebrand factor ; von Willebrand Factor - metabolism</subject><ispartof>PloS one, 2015-08, Vol.10 (8), p.e0118737-e0118737</ispartof><rights>COPYRIGHT 2015 Public Library of Science</rights><rights>2015 Zhu et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2015 Zhu et al 2015 Zhu et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c692t-10c03ce48668e7f0c2f343004aa0b1aa6e1fe9e435b105a698763226b43037303</citedby><cites>FETCH-LOGICAL-c692t-10c03ce48668e7f0c2f343004aa0b1aa6e1fe9e435b105a698763226b43037303</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4534191/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4534191/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,729,782,786,866,887,2104,2930,23873,27931,27932,53798,53800</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26266817$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Bishopric, Nanette H</contributor><creatorcontrib>Zhu, Qiuyu Martin</creatorcontrib><creatorcontrib>Zhu, Qiuyu</creatorcontrib><creatorcontrib>Yamakuchi, Munekazu</creatorcontrib><creatorcontrib>Lowenstein, Charles J</creatorcontrib><title>SNAP23 Regulates Endothelial Exocytosis of von Willebrand Factor</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Endothelial exocytosis regulates vascular thrombosis and inflammation. The trafficking and release of endothelial vesicles is mediated by SNARE (Soluble NSF Attachment protein REceptors) molecules, but the exact identity of endothelial SNAREs has been unclear. Three SNARE molecules form a ternary complex, including isoforms of the syntaxin (STX), vesicle-associated membrane protein (VAMP), and synaptosomal-associated protein (SNAP) families. We now identify SNAP23 as the predominant endothelial SNAP isoform that mediates endothelial exocytosis of von Willebrand Factor (VWF). SNAP23 was localized to the plasma membrane. Knockdown of SNAP23 decreased endothelial exocytosis, suggesting it is important for endothelial exocytosis. SNAP23 interacted with the endothelial exocytic machinery, and formed complexes with other known endothelial SNARE molecules. Taken together, these data suggest that SNAP23 is a key component of the endothelial SNARE machinery that mediates endothelial exocytosis.</description><subject>Animals</subject><subject>Autophagy</subject><subject>Cell death</subject><subject>Cell Membrane - metabolism</subject><subject>Endothelial Cells - metabolism</subject><subject>Endothelium</subject><subject>Exocytosis</subject><subject>Gene Expression</subject><subject>Human Umbilical Vein Endothelial Cells</subject><subject>Humans</subject><subject>Isoforms</subject><subject>Laboratory animals</subject><subject>Machinery and equipment</subject><subject>Medicine</subject><subject>Membrane proteins</subject><subject>Mice</subject><subject>Molecular chains</subject><subject>Neurosciences</subject><subject>Plasma</subject><subject>Polyclonal antibodies</subject><subject>Protein Binding</subject><subject>Protein Transport</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>Qb-SNARE Proteins - genetics</subject><subject>Qb-SNARE Proteins - metabolism</subject><subject>Qc-SNARE Proteins - genetics</subject><subject>Qc-SNARE Proteins - metabolism</subject><subject>Receptors</subject><subject>SNAP receptors</subject><subject>Syntaxin</subject><subject>Thromboembolism</subject><subject>Thrombosis</subject><subject>Von Willebrand factor</subject><subject>von Willebrand Factor - metabolism</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNqNkl1v0zAUhiMEYmPwDxBEQkJw0eKPxEluJqqpg0oTQxsfl9aJc9x6cuMSO9P273HXbGrQLpBl2Tp-znt87DdJXlMypbygn65c37VgpxvX4pRQWha8eJIc0oqziWCEP93bHyQvvL8iJOelEM-TAyaYECUtDpPPl99m3xlPL3DZWwjo03nbuLBCa8Cm8xunboPzxqdOp9euTX8ba7HuoG3SU1DBdS-TZxqsx1fDepT8PJ3_OPk6OTv_sjiZnU2UqFiYUKIIV5jF-iUWmiimecYJyQBITQEEUo0VZjyvKclBVGUhOGOijhAv4jxK3u50N9Z5OTTvJS0Iz0uaVzwSix3ROLiSm86sobuVDoy8C7huKaELRlmUjah1SXWR1znJqqYqCdBaaQRSaSKUjlrHQ7W-XmOjsA0d2JHo-KQ1K7l01zLLeUYrGgU-DAKd-9OjD3JtvEJroUXX39079ho_kkX03T_o490N1BJiA6bVLtZVW1E5y1jOKeWiiNT0ESqOBtdGRadoE-OjhI-jhMgEvAlL6L2Xi8uL_2fPf43Z93vsCsGGlXe2D8a1fgxmO1B1zvsO9cMjUyK3Rr9_Dbk1uhyMHtPe7H_QQ9K9s_lfiST1kA</recordid><startdate>20150812</startdate><enddate>20150812</enddate><creator>Zhu, Qiuyu Martin</creator><creator>Zhu, Qiuyu</creator><creator>Yamakuchi, Munekazu</creator><creator>Lowenstein, Charles J</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20150812</creationdate><title>SNAP23 Regulates Endothelial Exocytosis of von Willebrand Factor</title><author>Zhu, Qiuyu Martin ; Zhu, Qiuyu ; Yamakuchi, Munekazu ; Lowenstein, Charles J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c692t-10c03ce48668e7f0c2f343004aa0b1aa6e1fe9e435b105a698763226b43037303</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Animals</topic><topic>Autophagy</topic><topic>Cell death</topic><topic>Cell Membrane - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DAOJ: Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhu, Qiuyu Martin</au><au>Zhu, Qiuyu</au><au>Yamakuchi, Munekazu</au><au>Lowenstein, Charles J</au><au>Bishopric, Nanette H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>SNAP23 Regulates Endothelial Exocytosis of von Willebrand Factor</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2015-08-12</date><risdate>2015</risdate><volume>10</volume><issue>8</issue><spage>e0118737</spage><epage>e0118737</epage><pages>e0118737-e0118737</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Endothelial exocytosis regulates vascular thrombosis and inflammation. The trafficking and release of endothelial vesicles is mediated by SNARE (Soluble NSF Attachment protein REceptors) molecules, but the exact identity of endothelial SNAREs has been unclear. Three SNARE molecules form a ternary complex, including isoforms of the syntaxin (STX), vesicle-associated membrane protein (VAMP), and synaptosomal-associated protein (SNAP) families. We now identify SNAP23 as the predominant endothelial SNAP isoform that mediates endothelial exocytosis of von Willebrand Factor (VWF). SNAP23 was localized to the plasma membrane. Knockdown of SNAP23 decreased endothelial exocytosis, suggesting it is important for endothelial exocytosis. SNAP23 interacted with the endothelial exocytic machinery, and formed complexes with other known endothelial SNARE molecules. Taken together, these data suggest that SNAP23 is a key component of the endothelial SNARE machinery that mediates endothelial exocytosis.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>26266817</pmid><doi>10.1371/journal.pone.0118737</doi><oa>free_for_read</oa></addata></record> |
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subjects | Animals Autophagy Cell death Cell Membrane - metabolism Endothelial Cells - metabolism Endothelium Exocytosis Gene Expression Human Umbilical Vein Endothelial Cells Humans Isoforms Laboratory animals Machinery and equipment Medicine Membrane proteins Mice Molecular chains Neurosciences Plasma Polyclonal antibodies Protein Binding Protein Transport Proteins Proteomics Qb-SNARE Proteins - genetics Qb-SNARE Proteins - metabolism Qc-SNARE Proteins - genetics Qc-SNARE Proteins - metabolism Receptors SNAP receptors Syntaxin Thromboembolism Thrombosis Von Willebrand factor von Willebrand Factor - metabolism |
title | SNAP23 Regulates Endothelial Exocytosis of von Willebrand Factor |
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