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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2004-9-14
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pubmed:abstractText |
Despite our general understanding that members of the SNARE superfamily participate in diverse intracellular docking/fusion events, the physiological role of the majority of SNAREs in the intact organism remains elusive. In this study, through targeted gene knockout in mice, we establish that VAMP8/endobrevin is a major player in regulated exocytosis of the exocrine pancreas. VAMP8 is enriched on the membrane of zymogen granules and exists in a complex with syntaxin 4 and SNAP-23. VAMP8-/- mice developed normally but showed severe defects in the pancreas. VAMP8 null acinar cells contained three times more zymogen granules than control acinar cells. Furthermore, secretagogue-stimulated secretion was abolished in pancreatic fragments derived from VAMP8-/- mice. In addition, VAMP8-/- mice were partially resistant to supramaximal caerulein-induced pancreatitis. These results suggest a major physiological role of VAMP8 in regulated exocytosis of pancreatic acinar cells by serving as a v-SNARE of zymogen granules.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amylases,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Qa-SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Qb-SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Qc-SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/R-SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SNAP23 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Snap23 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Vamp8 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1534-5807
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
359-71
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pubmed:dateRevised |
2009-9-28
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pubmed:meshHeading |
pubmed-meshheading:15363411-Amylases,
pubmed-meshheading:15363411-Animals,
pubmed-meshheading:15363411-Blotting, Western,
pubmed-meshheading:15363411-Carrier Proteins,
pubmed-meshheading:15363411-Cell Division,
pubmed-meshheading:15363411-Cells, Cultured,
pubmed-meshheading:15363411-Endocytosis,
pubmed-meshheading:15363411-Exocytosis,
pubmed-meshheading:15363411-Fibroblasts,
pubmed-meshheading:15363411-Genotype,
pubmed-meshheading:15363411-Glutathione Transferase,
pubmed-meshheading:15363411-Immunohistochemistry,
pubmed-meshheading:15363411-Liver,
pubmed-meshheading:15363411-Membrane Proteins,
pubmed-meshheading:15363411-Mice,
pubmed-meshheading:15363411-Mice, Knockout,
pubmed-meshheading:15363411-Mice, Transgenic,
pubmed-meshheading:15363411-Microscopy, Fluorescence,
pubmed-meshheading:15363411-Models, Genetic,
pubmed-meshheading:15363411-Pancreas,
pubmed-meshheading:15363411-Pancreatitis,
pubmed-meshheading:15363411-Precipitin Tests,
pubmed-meshheading:15363411-Qa-SNARE Proteins,
pubmed-meshheading:15363411-Qb-SNARE Proteins,
pubmed-meshheading:15363411-Qc-SNARE Proteins,
pubmed-meshheading:15363411-R-SNARE Proteins,
pubmed-meshheading:15363411-SNARE Proteins,
pubmed-meshheading:15363411-Time Factors,
pubmed-meshheading:15363411-Vesicular Transport Proteins
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pubmed:year |
2004
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pubmed:articleTitle |
A role of VAMP8/endobrevin in regulated exocytosis of pancreatic acinar cells.
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pubmed:affiliation |
Membrane Biology Laboratory, Institute of Molecular and Cell Biology, Proteos, 61 Biopolis Drive, Singapore 138673, Singapore.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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