| pubmed-article:10329959 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10329959 | lifeskim:mentions | umls-concept:C0206131 | lld:lifeskim |
| pubmed-article:10329959 | lifeskim:mentions | umls-concept:C0010853 | lld:lifeskim |
| pubmed-article:10329959 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:10329959 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:10329959 | lifeskim:mentions | umls-concept:C1420269 | lld:lifeskim |
| pubmed-article:10329959 | lifeskim:mentions | umls-concept:C0599781 | lld:lifeskim |
| pubmed-article:10329959 | pubmed:issue | 5 Pt 1 | lld:pubmed |
| pubmed-article:10329959 | pubmed:dateCreated | 1999-6-7 | lld:pubmed |
| pubmed-article:10329959 | pubmed:abstractText | The acute stimulation of glucose uptake by insulin in fat and muscle cells is primarily the result of translocation of facilitative glucose transporter 4 (GLUT-4) from an internal compartment to the plasma membrane. Here, we investigate the role of SNAP23 (a 23-kDa molecule resembling the 25-kDa synaptosome associated protein) in GLUT-4 translocation and glucose uptake in 3T3-L1 adipocytes. Microinjection of a polyclonal antibody directed to the carboxy terminus of SNAP23 inhibited GLUT-4 incorporation into the membrane in response to insulin, whereas microinjection of full-length recombinant SNAP23 enhanced the insulin effect. Introduction of recombinant SNAP23 into chemically permeabilized cells also enhanced insulin-stimulated glucose transport. These results indicate that SNAP23 is required for insulin-dependent, functional incorporation of GLUT-4 into the plasma membrane and that the carboxy terminus of the protein is essential for this process. SNAP23 is therefore likely to be a fusion catalyst along with syntaxin-4 and vesicle-associated membrane protein (VAMP)-2. Furthermore, the endogenous content of SNAP23 appears to be limiting for insulin-dependent GLUT-4 exposure at the cell surface. A measurable fraction of SNAP23 was sedimented with cytoskeletal elements when extracted with Triton X-100, unlike VAMP-2 and syntaxin-4, which were exclusively soluble in detergent. We hypothesize that SNAP23 and its interaction with the cytoskeleton may be targets for regulation of GLUT-4 traffic. | lld:pubmed |
| pubmed-article:10329959 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10329959 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10329959 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10329959 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10329959 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10329959 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10329959 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10329959 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10329959 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10329959 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10329959 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10329959 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10329959 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10329959 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10329959 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10329959 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10329959 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10329959 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10329959 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10329959 | pubmed:month | May | lld:pubmed |
| pubmed-article:10329959 | pubmed:issn | 0002-9513 | lld:pubmed |
| pubmed-article:10329959 | pubmed:author | pubmed-author:KlikJJ | lld:pubmed |
| pubmed-article:10329959 | pubmed:author | pubmed-author:FosterL JLJ | lld:pubmed |
| pubmed-article:10329959 | pubmed:author | pubmed-author:TrimbleW SWS | lld:pubmed |
| pubmed-article:10329959 | pubmed:author | pubmed-author:YaworskyKK | lld:pubmed |
| pubmed-article:10329959 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10329959 | pubmed:volume | 276 | lld:pubmed |
| pubmed-article:10329959 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10329959 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10329959 | pubmed:pagination | C1108-14 | lld:pubmed |
| pubmed-article:10329959 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:10329959 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10329959 | pubmed:articleTitle | SNAP23 promotes insulin-dependent glucose uptake in 3T3-L1 adipocytes: possible interaction with cytoskeleton. | lld:pubmed |
| pubmed-article:10329959 | pubmed:affiliation | Cell Biology Programme, Hospital for Sick Children, Toronto, Ontario M5G 1X8; and Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada M5S 1A8. | lld:pubmed |
| pubmed-article:10329959 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10329959 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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