| pubmed-article:8707843 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8707843 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:8707843 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:8707843 | lifeskim:mentions | umls-concept:C2262706 | lld:lifeskim |
| pubmed-article:8707843 | lifeskim:mentions | umls-concept:C0017742 | lld:lifeskim |
| pubmed-article:8707843 | lifeskim:mentions | umls-concept:C0148340 | lld:lifeskim |
| pubmed-article:8707843 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:8707843 | pubmed:dateCreated | 1996-9-12 | lld:pubmed |
| pubmed-article:8707843 | pubmed:abstractText | Insulin stimulates glucose transport in adipocytes by translocation of the glucose transporter (GLUT-4) from an intracellular site to the cell surface. We have characterized different synaptobrevin/vesicle-associated membrane protein (VAMP) homologues in adipocytes and studied their intracellular distribution with respect to GLUT-4. VAMP-1, VAMP-2, and cellubrevin cDNAs were isolated from a 3T3-L1 adipocyte expression library. VAMP-2 and cellubrevin were: (a) the most abundant isoforms in adipocytes, (b) detectable in all insulin responsive tissues, (c) translocated to the cell surface in response to insulin, and (d) found in immunoadsorbed GLUT-4 vesicles. To further define their intracellular distribution, 3T3-L1 adipocytes were incubated with a transferrin/HRP conjugate (Tf/HRP) and endosomes ablated following addition of DAB and H2O2. While this resulted in ablation of > 90% of the transferrin receptor (TfR) and cellubrevin found in intracellular membranes, 60% of GLUT-4 and 90% of VAMP-2 was not ablated. Immuno-EM on intracellular vesicles from adipocytes revealed that VAMP-2 was colocalized with GLUT-4, whereas only partial colocalization was observed between GLUT-4 and cellubrevin. These studies show that two different v-SNAREs, cellubrevin and VAMP-2, are partially segregated in different intracellular compartments in adipocytes, implying that they may define separate classes of secretory vesicles in these cells. We conclude that a proportion of GLUT-4 is found in recycling endosomes in nonstimulated adipocytes together with cellubrevin and the transferrin receptor. In addition, GLUT-4 and VAMP-2 are selectively enriched in a postendocytic compartment. Further study is required to elucidate the function of this latter compartment in insulin-responsive cells. | lld:pubmed |
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| pubmed-article:8707843 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8707843 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8707843 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8707843 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:8707843 | pubmed:issn | 0021-9525 | lld:pubmed |
| pubmed-article:8707843 | pubmed:author | pubmed-author:GouldG WGW | lld:pubmed |
| pubmed-article:8707843 | pubmed:author | pubmed-author:MartinSS | lld:pubmed |
| pubmed-article:8707843 | pubmed:author | pubmed-author:SlotJ WJW | lld:pubmed |
| pubmed-article:8707843 | pubmed:author | pubmed-author:JamesD EDE | lld:pubmed |
| pubmed-article:8707843 | pubmed:author | pubmed-author:LivingstoneCC | lld:pubmed |
| pubmed-article:8707843 | pubmed:author | pubmed-author:TellamJJ | lld:pubmed |
| pubmed-article:8707843 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8707843 | pubmed:volume | 134 | lld:pubmed |
| pubmed-article:8707843 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8707843 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8707843 | pubmed:pagination | 625-35 | lld:pubmed |
| pubmed-article:8707843 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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