| pubmed-article:1881918 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1881918 | lifeskim:mentions | umls-concept:C1335837 | lld:lifeskim |
| pubmed-article:1881918 | lifeskim:mentions | umls-concept:C1705603 | lld:lifeskim |
| pubmed-article:1881918 | lifeskim:mentions | umls-concept:C0206131 | lld:lifeskim |
| pubmed-article:1881918 | lifeskim:mentions | umls-concept:C0205102 | lld:lifeskim |
| pubmed-article:1881918 | lifeskim:mentions | umls-concept:C0017742 | lld:lifeskim |
| pubmed-article:1881918 | lifeskim:mentions | umls-concept:C1264638 | lld:lifeskim |
| pubmed-article:1881918 | lifeskim:mentions | umls-concept:C0243102 | lld:lifeskim |
| pubmed-article:1881918 | pubmed:issue | 17 | lld:pubmed |
| pubmed-article:1881918 | pubmed:dateCreated | 1991-10-3 | lld:pubmed |
| pubmed-article:1881918 | pubmed:abstractText | Previous studies indicated that the erythroidtype (GLUT1) glucose transporter isoform contributes to basal but not insulin-stimulated hexose transport in mouse 3T3-L1 adipocytes. In the present studies it was found that basal hexose uptake in 3T3-L1 adipocytes was about 50% lower than that in 3T3-L1 or CHO-K1 fibroblasts. Intrinsic catalytic activities of GLUT1 transporters in CHO-K1 and 3T3-L1 cells were compared by normalizing these hexose transport rates to GLUT1 content on the cell surface, as measured by two independent methods. Cell surface GLUT1 levels in 3T3-L1 fibroblasts and adipocytes were about 10- and 25-fold higher, respectively, than in CHO-K1 fibroblasts, as assessed with an anti-GLUT1 exofacial domain antiserum, delta. The large excess of cell surface GLUT1 transporters in 3T3-L1 adipocytes relative to CHO-K1 fibroblasts was confirmed by GLUT1 protein immunoblot analysis and by photoaffinity labelling (with 3-[125I]iodo-4-azidophenethylamido-7-O-succinyldeacetylforskoli n) of glucose transporters in isolated plasma membranes. Thus, GLUT1 intrinsic activity is markedly reduced in 3T3-L1 fibroblasts compared with the CHO-K1 fibroblasts, and further reduction occurs upon differentiation to adipocytes. Intrinsic catalytic activities specifically associated with heterologously expressed human GLUT1 protein in transfected CHO-K1 versus 3T3-L1 cells were determined by subtracting appropriate control cell values for hexose transport and delta-antibody binding from those determined in the transfected cells expressing high levels of human GLUT1. The results confirmed a greater than 90% inhibition of the intrinsic catalytic activity of human GLUT1 transporters on the surface of mouse 3T3-L1 adipocytes relative to CHO-K1 fibroblasts. We conclude that a mechanism that markedly suppresses basal hexose transport catalyzed by GLUT1 is a major contributor to the dramatic insulin sensitivity of glucose uptake in 3T3-L1 adipocytes. | lld:pubmed |
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| pubmed-article:1881918 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:1881918 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1881918 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1881918 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:1881918 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:1881918 | pubmed:author | pubmed-author:CzechM PMP | lld:pubmed |
| pubmed-article:1881918 | pubmed:author | pubmed-author:HarrisonS ASA | lld:pubmed |
| pubmed-article:1881918 | pubmed:author | pubmed-author:BuxtonJ MJM | lld:pubmed |
| pubmed-article:1881918 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1881918 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:1881918 | pubmed:volume | 88 | lld:pubmed |
| pubmed-article:1881918 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1881918 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1881918 | pubmed:pagination | 7839-43 | lld:pubmed |
| pubmed-article:1881918 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:1881918 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1881918 | pubmed:articleTitle | Suppressed intrinsic catalytic activity of GLUT1 glucose transporters in insulin-sensitive 3T3-L1 adipocytes. | lld:pubmed |
| pubmed-article:1881918 | pubmed:affiliation | Program in Molecular Medicine, University of Massachusetts Medical Center, Worcester 01605. | lld:pubmed |
| pubmed-article:1881918 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1881918 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:1881918 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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