pubmed-article:2199443 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2199443 | lifeskim:mentions | umls-concept:C0206131 | lld:lifeskim |
pubmed-article:2199443 | lifeskim:mentions | umls-concept:C0021641 | lld:lifeskim |
pubmed-article:2199443 | lifeskim:mentions | umls-concept:C0017742 | lld:lifeskim |
pubmed-article:2199443 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:2199443 | pubmed:issue | 23 | lld:pubmed |
pubmed-article:2199443 | pubmed:dateCreated | 1990-9-13 | lld:pubmed |
pubmed-article:2199443 | pubmed:abstractText | The amounts of the brain type and muscle type glucose transporters (designated Glut 1 and 4, respectively) in 3T3-L1 adipocytes have been determined by quantitative immunoblotting with antibodies against their carboxyl-terminal peptides. There are about 950,000 and 280,000 copies of Glut 1 and 4, respectively, per cell. Insulin caused the translocation of both types of transporters from an intracellular location to the plasma membrane. The insulin-elicited increase in cell surface transporters was assessed by labeling the surface transporters with a newly developed, membrane-impermeant, photoaffinity labeling reagent for glucose transporters. The increases in Glut 1 and 4 averaged 6.5- and 17-fold, respectively, whereas there was a 21-fold in hexose transport. These results indicate that the translocation of Glut 4 could largely account for the insulin effect on transport rate, but only if the intrinsic activity of Glut 4 is much higher than that of Glut 1. The two transporters are colocalized intracellularly: vesicles (average diameter 72 nm) isolated from the intracellular membranes by immunoadsorption with antibodies against Glut 1 contained 95% of the Glut 4 and, conversely, vesicles isolated with antibodies against Glut 4 contained 85% of the Glut 1. | lld:pubmed |
pubmed-article:2199443 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2199443 | pubmed:language | eng | lld:pubmed |
pubmed-article:2199443 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2199443 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2199443 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:2199443 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2199443 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2199443 | pubmed:month | Aug | lld:pubmed |
pubmed-article:2199443 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:2199443 | pubmed:author | pubmed-author:KitagawaKK | lld:pubmed |
pubmed-article:2199443 | pubmed:author | pubmed-author:LienhardG EGE | lld:pubmed |
pubmed-article:2199443 | pubmed:author | pubmed-author:HolmanG DGD | lld:pubmed |
pubmed-article:2199443 | pubmed:author | pubmed-author:CalderheadD... | lld:pubmed |
pubmed-article:2199443 | pubmed:author | pubmed-author:TannerL ILI | lld:pubmed |
pubmed-article:2199443 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2199443 | pubmed:day | 15 | lld:pubmed |
pubmed-article:2199443 | pubmed:volume | 265 | lld:pubmed |
pubmed-article:2199443 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2199443 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2199443 | pubmed:pagination | 13801-8 | lld:pubmed |
pubmed-article:2199443 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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pubmed-article:2199443 | pubmed:year | 1990 | lld:pubmed |
pubmed-article:2199443 | pubmed:articleTitle | Insulin regulation of the two glucose transporters in 3T3-L1 adipocytes. | lld:pubmed |
pubmed-article:2199443 | pubmed:affiliation | Department of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 03756. | lld:pubmed |
pubmed-article:2199443 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2199443 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:2199443 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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