| pubmed-article:8429011 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8429011 | lifeskim:mentions | umls-concept:C0439849 | lld:lifeskim |
| pubmed-article:8429011 | lifeskim:mentions | umls-concept:C0205102 | lld:lifeskim |
| pubmed-article:8429011 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:8429011 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:8429011 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:8429011 | pubmed:dateCreated | 1993-3-9 | lld:pubmed |
| pubmed-article:8429011 | pubmed:abstractText | In this study, we examined the effect of phosphorylation on GLUT-4 function in isolated rat adipocytes. Adipocytes labeled with 32P for 2 h were incubated with parathyroid hormone (PTH) (20 ng/ml) for 60 min and then exposed to insulin (25 ng/ml) for an additional 30 min. 32P-GLUT-4 was immunoprecipitated from the plasma membrane and low density microsomal fractions, and its degree of phosphorylation was determined by autoradiography and densitometry. Results were expressed as 32P-GLUT-4 specific activity (phosphorylation/unit of protein). GLUT-4 intrinsic activity was measured using [14C]2-deoxyglucose uptake in plasma membrane vesicles. PTH significantly increased GLUT-4 phosphorylation and eliminated the insulin-stimulated dephosphorylation of GLUT-4. Western blotting revealed normal distribution of GLUT-4 before and after insulin stimulation in control and PTH-treated cells, suggesting that phosphorylation of GLUT-4 does not interfere with its recruitment to the plasma membrane. In contrast, intrinsic activity of phosphorylated GLUT-4 was significantly reduced (p < 0.01). Preincubation of adipocytes with calcium channel blocker (nitrendipine) and cyclic AMP antagonist (RpcAMP) restored GLUT-4 intrinsic activity in the PTH-treated cells. In several experiments, GLUT-4 was phosphorylated in vitro in plasma membrane vesicles isolated from normal adipocytes exposed to insulin. This in vitro phosphorylation reduced GLUT-4 intrinsic activity by approximately 35% (p < 0.01). We conclude that phosphorylation of GLUT-4 significantly impairs the ability of insulin to stimulate its intrinsic activity. | lld:pubmed |
| pubmed-article:8429011 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8429011 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8429011 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8429011 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8429011 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8429011 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8429011 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8429011 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8429011 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8429011 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8429011 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:8429011 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8429011 | pubmed:author | pubmed-author:SussmanK EKE | lld:pubmed |
| pubmed-article:8429011 | pubmed:author | pubmed-author:DrazninBB | lld:pubmed |
| pubmed-article:8429011 | pubmed:author | pubmed-author:ReuschJ EJE | lld:pubmed |
| pubmed-article:8429011 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8429011 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8429011 | pubmed:volume | 268 | lld:pubmed |
| pubmed-article:8429011 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8429011 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8429011 | pubmed:pagination | 3348-51 | lld:pubmed |
| pubmed-article:8429011 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:8429011 | pubmed:meshHeading | pubmed-meshheading:8429011-... | lld:pubmed |
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| pubmed-article:8429011 | pubmed:meshHeading | pubmed-meshheading:8429011-... | lld:pubmed |
| pubmed-article:8429011 | pubmed:meshHeading | pubmed-meshheading:8429011-... | lld:pubmed |
| pubmed-article:8429011 | pubmed:meshHeading | pubmed-meshheading:8429011-... | lld:pubmed |
| pubmed-article:8429011 | pubmed:meshHeading | pubmed-meshheading:8429011-... | lld:pubmed |
| pubmed-article:8429011 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8429011 | pubmed:articleTitle | Inverse relationship between GLUT-4 phosphorylation and its intrinsic activity. | lld:pubmed |
| pubmed-article:8429011 | pubmed:affiliation | Department of Medicine, Veterans Affairs Medical Center, Denver, Colorado 80220. | lld:pubmed |
| pubmed-article:8429011 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8429011 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8429011 | lld:pubmed |
