| pubmed-article:2905679 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2905679 | lifeskim:mentions | umls-concept:C0034818 | lld:lifeskim |
| pubmed-article:2905679 | lifeskim:mentions | umls-concept:C0312418 | lld:lifeskim |
| pubmed-article:2905679 | lifeskim:mentions | umls-concept:C0597304 | lld:lifeskim |
| pubmed-article:2905679 | lifeskim:mentions | umls-concept:C0443199 | lld:lifeskim |
| pubmed-article:2905679 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
| pubmed-article:2905679 | lifeskim:mentions | umls-concept:C0036667 | lld:lifeskim |
| pubmed-article:2905679 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:2905679 | pubmed:dateCreated | 1989-3-6 | lld:pubmed |
| pubmed-article:2905679 | pubmed:abstractText | The cellular mechanism by which the specific binding of [125I]insulin to intact rat adipocytes is inhibited by isoproterenol has been studied. By exposing control and isoproterenol-treated cells to trypsin (0-150 micrograms/ml for 20 min at 4 degrees C) and measuring the intact insulin receptor pool following detergent solubilization, a differential sensitivity to proteolysis of the cell membrane receptor was observed. At low trypsin concentration (less than 30 micrograms/ml), approximately 40% of the specific insulin binding in isoproterenol-treated cells was insensitive to proteolysis as compared to control cells. At higher levels of trypsin (50-150 micrograms/ml) both groups displayed similar levels of trypsin-insensitive receptors which, at the highest trypsin concentration, accounted for 10% of the total receptors in intact cells. Detergent-solubilized receptors from isoproterenol-treated cells, on the other hand, exhibited the same sensitivity to trypsin proteolysis as solubilized receptors from control cells. The time course of the onset and reversal of the isoproterenol-induced binding alteration in intact adipocytes has been analyzed by mild trypsinization (20 micrograms/ml). Results indicated that insulin receptors resistant to trypsin under these conditions mediated the decreased surface binding and were re-expressed on the cell surface upon removal of isoproterenol. Experiments in which adipocytes were fractionated into plasma membrane and Golgi-enriched fractions indicated that the loss of surface insulin binding was not accompanied by a decrease in the proportion of receptors in the adipocyte plasma membrane.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
| pubmed-article:2905679 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2905679 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2905679 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2905679 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2905679 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2905679 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2905679 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2905679 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2905679 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2905679 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:2905679 | pubmed:issn | 0303-7207 | lld:pubmed |
| pubmed-article:2905679 | pubmed:author | pubmed-author:SandraAA | lld:pubmed |
| pubmed-article:2905679 | pubmed:author | pubmed-author:MarshallS JSJ | lld:pubmed |
| pubmed-article:2905679 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2905679 | pubmed:volume | 60 | lld:pubmed |
| pubmed-article:2905679 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2905679 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2905679 | pubmed:pagination | 87-94 | lld:pubmed |
| pubmed-article:2905679 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:2905679 | pubmed:meshHeading | pubmed-meshheading:2905679-... | lld:pubmed |
| pubmed-article:2905679 | pubmed:meshHeading | pubmed-meshheading:2905679-... | lld:pubmed |
| pubmed-article:2905679 | pubmed:meshHeading | pubmed-meshheading:2905679-... | lld:pubmed |
| pubmed-article:2905679 | pubmed:meshHeading | pubmed-meshheading:2905679-... | lld:pubmed |
| pubmed-article:2905679 | pubmed:meshHeading | pubmed-meshheading:2905679-... | lld:pubmed |
| pubmed-article:2905679 | pubmed:meshHeading | pubmed-meshheading:2905679-... | lld:pubmed |
| pubmed-article:2905679 | pubmed:meshHeading | pubmed-meshheading:2905679-... | lld:pubmed |
| pubmed-article:2905679 | pubmed:meshHeading | pubmed-meshheading:2905679-... | lld:pubmed |
| pubmed-article:2905679 | pubmed:meshHeading | pubmed-meshheading:2905679-... | lld:pubmed |
| pubmed-article:2905679 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:2905679 | pubmed:articleTitle | Differential sensitivity of the insulin receptor to proteolysis after beta-adrenergic stimulation. | lld:pubmed |
| pubmed-article:2905679 | pubmed:affiliation | Department of Anatomy, University of Iowa, Iowa City 52242. | lld:pubmed |
| pubmed-article:2905679 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2905679 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2905679 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
