Linked Life Data

1316856

Source:http://linkedlifedata.com/resource/pubmed/id/1316856

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1992-6-19
pubmed:abstractText
To elucidate the acute effect of insulin on its receptor, rat adipocytes were preincubated with insulin, washed with KCN to inhibit receptor cycling, and 125I-labeled insulin binding was measured. Preincubating cells from young insulin-sensitive rats with insulin increased cell surface binding up to approximately fourfold without changing apparent receptor affinity. This effect was rapid (t1/2 less than 5 min) and had a similar dose-response relationship as the effect on glucose transport. It was also energy dependent because preincubation with KCN completely abolished the effect of subsequent insulin exposure. The increased binding capacity was not recovered after cell solubilization or in partially purified receptors or isolated plasma membranes. Cells pretreated with insulin were less sensitive to the ability of trypsin to remove cell surface receptors, suggesting a conformational change of the receptors. This was also supported by the finding that the polyclonal binding in insulin-treated but not in control cells. Vanadate mimicked the effect of insulin to increase insulin binding, whereas concanavalin A, vasopressin, phorbol esters, or the adenosine analogue phenyl isopropyl adenosine was without effect. Insulin-resistant adipocytes from obese rats displayed no increase in cell surface binding after insulin treatment, despite normal tyrosine kinase activity in response to insulin. Thus, both insulin and vanadate elicit a rapid effect to markedly increase the number of cell surface insulin binding sites in intact rat adipocytes. This appears to occur independently of protein kinase C and the inhibitory GTP binding protein (Gi). Furthermore, the effect of insulin could not be demonstrated in insulin-resistant cells, suggesting that this mechanism may be of importance for the regulation of insulin sensitivity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0012-1797
pubmed:author
pubmed:issnType
Print
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
707-14
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:1316856-3-O-Methylglucose, pubmed-meshheading:1316856-Adipose Tissue, pubmed-meshheading:1316856-Animals, pubmed-meshheading:1316856-Biological Transport, pubmed-meshheading:1316856-Cell Membrane, pubmed-meshheading:1316856-Cells, Cultured, pubmed-meshheading:1316856-Concanavalin A, pubmed-meshheading:1316856-Cytochalasin D, pubmed-meshheading:1316856-Insulin, pubmed-meshheading:1316856-Kinetics, pubmed-meshheading:1316856-Male, pubmed-meshheading:1316856-Methylglucosides, pubmed-meshheading:1316856-Phenylisopropyladenosine, pubmed-meshheading:1316856-Potassium Cyanide, pubmed-meshheading:1316856-Protein-Tyrosine Kinases, pubmed-meshheading:1316856-Rats, pubmed-meshheading:1316856-Rats, Inbred Strains, pubmed-meshheading:1316856-Receptor, Insulin, pubmed-meshheading:1316856-Tetradecanoylphorbol Acetate, pubmed-meshheading:1316856-Trypsin
pubmed:year
1992
pubmed:articleTitle
Insulin can rapidly increase cell surface insulin binding capacity in rat adipocytes. A novel mechanism related to insulin sensitivity.
pubmed:affiliation
Department of Medicine II, Sahlgren's Hospital, University of Göteborg, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't