Linked Life Data

3007472

Source:http://linkedlifedata.com/resource/pubmed/id/3007472

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1986-5-9
pubmed:abstractText
We have studied the effect of incubation of intact cells with insulin on insulin receptor kinase activity. Following exposure of rat adipocytes to insulin, cells were solubilized and insulin receptors purified by specific immunoprecipitation or by insulin affinity chromatography. Kinase activity of the receptors, as measured by phosphorylation of histone 2B, was then determined. Insulin treatment of the cells resulted in a 10-20-fold increase in histone kinase activity of the subsequently isolated insulin receptors. The insulin effect was half-maximal at 3 s and maximal within 15 s of exposure, was dose-dependent (EC50 = 21 ng/ml), and was rapidly reversible following dissociation of insulin from the cells. The insulin effect in intact cells on insulin receptor kinase activity could be partially reversed in vitro by dephosphorylation of the isolated receptors by alkaline phosphatase. It is proposed that: in intact cells, insulin causes alterations in insulin receptors, such that their kinase activity toward non-receptor substrates increases; increased insulin receptor kinase activity following insulin stimulation in intact cells is, at least in part, the result of an increased phosphate content of the receptors; and effects of insulin on insulin receptors in intact cells can be preserved during receptor isolation and thus can be measured in a cell-free system.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
261
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4691-7
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Insulin activation of insulin receptor tyrosine kinase in intact rat adipocytes. An in vitro system to measure histone kinase activity of insulin receptors activated in vivo.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S.