Linked Life Data

8739910

Source:http://linkedlifedata.com/resource/pubmed/id/8739910

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1996-9-30
pubmed:abstractText
Phosphoinositide 3-kinase (PI3-kinase) plays a crucial role in insulin signal transduction. We studied the molecular mechanism of the insulin-induced activation of PI3-kinase in rat hepatoma Fao cells using an antibody against the 110-kDa catalytic subunit (p110) and two against the 85-kDa regulatory subunit (p85 alpha). PI3-kinase activity increased 1.6-fold in anti-p85 immunoprecipitates after insulin stimulation, whereas it did not increase when cell lysates were first immunoprecipitated with anti-phosphotyrosine or anti-insulin receptor substrate-1 (IRS-1), then with anti-p85, suggesting that the PI3-kinase which associates with tyrosyl phosphoproteins including IRS-1 is responsible for the increase in kinase activity. The activated PI3-kinase molecules constituted 4-6% of the total PI3-kinase, and their specific activity was 11-14 times higher than that of the basal state. Anti-p110 recognized the catalytically active form of p110, and immunoprecipitated p110 only after exposure to insulin. Hence, the epitope of anti-p110, P200-C215, seems to be included in the portion of p110, the conformation of which is changed by insulin stimulation. We conclude that, in response to insulin stimulation, only a small fraction of p85 in the PI3-kinase pool associates with tyrosyl phosphoproteins including IRS-1, and that the specific activity of p110 is increased presumably through a conformational change including the P200-C215 region.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0012-186X
pubmed:author
pubmed:issnType
Print
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
515-22
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:8739910-Animals, pubmed-meshheading:8739910-Autoradiography, pubmed-meshheading:8739910-Cell Line, pubmed-meshheading:8739910-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:8739910-Enzyme Activation, pubmed-meshheading:8739910-Insulin, pubmed-meshheading:8739910-Liver Neoplasms, Experimental, pubmed-meshheading:8739910-Methionine, pubmed-meshheading:8739910-Phosphates, pubmed-meshheading:8739910-Phosphatidylinositol 3-Kinases, pubmed-meshheading:8739910-Phosphoproteins, pubmed-meshheading:8739910-Phosphorus Radioisotopes, pubmed-meshheading:8739910-Phosphorylation, pubmed-meshheading:8739910-Phosphotransferases (Alcohol Group Acceptor), pubmed-meshheading:8739910-Rats, pubmed-meshheading:8739910-Sulfur Radioisotopes, pubmed-meshheading:8739910-Tumor Cells, Cultured
pubmed:year
1996
pubmed:articleTitle
Insulin-induced activation of phosphoinositide 3-kinase in Fao cells.
pubmed:affiliation
Department of Medicine and Clinical Science, Kyoto University Graduate School of Medicine, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't