Linked Life Data

10860857

Source:http://linkedlifedata.com/resource/pubmed/id/10860857

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2000-7-26
pubmed:abstractText
In rat liver derived HTC cells transfected with and expressing human insulin receptors, there are multiple p60-70 proteins that are tyrosine phosphorylated following insulin treatment of cells. Employing antibodies to insulin receptor substrate 3 (alpha-IRS-3), we found that IRS-3 is a major p60 phosphoprotein that is tyrosine phosphorylated following insulin treatment of cells and interacts with phosphatidylinositol-3-kinase (PI3K). Majority of IRS-3 when phosphorylated appears to interact with PI3K. Tyrosine phosphorylation of IRS-3 is robust at 2 min and steadily increases up to 30-90 min of insulin treatment. Following insulin treatment of cells, some high molecular weight phosphoproteins are coimmunoprecipitated with alpha-IRS-3. In summary, IRS-3 is the major p60 protein that is tyrosine phosphorylated and interacts with PI3K in HTC rat liver derived cells following insulin treatment of cells. Unlike related IRS-1/2 that is transiently phosphorylated, IRS-3 shows robust and prolonged tyrosine phosphorylation upon insulin treatment of cells and may play a role in delayed and/or prolonged insulin actions.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-291X
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
272
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
953-8
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Characterization of insulin receptor substrate 3 in rat liver derived cells.
pubmed:affiliation
Department of Physiology and Biophysics, University of Southern California, Los Angeles 90033, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't