Linked Life Data

2839176

Source:http://linkedlifedata.com/resource/pubmed/id/2839176

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1988-8-3
pubmed:abstractText
The ability of insulin and an insulinomimetic oligosaccharide (IOS) isolated from conditioned medium of Reuber hepatoma cells to regulate protein phosphorylation in 3T3-L1 adipocytes and Fao hepatoma cells has been examined in extracts prepared from 32P-labeled cells and by immunoblotting of unlabeled extracts with an anti-phosphotyrosine antibody. In 32P-labeled 3T3-L1 cells, both insulin and IOS stimulate the dephosphorylation of a 55K membrane-associated protein, yet only insulin stimulates the phosphorylation of the ribosomal S6 protein and a 22K heat-stable soluble protein. In 32P-labeled Fao cells, both insulin and IOS stimulate the phosphorylation of a 16K protein, but only insulin stimulates S6 phosphorylation. As judged by immunoblotting, IOS does not stimulate the tyrosine phosphorylation of the beta subunit of the insulin receptor and a 180K soluble protein in a manner similar to insulin. These data indicate that the insulinomimetic effects of IOS are selective for certain insulin-regulated pathways and that the effects of IOS are unlikely to be operating through stimulation of the insulin receptor tyrosine kinase.
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:issnType
Print
pubmed:day
30
pubmed:volume
153
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
992-8
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Regulation of protein phosphorylation by insulin and an insulinomimetic oligosaccharide in 3T3-L1 adipocytes and Fao hepatoma cells.
pubmed:affiliation
Department of Medicine, Dartmouth Medical School, Hanover, N.H. 03756.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't