Linked Life Data

3313056

Source:http://linkedlifedata.com/resource/pubmed/id/3313056

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6143
pubmed:dateCreated
1987-12-16
pubmed:abstractText
The mechanism of insulin action is only partly understood. At one end of the signalling chain, the structure of the insulin receptor is known in detail, and at the other end, insulin controls cellular metabolism by regulating the phosphorylation of serine and threonine residues in key target enzymes. The molecular events linking the occupied receptor to changes in target enzyme phosphorylation have remained obscure. Recently, insulin was shown to promote the hydrolysis of a phosphatidylinositol glycan with release of its polar head-group. The head group was reported to activate a high-affinity cyclic AMP-phosphodiesterase and pyruvate dehydrogenase, to inhibit catecholamine-stimulated lipolysis, and also to inhibit phospholipid methyltransferase and adenylate cyclase. We report here that in intact adipocytes this head-group faithfully copies the insulin-directed effects on the phosphorylation and dephosphorylation of target proteins of the hormone.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:volume
330
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
77-9
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:articleTitle
Phospho-dephospho-control by insulin is mimicked by a phospho-oligosaccharide in adipocytes.
pubmed:affiliation
Departmento de Metabolismo, Nutricion y Hormonas, Fundacion Jiménez Diaz, Madrid, Spain.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't