Linked Life Data

3038645

Source:http://linkedlifedata.com/resource/pubmed/id/3038645

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1987-9-16
pubmed:abstractText
A soybean phospholipid mixture produced a concentration-dependent enhancement of beta subunit autophosphorylation of the detergent-soluble, purified human placental insulin receptor. Although phosphatidylcholine, phosphatidylethanolamine, or phosphatidylserine also increased insulin receptor autophosphorylation, only phosphatidylinositol (PtdIns) stimulated to a similar extent as the phospholipid mixture. The effect of PtdIns was biphasic, stimulating at low concentrations (75 microM), but having no stimulatory effect at high concentrations (1.0 mM). Phospholipids also stimulated the exogenous protein kinase activity of the insulin receptor toward histone H2B. Phosphorylation of PtdIns occurred with these purified insulin receptor preparations, but this activity was insulin-independent, and the turnover number for PtdIns phosphorylation in the presence of soybean phospholipid was 1/220th as small as the turnover number for the autophosphorylating activity. These results suggest that although PtdIns can modulate the activity of the insulin receptor kinase, PtdIns phosphorylation itself is not directly involved in this regulation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0892-6638
pubmed:author
pubmed:issnType
Print
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
55-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Phospholipid activation of the insulin receptor kinase: regulation by phosphatidylinositol.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't