Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1983-2-14
pubmed:abstractText
Addition of insulin to Triton-solubilized extracts of human placental membranes selectively stimulates the incorporation of 32P from [gamma-32P]ATP into an endogenous 95,000-dalton protein, which is identified as a component of the insulin receptor by immunoprecipitation. The insulin-stimulated increment in 32P is recovered largely in [32P]tyrosine after acid hydrolysis. E Epidermal growth factor (EGF) stimulates the phosphorylation of a 150,000-dalton protein in these detergent extracts. This reaction differs in several respects from the insulin-stimulated phosphorylation of the 95,000-dalton protein. Insulin-stimulated phosphorylation exhibits an absolute requirement for Mn2+ as the sole divalent cation, whereas EGF-stimulated phosphorylation is supported by Mg2+ and Co2+ as well as Mn2+. In the presence of Mn2+, insulin-stimulated phosphorylation is not detected at less than 50 microM ATP, whereas EGF-stimulated phosphorylation is well expressed at 5 microM ATP. Thus, in detergent-solubilized membrane extracts, insulin stimulates the phosphorylation of its own receptor on tyrosine residues. This reaction has enzymatic properties distinct from those of the EGF-stimulated phosphorylation in these same extracts. The role of this insulin-stimulated phosphorylation reaction in the initiation of insulin's many biologic actions merits further study.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
257
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15162-6
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Insulin-stimulated tyrosine phosphorylation of the insulin receptor in detergent extracts of human placental membranes. Comparison to epidermal growth factor-stimulated phosphorylation.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't