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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
24
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pubmed:dateCreated |
1983-2-14
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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.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Cations, Divalent,
http://linkedlifedata.com/resource/pubmed/chemical/Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
257
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15162-6
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:6757253-Adenosine Triphosphate,
pubmed-meshheading:6757253-Cations, Divalent,
pubmed-meshheading:6757253-Cell Membrane,
pubmed-meshheading:6757253-Epidermal Growth Factor,
pubmed-meshheading:6757253-Female,
pubmed-meshheading:6757253-Humans,
pubmed-meshheading:6757253-Insulin,
pubmed-meshheading:6757253-Kinetics,
pubmed-meshheading:6757253-Phosphorylation,
pubmed-meshheading:6757253-Placenta,
pubmed-meshheading:6757253-Pregnancy,
pubmed-meshheading:6757253-Receptor, Insulin,
pubmed-meshheading:6757253-Tyrosine
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pubmed:year |
1982
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pubmed:articleTitle |
Insulin-stimulated tyrosine phosphorylation of the insulin receptor in detergent extracts of human placental membranes. Comparison to epidermal growth factor-stimulated phosphorylation.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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