rdf:type |
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lifeskim:mentions |
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pubmed:issue |
17
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pubmed:dateCreated |
1988-10-6
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pubmed:abstractText |
Incubation of Swiss mouse 3T3-D1 cells with physiological concentrations of insulin resulted in a rapid and transient activation of protein phosphatase activity as measured by using [32P]phosphorylase a as substrate. Activation reached a maximum level (140% of control value) within 5 min of addition and returned to control levels within 20 min. The effect of insulin was dose-dependent with half-maximal activation occurring at approximately 5 nM insulin. This activity could be completely inhibited by addition of the heat-stable protein inhibitor 2, which suggests the presence of an activated type-1 phosphatase. Similar effects on phosphatase activity were seen when epidermal growth factor and platelet-derived growth factor were tested. These results suggest that some of the intracellular effects caused by insulin and growth factors are mediated through the activation of a protein phosphatase.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842761-2820993,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842761-2826150,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842761-2827626,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842761-2827665,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842761-2956925,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842761-3007140,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842761-3008843,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842761-3024984,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842761-3025206,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842761-3030262,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842761-3100537,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842761-3321056,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842761-3512270,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842761-3597418,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2842761-3927284,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/2842761-6089223,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/2842761-942051
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
85
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6257-61
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:2842761-Animals,
pubmed-meshheading:2842761-Cations, Divalent,
pubmed-meshheading:2842761-Cells, Cultured,
pubmed-meshheading:2842761-Edetic Acid,
pubmed-meshheading:2842761-Epidermal Growth Factor,
pubmed-meshheading:2842761-Insulin,
pubmed-meshheading:2842761-Kinetics,
pubmed-meshheading:2842761-Mice,
pubmed-meshheading:2842761-Phosphoprotein Phosphatases,
pubmed-meshheading:2842761-Phosphorylase a,
pubmed-meshheading:2842761-Platelet-Derived Growth Factor,
pubmed-meshheading:2842761-Tromethamine,
pubmed-meshheading:2842761-Trypsin
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pubmed:year |
1988
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pubmed:articleTitle |
Stimulation of protein phosphatase activity by insulin and growth factors in 3T3 cells.
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pubmed:affiliation |
Department of Pharmacology, University of Washington, Seattle 98195.
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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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