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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-3
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pubmed:dateCreated |
1999-1-8
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pubmed:abstractText |
In the insulin producing cell line RINm5F distribution of serine/threonine specific protein phosphatases type 1 (PP1) and 2A (PP2A) was studied. Using different agents which inhibit or stimulate PP1 and PP2A we found that in membrane and nuclear fractions phosphatase activity was inhibited by okadaic acid (OA), protamine, heparin, and inhibitor-2 in a concentration-dependent manner. C2-ceramide had no effect. In the cytosolic fraction the inhibitory effect of okadaic acid was tenfold higher. Protamine stimulated phosphatase activity at low concentrations and became inhibitory at higher concentrations. Inhibitor-2 and heparin caused a decrease in phosphatase activity whereas C2-ceramide led to a slight activation. The data suggest that in membrane and nuclear fractions of RINmSF cells predominantly PP1 is present, whereas in the cytosol PP1 as well as PP2A can be detected.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Biological Markers,
http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Heparin,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/N-acetylsphingosine,
http://linkedlifedata.com/resource/pubmed/chemical/Okadaic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphorylase a,
http://linkedlifedata.com/resource/pubmed/chemical/Protamines,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SET protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Sphingosine,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0167-0115
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
77
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
77-81
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9809799-Animals,
pubmed-meshheading:9809799-Biological Markers,
pubmed-meshheading:9809799-Cell Fractionation,
pubmed-meshheading:9809799-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:9809799-Enzyme Inhibitors,
pubmed-meshheading:9809799-Heparin,
pubmed-meshheading:9809799-Histone Chaperones,
pubmed-meshheading:9809799-Islets of Langerhans,
pubmed-meshheading:9809799-Okadaic Acid,
pubmed-meshheading:9809799-Phosphoprotein Phosphatases,
pubmed-meshheading:9809799-Phosphoproteins,
pubmed-meshheading:9809799-Phosphorylase a,
pubmed-meshheading:9809799-Protamines,
pubmed-meshheading:9809799-Proteins,
pubmed-meshheading:9809799-Rats,
pubmed-meshheading:9809799-Sphingosine,
pubmed-meshheading:9809799-Transcription Factors,
pubmed-meshheading:9809799-Tumor Cells, Cultured
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pubmed:year |
1998
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pubmed:articleTitle |
Distribution of protein phosphatases type 1 and 2A in RINm5F cells.
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pubmed:affiliation |
Institute of Pharmaceutical Sciences, Department of Pharmacology, University of Tübingen, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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