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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1998-7-9
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pubmed:abstractText |
We have found that modification of rat PC12 cells with pertussis toxin resulted in an approximately 50% inhibition of a protein phosphatase 2A-like phosphatase. Protein phosphatase 2A (PP2A) is a major cellular serine/threonine-specific protein phosphatase. Treatment of extracts from pertussis toxin-modified PC12 cells with either immobilized alkaline phosphatase or Ca2+ reversed this inhibition. Reactivation of the PP2A-like phosphatase in Ca2+ appears to result from the dephosphorylation of a protein by the Ca2+/calmodulin-dependent protein phosphatase calcineurin. The PP2A-like phosphatase in extracts from pertussis toxin-modified PC12 cells eluted from a Mono Q column at a higher ionic strength than did the PP2A-like phosphatase in extracts from control cells. After incubation in Ca2+, the PP2A-like phosphatase in extracts from pertussis toxin-modified cells eluted from a Mono Q column at the same ionic strength as did the PP2A-like phosphatase in extracts from control cells. These results indicate that the effect of pertussis toxin on this PP2A-like activity results from the phosphorylation of either one of the subunits of the PP2A-like phosphatase or a protein that when phosphorylated binds to and inhibits this phosphatase. Pertussis toxin modification did not result in the phosphorylation of the catalytic subunit of PP2A. Because phosphorylation regulates the activities of many enzymes and cell surface receptors, a pertussis toxin-induced decrease in PP2A activity could alter signaling pathways and other cellular processes in which G proteins are not directly involved.
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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/Alkaline Phosphatase,
http://linkedlifedata.com/resource/pubmed/chemical/Anion Exchange Resins,
http://linkedlifedata.com/resource/pubmed/chemical/Calcineurin,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Forskolin,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mono Q,
http://linkedlifedata.com/resource/pubmed/chemical/Pertussis Toxin,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphorus Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Resins, Synthetic,
http://linkedlifedata.com/resource/pubmed/chemical/Virulence Factors, Bordetella
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0022-3042
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
71
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
248-57
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:9648872-Alkaline Phosphatase,
pubmed-meshheading:9648872-Animals,
pubmed-meshheading:9648872-Anion Exchange Resins,
pubmed-meshheading:9648872-Calcineurin,
pubmed-meshheading:9648872-Calcium,
pubmed-meshheading:9648872-Forskolin,
pubmed-meshheading:9648872-GTP-Binding Proteins,
pubmed-meshheading:9648872-Neurons,
pubmed-meshheading:9648872-PC12 Cells,
pubmed-meshheading:9648872-Pertussis Toxin,
pubmed-meshheading:9648872-Phosphates,
pubmed-meshheading:9648872-Phosphoprotein Phosphatases,
pubmed-meshheading:9648872-Phosphorus Radioisotopes,
pubmed-meshheading:9648872-Phosphorylation,
pubmed-meshheading:9648872-Precipitin Tests,
pubmed-meshheading:9648872-Protein Binding,
pubmed-meshheading:9648872-Protein Phosphatase 2,
pubmed-meshheading:9648872-Rats,
pubmed-meshheading:9648872-Resins, Synthetic,
pubmed-meshheading:9648872-Virulence Factors, Bordetella
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pubmed:year |
1998
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pubmed:articleTitle |
Pertussis toxin modification of PC12 cells inhibits a protein phosphatase 2A-like phosphatase.
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pubmed:affiliation |
Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
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pubmed:publicationType |
Journal Article
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