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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
28
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pubmed:dateCreated |
1991-8-22
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pubmed:abstractText |
The involvement of protein phosphatases in regulating platelet activation was studied. The major portion of the phosphorylase phosphatase activity found in platelet lysates appears to be of the type 1 variety. The identification of this enzyme was based on the finding that greater than 80% of protein phosphatase activity was inhibited by the heat-stable inhibitor protein inhibitor 2 and, while only 20% of the phosphorylase phosphatase activity in platelet extracts was inhibited by 2 nM okadaic acid, greater than 95% of the activity was inhibited in the presence of 1 microM okadaic acid. Increases in protein phosphorylations occurred and thrombin-induced release of serotonin was prevented as a result of artificially inhibiting the enzyme with okadaic acid in intact platelets. This implies either that the regulation of okadaic acid sensitive protein phosphatases is necessary for some agonist-induced effects or that okadaic acid sensitive phosphatases are required for maintaining platelets in a responsive state.
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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/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Endoribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Ethers, Cyclic,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Okadaic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/PPP1R8 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Serotonin,
http://linkedlifedata.com/resource/pubmed/chemical/Threonine,
http://linkedlifedata.com/resource/pubmed/chemical/Thrombin,
http://linkedlifedata.com/resource/pubmed/chemical/protein phosphatase inhibitor-1,
http://linkedlifedata.com/resource/pubmed/chemical/protein phosphatase inhibitor-2
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0006-2960
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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 |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6819-24
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:1648961-Blood Platelets,
pubmed-meshheading:1648961-Carrier Proteins,
pubmed-meshheading:1648961-Endoribonucleases,
pubmed-meshheading:1648961-Ethers, Cyclic,
pubmed-meshheading:1648961-Humans,
pubmed-meshheading:1648961-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:1648961-Okadaic Acid,
pubmed-meshheading:1648961-Phosphoprotein Phosphatases,
pubmed-meshheading:1648961-Phosphorylation,
pubmed-meshheading:1648961-Platelet Activation,
pubmed-meshheading:1648961-Proteins,
pubmed-meshheading:1648961-RNA-Binding Proteins,
pubmed-meshheading:1648961-Serine,
pubmed-meshheading:1648961-Serotonin,
pubmed-meshheading:1648961-Threonine,
pubmed-meshheading:1648961-Thrombin
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pubmed:year |
1991
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pubmed:articleTitle |
Thrombin-induced effects are selectively inhibited following treatment of intact human platelets with okadaic acid.
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pubmed:affiliation |
Department of Cell Biology and Anatomy, New York Medical College, Valhalla 10595.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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