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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2003-2-7
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pubmed:abstractText |
P-selectin is rapidly translocated from platelet alpha-granules following activation. Intracellular cyclic AMP (cAMP) is a potent inhibitory pathway that results in global downregulation of platelet activation. While cAMP-dependent protein kinase (PKA) has long been considered as the main mediator of cAMP-dependent effects, no study has yet evaluated its effect on P-selectin expression in human platelets. Pretreatment of thrombin-stimulated platelets with forskolin resulted in a concentration- dependent inhibition of P-selectin expression that correlated with adenylyl cyclase activity. Inhibition of PKA with H-89 reversed cAMP-induced inhibition of P-selectin while cGMP-dependent protein kinase (PKG) inhibition with KT5823 significantly potentiated cAMP-dependent inhibition of P-selectin. Similar results were also observed in a platelet/neutrophil binding assay. In conclusion, cAMP-induced inhibition of P-selectin expression is, in large part, mediated through activation of PKA. PKG appears to be solicited for P-selectin expression when cAMP levels are elevated which suggest a cAMP/PKG-dependent pathway of platelet activation.
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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/Adenylate Cyclase,
http://linkedlifedata.com/resource/pubmed/chemical/Alkaloids,
http://linkedlifedata.com/resource/pubmed/chemical/Carbazoles,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP-Dependent Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic GMP,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic GMP-Dependent Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Forskolin,
http://linkedlifedata.com/resource/pubmed/chemical/Indoles,
http://linkedlifedata.com/resource/pubmed/chemical/Isoquinolines,
http://linkedlifedata.com/resource/pubmed/chemical/KT 5823,
http://linkedlifedata.com/resource/pubmed/chemical/N-(2-(4-bromocinnamylamino)ethyl)-5-...,
http://linkedlifedata.com/resource/pubmed/chemical/P-Selectin,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfonamides,
http://linkedlifedata.com/resource/pubmed/chemical/Thrombin
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0340-6245
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
89
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
310-7
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:12574812-Adenylate Cyclase,
pubmed-meshheading:12574812-Alkaloids,
pubmed-meshheading:12574812-Blood Platelets,
pubmed-meshheading:12574812-Carbazoles,
pubmed-meshheading:12574812-Cell Adhesion,
pubmed-meshheading:12574812-Cyclic AMP,
pubmed-meshheading:12574812-Cyclic AMP-Dependent Protein Kinases,
pubmed-meshheading:12574812-Cyclic GMP,
pubmed-meshheading:12574812-Cyclic GMP-Dependent Protein Kinases,
pubmed-meshheading:12574812-Enzyme Activation,
pubmed-meshheading:12574812-Enzyme Inhibitors,
pubmed-meshheading:12574812-Forskolin,
pubmed-meshheading:12574812-Gene Expression Regulation,
pubmed-meshheading:12574812-Humans,
pubmed-meshheading:12574812-Indoles,
pubmed-meshheading:12574812-Isoquinolines,
pubmed-meshheading:12574812-Neutrophils,
pubmed-meshheading:12574812-P-Selectin,
pubmed-meshheading:12574812-Phosphorylation,
pubmed-meshheading:12574812-Platelet Activation,
pubmed-meshheading:12574812-Protein Processing, Post-Translational,
pubmed-meshheading:12574812-Second Messenger Systems,
pubmed-meshheading:12574812-Sulfonamides,
pubmed-meshheading:12574812-Thrombin
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pubmed:year |
2003
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pubmed:articleTitle |
Differential regulation of P-selectin expression by protein kinase A and protein kinase G in thrombin-stimulated human platelets.
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pubmed:affiliation |
Montreal Heart Institute, Montreal, Quebec, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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