|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:dateCreated |
1994-7-11
|
|
pubmed:abstractText |
The activation of human platelets is inhibited by two intracellular pathways regulated by either cGMP- or cAMP-elevating agents. There is considerable evidence that the inhibitory effects of cGMP and cAMP are mediated by the cGMP-PK and cAMP-PK, respectively, in human platelets. The cGI-PDE is an additional target for cGMP, and the cGMP-mediated elevation of cAMP levels contributes to the well known synergism between cAMP- and cGMP-elevating platelet inhibitors. Stimulation of both cAMP-PK and cGMP-PK prevents the agonist-induced activation of MLCK and PKC and inhibits the agonist-induced calcium mobilization from intracellular stores without any major effect on the ADP-regulated cation channel. These studies suggest that the inhibition of an early event of platelet activation, e.g. activation of PLC, is an effect common to both cGMP-PK and cAMP-PK stimulation. A common substrate of both cGMP-PK and cAMP-PK, the 46/50 kDa protein VASP, has been recently identified as a novel microfilament- and focal contact-associated protein whose phosphorylation correlates very well with platelet inhibition. Future investigations will have to identify the precise molecular mechanism of cyclic nucleotide inhibition of Ca2+ discharge from intracellular stores and whether cGMP-PK- and cAMP-PK-mediated VASP phosphorylation is an important component of this effect of cyclic nucleotides in human platelets.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenylate Cyclase,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
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/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin-Light-Chain Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Aggregation Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C
|
|
pubmed:status |
MEDLINE
|
|
pubmed:issn |
0065-2598
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
344
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
237-49
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:8209791-Adenylate Cyclase,
pubmed-meshheading:8209791-Blood Platelets,
pubmed-meshheading:8209791-Calcium,
pubmed-meshheading:8209791-Cell Adhesion Molecules,
pubmed-meshheading:8209791-Cyclic AMP,
pubmed-meshheading:8209791-Cyclic AMP-Dependent Protein Kinases,
pubmed-meshheading:8209791-Cyclic GMP,
pubmed-meshheading:8209791-Humans,
pubmed-meshheading:8209791-Membrane Proteins,
pubmed-meshheading:8209791-Microfilament Proteins,
pubmed-meshheading:8209791-Myosin-Light-Chain Kinase,
pubmed-meshheading:8209791-Phosphoproteins,
pubmed-meshheading:8209791-Phosphorylation,
pubmed-meshheading:8209791-Platelet Activation,
pubmed-meshheading:8209791-Platelet Aggregation Inhibitors,
pubmed-meshheading:8209791-Protein Kinase C,
pubmed-meshheading:8209791-Protein Processing, Post-Translational,
pubmed-meshheading:8209791-Signal Transduction
|
|
pubmed:year |
1993
|
|
pubmed:articleTitle |
Role of cyclic nucleotide-dependent protein kinases and their common substrate VASP in the regulation of human platelets.
|
|
pubmed:affiliation |
Medizinische Universitätsklinik, Klinische Forschergruppe, Würzburg, Germany.
|
|
pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
|
