Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
1996-3-1
|
pubmed:abstractText |
Proteolytically active forms of thrombin ( alpha- and gamma-thrombin) and thrombin receptor peptides inhibited the release of nitrite, a stable endproduct of nitric oxide, evoked by interleukin-1 beta (IL-1 beta ) in cultured vascular smooth muscle cells while proteolytically inactive forms [D-Phe-Pro-Arg chloromethyl ketone-alpha-thrombin (PPACK-alpha-thrombin) and diisopropylphosphoryl-alpha-thrombin (DIP-alpha-thrombin)] had either no or only minimal inhibitory effects. Under bioassay conditions, perfusates from columns containing IL-1 beta-activated vascular smooth muscle cells or cells treated with IL-1 beta plus PPACK-alpha-thrombin relaxed detector blood vessels. These relaxations were abolished by the inhibitor of nitric oxide synthesis, NG-nitro-L-arginine. No relaxations were obtained with untreated cells or IL-1 beta-treated cells in the presence of alpha-thrombin. The expression of inducible nitric oxide synthase mRNA and protein in vascular smooth muscle cells by IL-1 beta was impaired by alpha-thrombin. These results demonstrate that thrombin regulates the expression of the inducible nitric oxide synthase at a transcriptional level via the proteolytic activation of the thrombin receptor in vascular smooth muscle cells.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrites,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Thrombin,
http://linkedlifedata.com/resource/pubmed/chemical/Thrombin
|
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
0340-6245
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
74
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
980-6
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:8571333-Amino Acid Sequence,
pubmed-meshheading:8571333-Animals,
pubmed-meshheading:8571333-Biological Assay,
pubmed-meshheading:8571333-Catalysis,
pubmed-meshheading:8571333-Cells, Cultured,
pubmed-meshheading:8571333-Endopeptidases,
pubmed-meshheading:8571333-Enzyme Induction,
pubmed-meshheading:8571333-Molecular Sequence Data,
pubmed-meshheading:8571333-Muscle, Smooth, Vascular,
pubmed-meshheading:8571333-Nitric Oxide,
pubmed-meshheading:8571333-Nitric Oxide Synthase,
pubmed-meshheading:8571333-Nitrites,
pubmed-meshheading:8571333-Rats,
pubmed-meshheading:8571333-Rats, Wistar,
pubmed-meshheading:8571333-Receptors, Thrombin,
pubmed-meshheading:8571333-Thrombin,
pubmed-meshheading:8571333-Transcription, Genetic
|
pubmed:year |
1995
|
pubmed:articleTitle |
Thrombin prevents the expression of inducible nitric oxide synthase in vascular smooth muscle cells by a proteolytically-activated thrombin receptor.
|
pubmed:affiliation |
Zentrum der Physiologie, Klinikum der JWG-Universität, Frankfurt, Germany.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|