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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1 Pt 1
|
| pubmed:dateCreated |
1997-9-3
|
| pubmed:abstractText |
Cyclooxygenase (COX) catalyzes the formation of prostaglandins from arachidonic acid. Nitric oxide synthase catalyzes the production of nitric oxide, a short-lived messenger molecule involved in many diverse cellular processes. Both of these enzymes have inducible forms [COX-2 and inducible nitric oxide synthase (iNOS), respectively] that respond to environmental stresses, chemicals, and extracellular ligands such as interleukin-1, epidermal growth factor, and platelet-derived growth factor. The precise cascade of intracellular events that leads to the expression of either COX-2 or iNOS is not known. Protein kinase C (PKC) is a family of 11 serine-threonine kinases conserved throughout eukaryotic species that transduce a wide variety of signals critical for cellular functions. Using a retroviral vector to overexpress the zeta-isoform of PKC in rat mesangial cells, we demonstrate markedly increased COX-2, prostaglandin E2 (PGE2), iNOS, and altered cellular morphology compared with mesangial cells expressing a control retroviral vector and untransfected mesangial cells. NIH/3T3 cells overexpressing PKC-zeta showed no change in morphology, PGE2 production, COX-2 expression, or iNOS expression at basal conditions. This suggests a role for PKC-zeta in the expression of these enzymes in mesangial cells.
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| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cyclooxygenase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Dinoprostone,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase,
http://linkedlifedata.com/resource/pubmed/chemical/Prostaglandin-Endoperoxide Synthases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/protein kinase C zeta
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| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0002-9513
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
273
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
C130-6
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| pubmed:dateRevised |
2009-4-7
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| pubmed:meshHeading |
pubmed-meshheading:9252450-3T3 Cells,
pubmed-meshheading:9252450-Animals,
pubmed-meshheading:9252450-Cells, Cultured,
pubmed-meshheading:9252450-Cyclooxygenase 2,
pubmed-meshheading:9252450-Dinoprostone,
pubmed-meshheading:9252450-Enzyme Induction,
pubmed-meshheading:9252450-Genetic Vectors,
pubmed-meshheading:9252450-Glomerular Mesangium,
pubmed-meshheading:9252450-Isoenzymes,
pubmed-meshheading:9252450-Male,
pubmed-meshheading:9252450-Mice,
pubmed-meshheading:9252450-Nitric Oxide Synthase,
pubmed-meshheading:9252450-Prostaglandin-Endoperoxide Synthases,
pubmed-meshheading:9252450-Protein Kinase C,
pubmed-meshheading:9252450-Rats,
pubmed-meshheading:9252450-Rats, Sprague-Dawley,
pubmed-meshheading:9252450-Recombinant Proteins,
pubmed-meshheading:9252450-Retroviridae,
pubmed-meshheading:9252450-Transfection
|
| pubmed:year |
1997
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| pubmed:articleTitle |
Overexpression of protein kinase C-zeta isoform increases cyclooxygenase-2 and inducible nitric oxide synthase.
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| pubmed:affiliation |
Department of Medicine, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|