Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1994-4-18
pubmed:abstractText
Prostaglandins are synthesized from arachidonic acid by the rate-limiting enzyme cyclooxygenase (prostaglandin G/H synthase). Active cyclooxygenase is encoded by two distinct and independently regulated genes, termed cyclooxygenase-1 (cox1) and cyclooxygenase-2 (cox2). In this investigation, we examined the expression of cox1 and cox2 mRNA in rat aorta following balloon deendothelialization (BDE) in vivo and in rat aortic smooth muscle cells (SMC) after serum stimulation in vitro. Two h after BDE, rat aortic cox2 mRNA levels increased greater than 50-fold relative to the lowest detectable levels on days 2 and 14. No message was detectable in non-BDE control rat aortas. Similar to the results found in vivo, cultured SMC exhibited a greater than 45-fold increase in cox2 mRNA levels after a 2-h exposure to serum. This increase was transient because cox2 levels declined at 4 and 8 h. In contrast, minimal changes in cox1 mRNA levels were observed after BDE or serum treatments. Increased levels of cox2 mRNA and corresponding protein synthesis led to an accumulation of total cyclooxygenase protein, which remained elevated 24 h after serum stimulation. Serum-treated SMC also generated greater amounts of cyclooxygenase-dependent metabolites than quiescent SMC as evidenced by marked increases in prostaglandin E2 content in conditioned media. This increase is associated with a 2.5-3.0-fold increased rate of arachidonic acid conversion to prostaglandin E2. Our data indicate that injury and serum stimulation differentially regulate mRNA and protein expression of two distinct cox genes in vascular SMC in vivo and in vitro. The findings suggest that the prostanoid responses after vascular injury are, in part, mediated by acute increases in cox2 mRNA and cyclooxygenase-2 protein.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
269
pubmed:geneSymbol
cos2, cox1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8504-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:8132578-Animals, pubmed-meshheading:8132578-Aorta, pubmed-meshheading:8132578-Blotting, Northern, pubmed-meshheading:8132578-Blotting, Western, pubmed-meshheading:8132578-Cells, Cultured, pubmed-meshheading:8132578-Culture Media, pubmed-meshheading:8132578-Culture Media, Serum-Free, pubmed-meshheading:8132578-Endothelium, Vascular, pubmed-meshheading:8132578-Enzyme Induction, pubmed-meshheading:8132578-Gene Expression Regulation, Enzymologic, pubmed-meshheading:8132578-Isoenzymes, pubmed-meshheading:8132578-Male, pubmed-meshheading:8132578-Multigene Family, pubmed-meshheading:8132578-Muscle, Smooth, Vascular, pubmed-meshheading:8132578-Prostaglandin-Endoperoxide Synthases, pubmed-meshheading:8132578-RNA, Messenger, pubmed-meshheading:8132578-Rats, pubmed-meshheading:8132578-Rats, Sprague-Dawley
pubmed:year
1994
pubmed:articleTitle
Induction of cyclooxygenase-2 in rat vascular smooth muscle cells in vitro and in vivo.
pubmed:affiliation
New York Medical College, Department of Experimental Pathology, Valhalla 10595.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't