Linked Life Data

7543000

Source:http://linkedlifedata.com/resource/pubmed/id/7543000

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1995-9-7
pubmed:abstractText
The promoter region of the endothelial cell nitric oxide synthase (ecNOS) gene contains potential response elements for transforming growth factor-beta 1 (TGF beta 1). TGF beta 1 plays an important role in the pathogenesis of atherosclerosis, vascular hypertrophy, and angiogenesis. We therefore sought to determine whether TGF beta 1 might modulate ecNOS expression in bovine aortic endothelial cells (BAEC). TGF beta 1 increased ecNOS mRNA in a dose-dependent manner. TGF beta 1 also increased ecNOS protein content. The production of nitrogen oxides (NOx), assessed by chemiluminescence, and nitric oxide synthase activity, assessed by arginine/citrulline conversion were increased in TGF beta 1-treated cells. Transcriptional activity of the 5'-flanking promoter region of the ecNOS gene was increased by TGF beta 1, as assessed by transfection with promoter/luciferase constructs. Deletion analysis suggested that the TGF beta 1-response element was present between nucleotides -1269 and -935 from the first transcription start site, in which a putative nuclear factor-1 (NF-1) binding site existed. Gel shift assays showed that nuclear protein(s), immunologically similar to CCAAT transcription factor/NF-1, bound to the putative NF-1 binding site in a sequence-specific manner. Mutation of the putative NF-1 binding site in the promoter/luciferase construct significantly decreased the responsiveness to TGF beta 1. In conclusion, TGF beta 1 increases ecNOS expression associated with an increase in production of NO in BAEC. This response is probably mediated by transcriptional activation of the ecNOS gene promoter.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1079-5642
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1255-61
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:7543000-Amino Acid Oxidoreductases, pubmed-meshheading:7543000-Animals, pubmed-meshheading:7543000-Base Sequence, pubmed-meshheading:7543000-Binding Sites, pubmed-meshheading:7543000-Cattle, pubmed-meshheading:7543000-Cell Division, pubmed-meshheading:7543000-Cell Nucleus, pubmed-meshheading:7543000-Cells, Cultured, pubmed-meshheading:7543000-DNA-Binding Proteins, pubmed-meshheading:7543000-Endothelium, Vascular, pubmed-meshheading:7543000-Molecular Sequence Data, pubmed-meshheading:7543000-Mutagenesis, Site-Directed, pubmed-meshheading:7543000-NFI Transcription Factors, pubmed-meshheading:7543000-Nitric Oxide, pubmed-meshheading:7543000-Nitric Oxide Synthase, pubmed-meshheading:7543000-Oligodeoxyribonucleotides, pubmed-meshheading:7543000-Promoter Regions, Genetic, pubmed-meshheading:7543000-Structure-Activity Relationship, pubmed-meshheading:7543000-Transcription, Genetic, pubmed-meshheading:7543000-Transcription Factors, pubmed-meshheading:7543000-Transforming Growth Factor beta
pubmed:year
1995
pubmed:articleTitle
Molecular regulation of the bovine endothelial cell nitric oxide synthase by transforming growth factor-beta 1.
pubmed:affiliation
Department of Medicine, Emory University School of Medicine, Atlanta, Ga 30322, USA.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.