Linked Life Data

9223444

Source:http://linkedlifedata.com/resource/pubmed/id/9223444

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pubmed-article:9223444pubmed:abstractTextCaveolin-1 and endothelial nitric oxide synthase (eNOS) are associated within endothelial caveolae. We have shown previously that eNOS is translocated to the detergent-insoluble, cytoskeletal fraction of bovine aortic endothelial cells (BAEC) in response to bradykinin (BK)-stimulation or tyrosine phosphatase inhibition. In the present study, we have examined whether caveolin-1 is similarly translocated in response to these or other stimuli. Exposure of BAEC to the eNOS-activating agonists, BK, histamine, or ATP produces transient increases in the amounts of detergent-insoluble caveolin-1. Increases in insolubility are blocked by tyrosine kinase inhibitors and are potently mimicked by tyrosine phosphatase inhibitors. Increased insolubility is accompanied by an increased association of caveolin-1 with eNOS and inhibition of eNOS catalytic activity. Agonist-activation of eNOS in endothelial cells thus appears to involve tyrosine phosphorylation-dependent changes in the interaction of eNOS with caveolin-1. Increased interaction of eNOS with caveolin-1 may deactivate the enzyme subsequent to its activation by Ca2+/calmodulin.lld:pubmed
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pubmed-article:9223444pubmed:pagination155-61lld:pubmed
pubmed-article:9223444pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:9223444pubmed:year1997lld:pubmed
pubmed-article:9223444pubmed:articleTitleCaveolin-1 detergent solubility and association with endothelial nitric oxide synthase is modulated by tyrosine phosphorylation.lld:pubmed
pubmed-article:9223444pubmed:affiliationVascular Biology Center, Department of Pediatrics, Medical College of Georgia, Augusta 30912, USA.lld:pubmed
pubmed-article:9223444pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9223444pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:9223444pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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