| pubmed-article:11340086 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11340086 | lifeskim:mentions | umls-concept:C0014257 | lld:lifeskim |
| pubmed-article:11340086 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:11340086 | lifeskim:mentions | umls-concept:C0006100 | lld:lifeskim |
| pubmed-article:11340086 | lifeskim:mentions | umls-concept:C0132555 | lld:lifeskim |
| pubmed-article:11340086 | lifeskim:mentions | umls-concept:C1704632 | lld:lifeskim |
| pubmed-article:11340086 | lifeskim:mentions | umls-concept:C0871261 | lld:lifeskim |
| pubmed-article:11340086 | lifeskim:mentions | umls-concept:C2911692 | lld:lifeskim |
| pubmed-article:11340086 | lifeskim:mentions | umls-concept:C1706817 | lld:lifeskim |
| pubmed-article:11340086 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
| pubmed-article:11340086 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:11340086 | lifeskim:mentions | umls-concept:C1882911 | lld:lifeskim |
| pubmed-article:11340086 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:11340086 | pubmed:dateCreated | 2001-5-7 | lld:pubmed |
| pubmed-article:11340086 | pubmed:abstractText | Endothelial nitric-oxide synthase (eNOS) is phosphorylated at Ser-1179 (bovine sequence) by Akt after growth factor or shear stress stimulation of endothelial cells, resulting in increased eNOS activity. Purified eNOS is also phosphorylated at Thr-497 by purified AMP-activated protein kinase, resulting in decreased eNOS activity. We investigated whether bradykinin (BK) stimulation of bovine aortic endothelial cells (BAECs) regulates eNOS through Akt activation and Ser-1179 or Thr-497 phosphorylation. Akt is transiently activated in BK-stimulated BAECs. Activation is blocked completely by wortmannin and LY294002, inhibitors of phosphatidylinositol 3-kinase, suggesting that Akt activation occurs downstream from phosphatidylinositol 3-kinase. BK stimulates a transient phosphorylation of eNOS at Ser-1179 that is correlated temporally with a transient dephosphorylation of eNOS at Thr-497. Phosphorylation at Ser-1179, but not dephosphorylation at Thr-497, is blocked by wortmannin and LY294002. BK also stimulates a transient nitric oxide (NO) release from BAECs with a time-course similar to Ser-1179 phosphorylation and Thr-497 dephosphorylation. NO release is not altered by wortmannin. BK-stimulated dephosphorylation of Thr-497 and NO release are blocked by the calcineurin inhibitor, cyclosporin A. These data suggest that BK activation of eNOS in BAECs primarily involves deinhibition of the enzyme through calcineurin-mediated dephosphorylation at Thr-497. | lld:pubmed |
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| pubmed-article:11340086 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11340086 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11340086 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11340086 | pubmed:month | May | lld:pubmed |
| pubmed-article:11340086 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:11340086 | pubmed:author | pubmed-author:KempB EBE | lld:pubmed |
| pubmed-article:11340086 | pubmed:author | pubmed-author:LiangHH | lld:pubmed |
| pubmed-article:11340086 | pubmed:author | pubmed-author:HarrisM BMB | lld:pubmed |
| pubmed-article:11340086 | pubmed:author | pubmed-author:VenemaV JVJ | lld:pubmed |
| pubmed-article:11340086 | pubmed:author | pubmed-author:JuHH | lld:pubmed |
| pubmed-article:11340086 | pubmed:author | pubmed-author:DICKY PYP | lld:pubmed |
| pubmed-article:11340086 | pubmed:author | pubmed-author:VenemaR CRC | lld:pubmed |
| pubmed-article:11340086 | pubmed:author | pubmed-author:MichellB JBJ | lld:pubmed |
| pubmed-article:11340086 | pubmed:author | pubmed-author:ZouRR | lld:pubmed |
| pubmed-article:11340086 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11340086 | pubmed:day | 11 | lld:pubmed |
| pubmed-article:11340086 | pubmed:volume | 276 | lld:pubmed |
| pubmed-article:11340086 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11340086 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11340086 | pubmed:pagination | 16587-91 | lld:pubmed |
| pubmed-article:11340086 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:11340086 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11340086 | pubmed:articleTitle | Reciprocal phosphorylation and regulation of endothelial nitric-oxide synthase in response to bradykinin stimulation. | lld:pubmed |
| pubmed-article:11340086 | pubmed:affiliation | Vascular Biology Center, Department of Pediatrics, Medical College of Georgia, Augusta, Georgia 30912, USA. | lld:pubmed |
| pubmed-article:11340086 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11340086 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11340086 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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