pubmed-article:11385506 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11385506 | lifeskim:mentions | umls-concept:C0042396 | lld:lifeskim |
pubmed-article:11385506 | lifeskim:mentions | umls-concept:C0538674 | lld:lifeskim |
pubmed-article:11385506 | lifeskim:mentions | umls-concept:C1514485 | lld:lifeskim |
pubmed-article:11385506 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:11385506 | pubmed:dateCreated | 2001-5-31 | lld:pubmed |
pubmed-article:11385506 | pubmed:abstractText | Heme oxygenase (HO-1, encoded by Hmox1) is an inducible protein activated in systemic inflammatory conditions by oxidant stress. Vascular injury is characterized by a local reparative process with inflammatory components, indicating a potential protective role for HO-1 in arterial wound repair. Here we report that HO-1 directly reduces vasoconstriction and inhibits cell proliferation during vascular injury. Expression of HO-1 in arteries stimulated vascular relaxation, mediated by guanylate cyclase and cGMP, independent of nitric oxide. The unexpected effects of HO-1 on vascular smooth muscle cell growth were mediated by cell-cycle arrest involving p21Cip1. HO-1 reduced the proliferative response to vascular injury in vivo; expression of HO-1 in pig arteries inhibited lesion formation and Hmox1-/- mice produced hyperplastic arteries compared with controls. Induction of the HO-1 pathway moderates the severity of vascular injury by at least two adaptive mechanisms independent of nitric oxide, and is a potential therapeutic target for diseases of the vasculature. | lld:pubmed |
pubmed-article:11385506 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11385506 | pubmed:language | eng | lld:pubmed |
pubmed-article:11385506 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11385506 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11385506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11385506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11385506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11385506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11385506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11385506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11385506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11385506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11385506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11385506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11385506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11385506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11385506 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11385506 | pubmed:month | Jun | lld:pubmed |
pubmed-article:11385506 | pubmed:issn | 1078-8956 | lld:pubmed |
pubmed-article:11385506 | pubmed:author | pubmed-author:SasMM | lld:pubmed |
pubmed-article:11385506 | pubmed:author | pubmed-author:KUON MNM | lld:pubmed |
pubmed-article:11385506 | pubmed:author | pubmed-author:ParrJ CJC | lld:pubmed |
pubmed-article:11385506 | pubmed:author | pubmed-author:BoehmMM | lld:pubmed |
pubmed-article:11385506 | pubmed:author | pubmed-author:ThiN vN | lld:pubmed |
pubmed-article:11385506 | pubmed:author | pubmed-author:NabelG JGJ | lld:pubmed |
pubmed-article:11385506 | pubmed:author | pubmed-author:NabelE GEG | lld:pubmed |
pubmed-article:11385506 | pubmed:author | pubmed-author:DuckersH JHJ | lld:pubmed |
pubmed-article:11385506 | pubmed:author | pubmed-author:TrueA LAL | lld:pubmed |
pubmed-article:11385506 | pubmed:author | pubmed-author:Clinton... | lld:pubmed |
pubmed-article:11385506 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11385506 | pubmed:volume | 7 | lld:pubmed |
pubmed-article:11385506 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11385506 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11385506 | pubmed:pagination | 693-8 | lld:pubmed |
pubmed-article:11385506 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:11385506 | pubmed:year | 2001 | lld:pubmed |
pubmed-article:11385506 | pubmed:articleTitle | Heme oxygenase-1 protects against vascular constriction and proliferation. | lld:pubmed |
pubmed-article:11385506 | pubmed:affiliation | Vascular Biology Branch, National Heart, Lung, and Blood Institute, Bethesda, Maryland, USA. | lld:pubmed |
pubmed-article:11385506 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11385506 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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