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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2001-5-31
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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.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cdkn1a protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, Serum-Free,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic GMP,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase Inhibitor...,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclins,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Heme Oxygenase (Decyclizing),
http://linkedlifedata.com/resource/pubmed/chemical/Heme Oxygenase-1,
http://linkedlifedata.com/resource/pubmed/chemical/Hmox1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protoporphyrins,
http://linkedlifedata.com/resource/pubmed/chemical/zinc protoporphyrin
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1078-8956
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
693-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11385506-Animals,
pubmed-meshheading:11385506-Arteries,
pubmed-meshheading:11385506-Cell Cycle,
pubmed-meshheading:11385506-Cells, Cultured,
pubmed-meshheading:11385506-Culture Media, Serum-Free,
pubmed-meshheading:11385506-Cyclic GMP,
pubmed-meshheading:11385506-Cyclin-Dependent Kinase Inhibitor p21,
pubmed-meshheading:11385506-Cyclins,
pubmed-meshheading:11385506-Enzyme Induction,
pubmed-meshheading:11385506-Enzyme Inhibitors,
pubmed-meshheading:11385506-Gene Deletion,
pubmed-meshheading:11385506-Heme Oxygenase (Decyclizing),
pubmed-meshheading:11385506-Heme Oxygenase-1,
pubmed-meshheading:11385506-Membrane Proteins,
pubmed-meshheading:11385506-Mice,
pubmed-meshheading:11385506-Muscle, Smooth, Vascular,
pubmed-meshheading:11385506-Protoporphyrins,
pubmed-meshheading:11385506-Swine,
pubmed-meshheading:11385506-Transfection,
pubmed-meshheading:11385506-Vasoconstriction,
pubmed-meshheading:11385506-Vasodilation
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pubmed:year |
2001
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pubmed:articleTitle |
Heme oxygenase-1 protects against vascular constriction and proliferation.
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pubmed:affiliation |
Vascular Biology Branch, National Heart, Lung, and Blood Institute, Bethesda, Maryland, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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