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http://hdl.handle.net/10261/40563
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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Genís, Laura | - |
dc.contributor.author | Gonzalo, Pilar | - |
dc.contributor.author | Tutor, Antonio S. | - |
dc.contributor.author | Gálvez, Beatriz G. | - |
dc.contributor.author | Martínez-Ruiz, Antonio | - |
dc.contributor.author | Zaragoza, Carlos | - |
dc.contributor.author | Lamas Peláez, Santiago | - |
dc.contributor.author | Tryggvason, Kral | - |
dc.contributor.author | Apte, Suneel S. | - |
dc.contributor.author | Arroyo, Alicia G. | - |
dc.date.issued | 2007-10-15 | - |
dc.identifier.citation | Blood 110:2916-2923 (2007) | es_ES |
dc.identifier.issn | 0006-4971 | - |
dc.identifier.uri | 10261/40563 | - |
dc.description | 4 Figures. The online version of this article contains a data supplement. | es_ES |
dc.description.abstract | Nitric oxide (NO) is essential for vascular homeostasis and is also a critical modulator of angiogenesis; however, the molecular mechanisms of NO action during angiogenesis remain elusive. We have investigated the potential relationship between NO and membrane type 1–matrix metalloproteinase (MT1-MMP) during endothelial migration and capillary tube formation. Endothelial NO synthase (eNOS) colocalizes with MT1-MMP at motility-associated structures in migratory human endothelial cells (ECs); moreover, NO is produced at these structures and is released into the medium during EC migration. We have therefore addressed 2 questions: (1) the putative regulation of MT1-MMP by NO in migratory ECs; and (2) the requirement for MT1-MMP in NO-induced EC migration and tube formation. NO upregulates MT1-MMP membrane clustering on migratory human ECs, and this is accompanied by increased degradation of type I collagen substrate. MT1-MMP membrane expression and localization are impaired in lung ECs from eNOS-deficient mice, and these cells also show impaired migration and tube formation in vitro. Inhibition of MT1-MMP with a neutralizing antibody impairs NOinduced tube formation by human ECs, and NO-induced endothelial migration and tube formation are impaired in lung ECs from mice deficient in MT1-MMP. MT1-MMP thus appears to be a key molecular effector of NO during the EC migration and angiogenic processes, and is a potential therapeutic target for NO-associated vascular disorders. | es_ES |
dc.description.sponsorship | National Institutes of Health grant AR47074 (S.A.), Comunidad Autónoma de Madrid grants CAM 08.4/0023/2003 (C.Z.) and GR/SAL/0309/2004 (A.G.A.), Spanish Ministerio de Sanidad y Consumo grant CP03/00 025 (A.M.R.), and Spanish Ministerio de Educación y Ciencia grants SAF2005- 06025 (C.Z.), SAF2006-02410 (S.L.), and SAF2005-02228(A.G.A.). P.G. is a postdoctoral researcher from the “Juan de la Cierva” program (MCyT) and C.Z. is a research investigator from the “Ramón y Cajal” program (MCyT). | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | American Society of Hematology | es_ES |
dc.rights | closedAccess | es_ES |
dc.subject | membrane type 1–matrix metalloproteinase (MT1-MMP) | es_ES |
dc.subject | EC migration | es_ES |
dc.title | Functional interplay between endothelial nitric oxide synthase and membrane type 1–matrix metalloproteinase in migrating endothelial cells | es_ES |
dc.type | artículo | es_ES |
dc.identifier.doi | 10.1182/blood-2007-01-068080 | - |
dc.description.peerreviewed | Peer reviewed | es_ES |
dc.relation.publisherversion | http://bloodjournal.hematologylibrary.org/content/110/8/2916.full | es_ES |
dc.identifier.e-issn | 1528-0020 | - |
dc.identifier.pmid | 17606763 | - |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.openairetype | artículo | - |
item.grantfulltext | none | - |
item.cerifentitytype | Publications | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.fulltext | No Fulltext | - |
item.languageiso639-1 | en | - |
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