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http://purl.uniprot.org/citations/15670768http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15670768http://www.w3.org/2000/01/rdf-schema#comment"Activated matrix metalloproteinases (MMPs) in patients with acute coronary syndromes may contribute to plaque destabilization. Since reactive oxygen species (ROS) induce MMP-2 and angiotensin II (ANG II) enhances NADPH-oxidase-dependent ROS formation, we assessed whether ANG II induces MMP-2 in a NADPH-oxidase-dependent manner. MMP-2 mRNA expression and activity were analyzed in wildtype and p47phox-deficient (p47phox-/-) murine smooth muscle cells (SMC). To address a clinical implication, sections of human atherosclerotic arteries were stained for MMP-2, p47phox, ANG II, AT1-receptor, and alpha-smooth muscle cell actin (alpha-SMC actin). MMP-2 protein expression and activity from these arteries were compared to those without atherosclerosis. ANG II enhances mRNA synthesis and activity of MMP-2 in a p47phox-dependent manner. Immunohistochemical analyses revealed a co-localization of MMP-2 with p47phox, ANG II, AT1-receptor, and alpha-SMC actin. MMP-2 protein expression and gelatinolytic activity are increased in atherosclerotic arteries. Thus, activation of the renin-angiotensin system may contribute to plaque destabilization via ROS-dependent induction of MMP-2."xsd:string
http://purl.uniprot.org/citations/15670768http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2004.12.152"xsd:string
http://purl.uniprot.org/citations/15670768http://purl.uniprot.org/core/author"Drexler H."xsd:string
http://purl.uniprot.org/citations/15670768http://purl.uniprot.org/core/author"Grote K."xsd:string
http://purl.uniprot.org/citations/15670768http://purl.uniprot.org/core/author"Haverich A."xsd:string
http://purl.uniprot.org/citations/15670768http://purl.uniprot.org/core/author"Luchtefeld M."xsd:string
http://purl.uniprot.org/citations/15670768http://purl.uniprot.org/core/author"Schieffer B."xsd:string
http://purl.uniprot.org/citations/15670768http://purl.uniprot.org/core/author"Bavendiek U."xsd:string
http://purl.uniprot.org/citations/15670768http://purl.uniprot.org/core/author"Grothusen C."xsd:string
http://purl.uniprot.org/citations/15670768http://purl.uniprot.org/core/author"Selle T."xsd:string
http://purl.uniprot.org/citations/15670768http://purl.uniprot.org/core/author"Bandlow N."xsd:string
http://purl.uniprot.org/citations/15670768http://purl.uniprot.org/core/author"Bley S."xsd:string
http://purl.uniprot.org/citations/15670768http://purl.uniprot.org/core/author"Struber M."xsd:string
http://purl.uniprot.org/citations/15670768http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15670768http://purl.uniprot.org/core/name"Biochem Biophys Res Commun"xsd:string
http://purl.uniprot.org/citations/15670768http://purl.uniprot.org/core/pages"183-188"xsd:string
http://purl.uniprot.org/citations/15670768http://purl.uniprot.org/core/title"Angiotensin II induces MMP-2 in a p47phox-dependent manner."xsd:string
http://purl.uniprot.org/citations/15670768http://purl.uniprot.org/core/volume"328"xsd:string
http://purl.uniprot.org/citations/15670768http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15670768
http://purl.uniprot.org/citations/15670768http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15670768
http://purl.uniprot.org/uniprot/#_F8WH69-mappedCitation-15670768http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15670768
http://purl.uniprot.org/uniprot/#_Q09014-mappedCitation-15670768http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15670768
http://purl.uniprot.org/uniprot/#_Q3UG07-mappedCitation-15670768http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15670768
http://purl.uniprot.org/uniprot/#_P33434-mappedCitation-15670768http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15670768