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http://purl.uniprot.org/citations/18157936http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18157936http://www.w3.org/2000/01/rdf-schema#comment"Mitochondrial aldehyde dehydrogenase (ALDH-2) reduces reactive oxygen species (ROS) formation related to toxic aldehydes; additionally, it provides a bioactivating pathway for nitroglycerin. Since acetaldehyde, nitroglycerin, and doxorubicin treatment provoke mitochondrial oxidative stress, we used ALDH-2(-/-) mice and purified recombinant human ALDH-2 to test the hypothesis that ALDH-2 has an indirect antioxidant function in mitochondria. Antioxidant capacity of purified ALDH-2 was comparable to equimolar doses of glutathione, cysteine, and dithiothreitol; mitochondrial oxidative stress was comparable in C57Bl6 and ALDH-2(-/-) mice after acute challenges with nitroglycerin or doxorubicin, whereas chronic acetaldehyde, nitroglycerin, and doxorubicin treatment dose-dependently increased mitochondrial ROS formation and impaired endothelial function to a greater extent in ALDH-2(-/-) mice. Maximal nitroglycerin dose applied in vivo lead to a "super-desensitized" nitroglycerin response in isolated ALDH-2(-/-) aortas, inaccessible in C57Bl6 mice. Our results suggest that ALDH-2 has an indirect antioxidative property independent of its thiol-moiety in disease states of cardiovascular oxidative stress."xsd:string
http://purl.uniprot.org/citations/18157936http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2007.12.089"xsd:string
http://purl.uniprot.org/citations/18157936http://purl.uniprot.org/core/author"Kawamoto T."xsd:string
http://purl.uniprot.org/citations/18157936http://purl.uniprot.org/core/author"Muller J."xsd:string
http://purl.uniprot.org/citations/18157936http://purl.uniprot.org/core/author"Schulz E."xsd:string
http://purl.uniprot.org/citations/18157936http://purl.uniprot.org/core/author"Pautz A."xsd:string
http://purl.uniprot.org/citations/18157936http://purl.uniprot.org/core/author"Wojnowski L."xsd:string
http://purl.uniprot.org/citations/18157936http://purl.uniprot.org/core/author"Wenzel P."xsd:string
http://purl.uniprot.org/citations/18157936http://purl.uniprot.org/core/author"Kleinert H."xsd:string
http://purl.uniprot.org/citations/18157936http://purl.uniprot.org/core/author"Munzel T."xsd:string
http://purl.uniprot.org/citations/18157936http://purl.uniprot.org/core/author"Oelze M."xsd:string
http://purl.uniprot.org/citations/18157936http://purl.uniprot.org/core/author"Daiber A."xsd:string
http://purl.uniprot.org/citations/18157936http://purl.uniprot.org/core/author"Schuhmacher S."xsd:string
http://purl.uniprot.org/citations/18157936http://purl.uniprot.org/core/author"Zurmeyer S."xsd:string
http://purl.uniprot.org/citations/18157936http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18157936http://purl.uniprot.org/core/name"Biochem Biophys Res Commun"xsd:string
http://purl.uniprot.org/citations/18157936http://purl.uniprot.org/core/pages"137-143"xsd:string
http://purl.uniprot.org/citations/18157936http://purl.uniprot.org/core/title"ALDH-2 deficiency increases cardiovascular oxidative stress--evidence for indirect antioxidative properties."xsd:string
http://purl.uniprot.org/citations/18157936http://purl.uniprot.org/core/volume"367"xsd:string
http://purl.uniprot.org/citations/18157936http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18157936
http://purl.uniprot.org/citations/18157936http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18157936
http://purl.uniprot.org/uniprot/#_A0A0G2JEU1-mappedCitation-18157936http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18157936
http://purl.uniprot.org/uniprot/#_D3YYF3-mappedCitation-18157936http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18157936
http://purl.uniprot.org/uniprot/#_A0A0G2JF60-mappedCitation-18157936http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18157936