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rdf:type |
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lifeskim:mentions |
umls-concept:C0001443,
umls-concept:C0028128,
umls-concept:C0035820,
umls-concept:C0041637,
umls-concept:C0043314,
umls-concept:C0068355,
umls-concept:C0086418,
umls-concept:C0225336,
umls-concept:C0242184,
umls-concept:C0443199,
umls-concept:C0851285
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pubmed:issue |
3
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pubmed:dateCreated |
2003-6-11
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pubmed:abstractText |
Although in tissue injury following hypoxia/reoxygenation (H/R) an increased endothelial formation of superoxide anions (O(2)(-)) plays an important role, it is still not fully understood which of the potential enzymatic sources of endothelial O(2)(-) are crucially involved. In this study, we particularly examined the activities of NAD(P)H oxidase and xanthine oxidase (XO) after 8 h of exposure to mild hypoxia. We further studied whether enzyme activities can be modified by NO and adenosine during hypoxic treatment.
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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/Adenosine,
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Arrhythmia Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Chromans,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochromes c,
http://linkedlifedata.com/resource/pubmed/chemical/HOE 234,
http://linkedlifedata.com/resource/pubmed/chemical/NADPH Oxidase,
http://linkedlifedata.com/resource/pubmed/chemical/NOS3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase Type III,
http://linkedlifedata.com/resource/pubmed/chemical/Nitroarginine,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Pyrrolidines,
http://linkedlifedata.com/resource/pubmed/chemical/Reactive Oxygen Species,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxide Dismutase,
http://linkedlifedata.com/resource/pubmed/chemical/Xanthine Oxidase
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0008-6363
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
58
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
638-46
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:12798437-Adenosine,
pubmed-meshheading:12798437-Anoxia,
pubmed-meshheading:12798437-Anti-Arrhythmia Agents,
pubmed-meshheading:12798437-Cells, Cultured,
pubmed-meshheading:12798437-Chromans,
pubmed-meshheading:12798437-Cytochromes c,
pubmed-meshheading:12798437-Endothelium, Vascular,
pubmed-meshheading:12798437-Humans,
pubmed-meshheading:12798437-NADPH Oxidase,
pubmed-meshheading:12798437-Nitric Oxide,
pubmed-meshheading:12798437-Nitric Oxide Synthase,
pubmed-meshheading:12798437-Nitric Oxide Synthase Type III,
pubmed-meshheading:12798437-Nitroarginine,
pubmed-meshheading:12798437-Oxygen,
pubmed-meshheading:12798437-Potassium Channels,
pubmed-meshheading:12798437-Pyrrolidines,
pubmed-meshheading:12798437-Reactive Oxygen Species,
pubmed-meshheading:12798437-Superoxide Dismutase,
pubmed-meshheading:12798437-Xanthine Oxidase
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pubmed:year |
2003
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pubmed:articleTitle |
Differential regulation of xanthine and NAD(P)H oxidase by hypoxia in human umbilical vein endothelial cells. Role of nitric oxide and adenosine.
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pubmed:affiliation |
Medizinische Poliklinik Innenstadt, Ludwig-Maximilians-University Munich, Ziemssenstrasse 1, 80336, Munich, Germany. sohn@lrz.uni-muenchen.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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