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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2000-8-24
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pubmed:abstractText |
Hsp70 is induced by hypoxia in most mammalian cell types and contributes to their ability to survive hypoxic episodes. However, little is known about Hsp70 expression in the hypoxia-tolerant endothelial cells (ECs). We investigated the effect of hypoxia on Hsp70 in human microvascular endothelial HMEC-1 cells. Reduction of pO(2) to 2.5% of normal for 20 h stimulated lactate production and the activity of glycolytic enzymes. This metabolic adaptation to hypoxia was accompanied by a remarkable reduction of Hsp70 on the protein level and on the mRNA level. Approximately 12 h after the hypoxic period Hsp70 expression reached pre-hypoxia levels again. Since ECs are adapted to the low oxygen tension of the vasculature they are confronted with a supraphysiological oxygen level during in vitro culture. We suppose that the high Hsp70 under these conditions reflects a stress response which disappears at the more physiological reduced oxygen tension during hypoxia.
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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/Blood Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lactic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NOS3 protein, human,
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/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/STOM protein, human
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2000 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
542-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10913374-Atmosphere Exposure Chambers,
pubmed-meshheading:10913374-Blood Proteins,
pubmed-meshheading:10913374-Blotting, Northern,
pubmed-meshheading:10913374-Blotting, Western,
pubmed-meshheading:10913374-Cell Hypoxia,
pubmed-meshheading:10913374-Cell Line,
pubmed-meshheading:10913374-Cell Survival,
pubmed-meshheading:10913374-Down-Regulation,
pubmed-meshheading:10913374-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:10913374-Endothelium, Vascular,
pubmed-meshheading:10913374-Energy Metabolism,
pubmed-meshheading:10913374-Glycolysis,
pubmed-meshheading:10913374-HSP70 Heat-Shock Proteins,
pubmed-meshheading:10913374-Heat-Shock Response,
pubmed-meshheading:10913374-Humans,
pubmed-meshheading:10913374-Lactic Acid,
pubmed-meshheading:10913374-Membrane Proteins,
pubmed-meshheading:10913374-Microcirculation,
pubmed-meshheading:10913374-Models, Biological,
pubmed-meshheading:10913374-Nitric Oxide Synthase,
pubmed-meshheading:10913374-Nitric Oxide Synthase Type III,
pubmed-meshheading:10913374-RNA, Messenger
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pubmed:year |
2000
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pubmed:articleTitle |
Endothelial cells downregulate expression of the 70 kDa heat shock protein during hypoxia.
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pubmed:affiliation |
Surgical Research Laboratories, University of Vienna, Vienna, A-1090, Austria. rudolf.oehler@akh-wien.ac.at
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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