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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2003-5-19
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pubmed:abstractText |
The formation of disulfide bonds in the endoplasmic reticulum requires protein disulfide isomerase (PDI) and endoplasmic reticulum oxidoreductin 1 (ERO1) that reoxidizes PDI. We report here that the expression of the rat, mouse and human homologues of ERO1-Like protein alpha but not of the isoform ERO1-Lbeta are stimulated by hypoxia in rats vivo and in rat, mouse and human cell cultures. The temporal pattern of hypoxic ERO1-Lalpha induction is very similar to that of genes triggered by the hypoxia inducible transcription factor (HIF-1) and is characteristically mimicked by cobalt and by deferoxamine, but is absent in cells with a defective aryl hydrocarbon receptor translocator (ARNT, HIF-1beta). We speculate from these findings that the expression of ERO1-Lalpha is probably regulated via the HIF-pathway and thus belongs to the family of classic oxygen regulated genes. Activation of the unfolded protein response (UPR) by tunicamycin, on the other hand, strongly induced ERO1-Lbeta and more moderately ERO1-Lalpha expression. The expression of the two ERO1-L isoforms therefore appears to be differently regulated, in the way that ERO1-Lalpha expression is mainly controlled by the cellular oxygen tension, whilst ERO1-Lbeta is triggered mainly by UPR. The physiological meaning of the oxygen regulation of ERO1-Lalpha expression likely is to maintain the transfer rate of oxidizing equivalents to PDI in situations of an altered cellular redox state induced by changes of the cellular oxygen tension.
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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/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Adrenomedullin,
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Disulfides,
http://linkedlifedata.com/resource/pubmed/chemical/ERO1L protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Ero1l protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Tunicamycin
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0014-2956
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2228-35
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:12752442-Actins,
pubmed-meshheading:12752442-Adrenomedullin,
pubmed-meshheading:12752442-Animals,
pubmed-meshheading:12752442-Anoxia,
pubmed-meshheading:12752442-Anti-Bacterial Agents,
pubmed-meshheading:12752442-Aorta,
pubmed-meshheading:12752442-Cells, Cultured,
pubmed-meshheading:12752442-Cloning, Molecular,
pubmed-meshheading:12752442-DNA, Complementary,
pubmed-meshheading:12752442-Disulfides,
pubmed-meshheading:12752442-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:12752442-Endoplasmic Reticulum,
pubmed-meshheading:12752442-Glycoproteins,
pubmed-meshheading:12752442-Humans,
pubmed-meshheading:12752442-Membrane Glycoproteins,
pubmed-meshheading:12752442-Mice,
pubmed-meshheading:12752442-Models, Biological,
pubmed-meshheading:12752442-Muscle, Smooth,
pubmed-meshheading:12752442-Oxidoreductases,
pubmed-meshheading:12752442-Oxygen,
pubmed-meshheading:12752442-Peptides,
pubmed-meshheading:12752442-Protein Folding,
pubmed-meshheading:12752442-Protein Isoforms,
pubmed-meshheading:12752442-RNA,
pubmed-meshheading:12752442-RNA, Messenger,
pubmed-meshheading:12752442-Rats,
pubmed-meshheading:12752442-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:12752442-Ribonucleases,
pubmed-meshheading:12752442-Time Factors,
pubmed-meshheading:12752442-Tumor Cells, Cultured,
pubmed-meshheading:12752442-Tunicamycin
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pubmed:year |
2003
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pubmed:articleTitle |
The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-Lalpha.
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pubmed:affiliation |
Institut für Physiologie der Universität Regensburg, Germany.
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pubmed:publicationType |
Journal Article
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