Gess, Bernhard and Hofbauer, Karl-Heinz and Wenger, Roland H. and Lohaus, Christiane and Meyer, Helmut E. and Kurtz, Armin (2003) The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-L alpha. EUROPEAN JOURNAL OF BIOCHEMISTRY, 270 (10). pp. 2228-2235. ISSN 0014-2956
Full text not available from this repository.Abstract
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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PROTEIN-DISULFIDE-ISOMERASE; HYPOXIA-INDUCIBLE FACTOR-1; MOUSE HEPATOMA-CELLS; PROLYL HYDROXYLATION; GENE-EXPRESSION; BOND FORMATION; RETICULUM; HIF; 4-HYDROXYLASE; INDUCTION; hypoxia; HIF; protein folding; UPR; PDI |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Physiologie > Prof. Dr. Armin Kurtz |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 11 Aug 2021 06:20 |
| Last Modified: | 11 Aug 2021 06:20 |
| URI: | https://pred.uni-regensburg.de/id/eprint/39025 |
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