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Originally published In Press as doi:10.1074/jbc.M009057200 on March 9, 2001

J. Biol. Chem., Vol. 276, Issue 23, 19699-19705, June 8, 2001
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Characterization of a Hypoxia-inducible Factor (HIF-1alpha ) from Rainbow Trout
ACCUMULATION OF PROTEIN OCCURS AT NORMAL VENOUS OXYGEN TENSION*

Arto J. SoitamoDagger §, Christina M. I. RåberghDagger §, Max Gassmann||, Lea SistonenDagger **, and Mikko Nikinmaa§

From the Dagger  Turku Centre for Biotechnology, University of Turku, Åbo Akademi University, FIN-20521 Turku, Finland, § Department of Biology, Laboratory of Animal Physiology, University of Turku, FIN-20014 Turku, Finland, ** Department of Biology, Åbo Akademi University, FIN-20521 Turku, Finland, and || Institute of Physiology, University of Zürich-Irchel, CH-8057, Switzerland

The mammalian hypoxia-inducible factor-1 (HIF-1) is a heterodimeric transcription factor that controls the induction of several genes involved in glycolysis, erythropoiesis, and angiogenesis when cells are exposed to hypoxic conditions. Until now, the expression and function of HIF-1alpha have not been studied in fish, which experience wide fluctuations of oxygen tensions in their natural environment. Using electrophoretic mobility shift assay, we have ascertained that a hypoxia-inducible factor is present in rainbow trout cells. We have also cloned the full-length cDNA (3605 base pairs) of the HIF-1alpha from rainbow trout with a predicted protein sequence of 766 amino acids that showed a 61% similarity to human and mouse HIF-1alpha . Polyclonal antibodies against the N-terminal part (amino acids 12-363) and the C-terminal part (amino acids 330-730) of rainbow trout HIF-1alpha protein recognized rainbow trout and chinook salmon HIF-1alpha protein in Western blot analysis. Also, the human and mouse HIF-1alpha proteins were recognized by the N-terminal rainbow trout anti-HIF-1alpha antibody but not by the C-terminal HIF-1alpha antibody. The accumulation of HIF-1alpha was studied by incubating rainbow trout and chinook salmon cells at different oxygen concentrations from 20 to 0.2% O2 for 1 h. The greatest accumulation of HIF-1alpha protein occurred at 5% O2 (38 torr), a typical oxygen tension of venous blood in normoxic animals. The protein stability experiments in the absence or presence of a proteasome inhibitor, MG-132, demonstrated that the inhibitor is able to stabilize the protein, which normally is degraded via the proteasome pathway both in normoxia and hypoxia. Notably, the hypoxia response element of oxygen-dependent degradation domain is identical in mammalian, Xenopus, and rainbow trout HIF-1alpha proteins, suggesting a high degree of evolutionary conservation in degradation of HIF-1alpha protein.

* This work was supported by the Academy of Finland.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF304864.

To whom all correspondence should be addressed: Arto Soitamo, Dept. of Biology, Laboratory of Animal Physiology, University of Turku, FIN-20014 Turku, Finland. Tel.: 358-2-333-5780; Fax: 358-2-333-6598; E-mail: arto.soitamo@utu.fi.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.