PMID- 11278461
OWN - NLM
STAT- MEDLINE
DCOM- 20010712
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 276
IP  - 23
DP  - 2001 Jun 8
TI  - Characterization of a hypoxia-inducible factor (HIF-1alpha ) from rainbow trout. 
      Accumulation of protein occurs at normal venous oxygen tension.
PG  - 19699-705
AB  - 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% O(2) for 1 h. The greatest accumulation of 
      HIF-1alpha protein occurred at 5% O(2) (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.
FAU - Soitamo, A J
AU  - Soitamo AJ
AD  - Turku Centre for Biotechnology, University of Turku, Abo Akademi University, 
      FIN-20521 Turku, Finland. arto.soitamo@utu.fi
FAU - Rabergh, C M
AU  - Rabergh CM
FAU - Gassmann, M
AU  - Gassmann M
FAU - Sistonen, L
AU  - Sistonen L
FAU - Nikinmaa, M
AU  - Nikinmaa M
LA  - eng
SI  - GENBANK/AF304864
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20010309
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA Primers)
RN  - 0 (DNA, Complementary)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (HIF1A protein, human)
RN  - 0 (Hypoxia-Inducible Factor 1)
RN  - 0 (Hypoxia-Inducible Factor 1, alpha Subunit)
RN  - 0 (Nuclear Proteins)
RN  - 0 (RNA, Messenger)
RN  - 0 (Transcription Factors)
RN  - S88TT14065 (Oxygen)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Cells, Cultured
MH  - Cloning, Molecular
MH  - DNA Primers
MH  - DNA, Complementary
MH  - DNA-Binding Proteins/chemistry/genetics/*metabolism
MH  - Humans
MH  - Hypoxia-Inducible Factor 1
MH  - Hypoxia-Inducible Factor 1, alpha Subunit
MH  - Molecular Sequence Data
MH  - Nuclear Proteins/chemistry/genetics/*metabolism
MH  - Oncorhynchus mykiss
MH  - Oxygen/*metabolism
MH  - RNA, Messenger/genetics
MH  - Sequence Homology, Amino Acid
MH  - *Transcription Factors
EDAT- 2001/03/30 10:00
MHDA- 2001/07/13 10:01
CRDT- 2001/03/30 10:00
PHST- 2001/03/30 10:00 [pubmed]
PHST- 2001/07/13 10:01 [medline]
PHST- 2001/03/30 10:00 [entrez]
AID - S0021-9258(19)40395-5 [pii]
AID - 10.1074/jbc.M009057200 [doi]
PST - ppublish
SO  - J Biol Chem. 2001 Jun 8;276(23):19699-705. doi: 10.1074/jbc.M009057200. Epub 2001 
      Mar 9.