Abstract
Hypoxia-inducible factor 1 (HIF-1) is a heterodimeric basic helix-loop-helix (bHLH)-PAS DNA-binding protein tightly regulated by cellular oxygen tension. Cellular redox states are related to hypoxia by changes in the expression of redox regulated genes and the generation of reactive oxygen intermediates. Here, we provide evidence that alteration of cellular redox states by treating cells with H2O2 or dithiothreitol impairs hypoxia signaling mechanisms and the expression of HIF-1α protein in hypoxic cells. In addition, HIF-1 DNA-binding activity in vitro is sensitive to oxidizing reagents diamide and H2O2 and the alkylating agent N-ethylmaleimide. The activity of N-ethylmaleimide-inactivated HIF-1 can be partially restored by addition of nuclear extract from nonhypoxic cells.
Original language | English (US) |
---|---|
Pages (from-to) | 550-556 |
Number of pages | 7 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 212 |
Issue number | 2 |
DOIs | |
State | Published - Jul 17 1995 |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology