Abstract
Nuclear extracts from Drosophila SL2 cells were found to contain a hypoxically inducible complex capable of binding to hypoxia response elements from mammalian genes. This complex (HIF-D) resembled mammalian hypoxia inducible factor (HIF-1) in DNA sequence specificity, abrogation of induction by cycloheximide, induction by desferrioxamine and redox sensitivity of DNA binding. However, HIF-D was not induced by cobalt and was less sensitive to phosphatase than HIF-1. Endogenous phosphoglycerate kinase mRNA in SL2 cells showed similar inducible characteristics to HIF-D. These findings are evidence that the mammalian HIF-1 dependent system of oxygen regulated gene expression has a functional homologue in Drosophila.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Base Sequence
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Binding Sites
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Cell Hypoxia
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Cell Line
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Cobalt / pharmacology
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Cycloheximide / pharmacology
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DNA Probes
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism*
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Deferoxamine / pharmacology
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Dithiothreitol / pharmacology
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Drosophila melanogaster / cytology
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Drosophila melanogaster / metabolism*
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HeLa Cells
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Humans
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Hypoxia-Inducible Factor 1
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Hypoxia-Inducible Factor 1, alpha Subunit
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Mice
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Molecular Sequence Data
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Nuclear Proteins / metabolism
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Phosphoglycerate Kinase / genetics
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Phosphoglycerate Kinase / metabolism
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Phosphoric Monoester Hydrolases / metabolism
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Transcription Factors*
Substances
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DNA Probes
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DNA-Binding Proteins
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HIF1A protein, human
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Hif1a protein, mouse
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Hypoxia-Inducible Factor 1
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Hypoxia-Inducible Factor 1, alpha Subunit
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Nuclear Proteins
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Transcription Factors
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Cobalt
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Cycloheximide
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Phosphoglycerate Kinase
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Phosphoric Monoester Hydrolases
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Deferoxamine
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Dithiothreitol