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https://hdl.handle.net/2440/9694
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Full metadata record
DC Field | Value | Language |
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dc.contributor.author | Lang, K. | - |
dc.contributor.author | Kappel, A. | - |
dc.contributor.author | Goodall, G. | - |
dc.contributor.editor | Wickens, M.P. | - |
dc.date.issued | 2002 | - |
dc.identifier.citation | Molecular Biology of the Cell, 2002; 13(5):1792-1801 | - |
dc.identifier.issn | 1059-1524 | - |
dc.identifier.issn | 1939-4586 | - |
dc.identifier.uri | http://hdl.handle.net/2440/9694 | - |
dc.description | Copyright © 2002 by The American Society for Cell Biology | - |
dc.description.abstract | HIF-1α is the regulated subunit of the HIF-1 transcription factor, which induces transcription of a number of genes involved in the cellular response to hypoxia. The HIF-1α protein is rapidly degraded in cells supplied with adequate oxygen but is stabilized in hypoxic cells. Using polysome profile analysis, we found that translation of HIF-1α mRNA in NIH3T3 cells is spared the general reduction in translation rate that occurs during hypoxia. To assess whether the 5'UTR of the HIF-1α mRNA contains an internal ribosome entry site (IRES), we constructed a dicistronic reporter with the HIF-1α 5'UTR inserted between two reporter coding regions. We found that the HIF-1α 5'UTR promoted translation of the downstream reporter, indicating the presence of an IRES. The IRES had activity comparable to that of the well-characterized c-myc IRES. IRES activity was not affected by hypoxic conditions that caused a reduction in cap-dependent translation, and IRES activity was less affected by serum-starvation than was cap-dependent translation. These data indicate that the presence of an IRES in the HIF-1α 5'UTR allows translation to be maintained under conditions that are inhibitory to cap-dependent translation. | - |
dc.description.statementofresponsibility | Kenneth J. D. Lang, Andreas Kappel, and Gregory J. Goodall | - |
dc.language.iso | en | - |
dc.publisher | Amer Soc Cell Biology | - |
dc.source.uri | http://dx.doi.org/10.1091/mbc.02-02-0017 | - |
dc.subject | Hela Cells | - |
dc.subject | 3T3 Cells | - |
dc.subject | Ribosomes | - |
dc.subject | Animals | - |
dc.subject | Humans | - |
dc.subject | Mice | - |
dc.subject | Oxygen | - |
dc.subject | Intercellular Signaling Peptides and Proteins | - |
dc.subject | Vascular Endothelial Growth Factors | - |
dc.subject | Vascular Endothelial Growth Factor A | - |
dc.subject | Endothelial Growth Factors | - |
dc.subject | Transcription Factors | - |
dc.subject | RNA, Messenger | - |
dc.subject | 5' Untranslated Regions | - |
dc.subject | Lymphokines | - |
dc.subject | Culture Media, Serum-Free | - |
dc.subject | Protein Biosynthesis | - |
dc.subject | Genes, myc | - |
dc.subject | Hypoxia-Inducible Factor 1, alpha Subunit | - |
dc.subject | Hypoxia | - |
dc.title | Hypoxia-inducible factor-1a mRNA contains an internal ribosome entry site that allows efficient translation during normoxia and hypoxia | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1091/mbc.02-02-0017 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Goodall, G. [0000-0003-1294-0692] | - |
Appears in Collections: | Aurora harvest 4 Medicine publications |
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