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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2003-10-16
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pubmed:abstractText |
Rapamycin is a clinically approved immunosuppressive agent that has recently shown promising antitumor activities in human patients. In contrast to many conventional chemotherapeutic agents, rapamycin displays a remarkably high level of selectivity for certain types of tumors. The pharmacological activities of rapamycin are attributable to the functional inhibition of a single target protein, termed the mammalian target of rapamycin (mTOR). Because mTOR is widely expressed in both normal and transformed cells, variations in mTOR expression levels are likely not a primary determinant of tumor sensitivity to rapamycin. However, recent studies highlighted an intriguing link between cancer cell sensitivity to rapamycin and deregulated signaling through the phosphoinositide (PI) 3-kinase pathway. These findings have prompted a search for cancer-related responses that are jointly regulated by the PI 3-kinase signaling cascade and mTOR. The oxygen-regulated transcription factor, hypoxia-induced factor (HIF)-1, has emerged as a candidate target for both of these two highly interactive signaling proteins. Here we review evidence that mTOR functions as a positive regulator of HIF-1-dependent responses to hypoxic stress in human cancer cells.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibiotics, Antineoplastic,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HIF1A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Hypoxia-Inducible Factor 1,
http://linkedlifedata.com/resource/pubmed/chemical/Hypoxia-Inducible Factor 1, alpha...,
http://linkedlifedata.com/resource/pubmed/chemical/MTOR protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Sirolimus,
http://linkedlifedata.com/resource/pubmed/chemical/TOR Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:issn |
0070-217X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
279
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
299-319
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:14560965-Animals,
pubmed-meshheading:14560965-Antibiotics, Antineoplastic,
pubmed-meshheading:14560965-Cell Hypoxia,
pubmed-meshheading:14560965-DNA-Binding Proteins,
pubmed-meshheading:14560965-Humans,
pubmed-meshheading:14560965-Hypoxia-Inducible Factor 1,
pubmed-meshheading:14560965-Hypoxia-Inducible Factor 1, alpha Subunit,
pubmed-meshheading:14560965-Neoplasms,
pubmed-meshheading:14560965-Nuclear Proteins,
pubmed-meshheading:14560965-Protein Kinases,
pubmed-meshheading:14560965-Sirolimus,
pubmed-meshheading:14560965-TOR Serine-Threonine Kinases,
pubmed-meshheading:14560965-Transcription, Genetic,
pubmed-meshheading:14560965-Transcription Factors,
pubmed-meshheading:14560965-Tumor Cells, Cultured
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pubmed:year |
2004
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pubmed:articleTitle |
mTOR as a positive regulator of tumor cell responses to hypoxia.
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pubmed:affiliation |
Program in Signal Transduction Research, The Burnham Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA. abraham@burnham.org
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pubmed:publicationType |
Journal Article,
Review
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