Regulation of Hypoxia-Inducible Factor 1α Expression and Function by the Mammalian Target of Rapamycin

By Christine C. Hudson, Mei Liu, G. Chiang, D. Otterness, Dawn C. Loomis, F. Kaper, Amato J. Giaccia, R. Abraham. Molecular and Cellular Biology, 2002

1,171 citations recorded by the source corpus.

Subfields: Cancer Research, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/db68ec3cd3177c319163ede8cff9d6df4ae1f026

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Citations in the corpus

Regulation of mTOR function in response to hypoxia by REDD1 and the TSC1/TSC2 tumor suppressor complex. (2004, background): “Hif up-regulation in Tsc2-deficient cells is likely to result from increased mTOR activity as mTOR increases Hif stability and increased Hif levels in Tsc2-deficient cells can be normalized by treatment with rapamycin (Hudson et al. 2002; Brugarolas et al. 2003).”
HIF-1 mediates metabolic responses to intratumoral hypoxia and oncogenic mutations. (2013, neutral): “…α synthesis as a result of PI3K and AKT signaling that stimulates mTOR activity, which stimulates translation of HIF1A mRNA into protein by phosphorylation of eIF4E binding protein (78, 80). mTOR has also been reported to stimulate HIF-1 α stabilization and transactivation domain function (81).”
mTOR- and HIF-1α–mediated aerobic glycolysis as metabolic basis for trained immunity (2014, positive): “On the basis of observations that mTOR induction of glycolysis is mediated through activation of HIF-1a and stimulation of glycolytic enzymes (24) and that rapamycin inhibits HIF-1a expression (25), we assessed the effect of a HIF-1a inhibitor on monocyte training.”
Vascular endothelial growth factor in eye disease. (2008, background): “Under normoxic conditions, HIF-1α is inactivated and targeted for proteasomal degradation by hydroxylation, whereas under hypoxic conditions the specific hydroxylases are inhibited, resulting in the rescue of HIF-1α from degradation (Schofield and Ratcliffe, 2004).”
Hypoxia-inducible factor determines sensitivity to inhibitors of mTOR in kidney cancer (2006, background): “HIF protein expression is dependent on mTOR in certain cellular context”
Targeting the phosphoinositide 3-kinase (PI3K) pathway in cancer (2009, background): “From a mechanistic perspective, rapamycin inhibits mTORC1-dependent translation and action of HIF1A, and thereby decreases VEGF productio”
Therapeutic targeting of hypoxia and hypoxia-inducible factors in cancer. (2016, background): “…et al., 2001 LY94002 PI3K Jiang et al., 2001; Mohlin et al., 2015 GDC-0941 PI3K Mohlin et al., 2015 PI-103 PI3K Mohlin et al., 2015 Rapamycin mTOR Hudson et al., 2002 PP242 mTOR Mohlin et al., 2015 Aminoflavone unknown Terzuoli et al., 2010 Glyceollins AKT/mTOR, Hsp90 Lee et al., 2015 Topotecan,…”
The mTOR Signalling Pathway in Human Cancer (2012, background): “In addition, mTORC1 is also involved in the regulation of other proteins including CLIP-170 (cytoplasm linker protein-170) [22], eEF2 (eukaryotic elongation factor 2) kinase [23], ODC (ornithine decarboxylase) [24], glycogen synthase [25], HIF-1 α (hypoxia-inducible factor 1α) [26], lipin [27],”
Randomized phase II study of multiple dose levels of CCI-779, a novel mammalian target of rapamycin kinase inhibitor, in patients with advanced refractory renal cell carcinoma. (2004, background): “mTOR activation increases HIF-1 gene expression at both the levels of mRNA translation and protein stabilization [33].”
IL‐1β mediated up‐regulation of HIF‐lα via an NFkB/COX‐2 pathway identifies HIF‐1 as a critical link between inflammation and oncogenesis (2003, background): “Furthermore, HIF-1α has been reported to be regulated by a mTOR-dependent pathway (61).”