Factor Inhibiting HIF Asparaginyl Hydroxylase Inhibitors

Factor Inhibiting HIF (FIH) Asparaginyl Hydroxylase Inhibitors inhibit the FIH pathway also catalyzed by Asparaginyl Hydroxylase inhibition. Before 2010s thought to be identical to HIF prolyl-hydroxylase pathway, studies have shown FIH to be the master regulator (relative to HIF) that controls HIF transcriptional activity in an oxygen-dependent manner.[1] and that HIF prolyl-hydroxylase inhibitors may only minimally inhibit FIH. Skeletal muscle expresses 50-fold higher levels of FIH than other tissues.[1]

The cytoplasmic tail of MT1-MMP, which can bind to FIH-1, promotes inhibition of FIH-1 during normoxia.[2]

  1. ^ a b Sim, Jingwei; Cowburn, Andrew S.; Palazon, Asis; Madhu, Basetti; Tyrakis, Petros A.; Macías, David; Bargiela, David M.; Pietsch, Sandra; Gralla, Michael; Evans, Colin E.; Kittipassorn, Thaksaon (2018-04-03). "The Factor Inhibiting HIF Asparaginyl Hydroxylase Regulates Oxidative Metabolism and Accelerates Metabolic Adaptation to Hypoxia". Cell Metabolism. 27 (4): 898–913.e7. doi:10.1016/j.cmet.2018.02.020. ISSN 1550-4131. PMC 5887987. PMID 29617647. Text was copied from this source, which is available under a Creative Commons Attribution 4.0 International License.
  2. ^ Knapinska, Anna M.; Fields, Gregg B. (2019-05-20). "The Expanding Role of MT1-MMP in Cancer Progression". Pharmaceuticals. 12 (2): 77. doi:10.3390/ph12020077. ISSN 1424-8247. PMC 6630478. PMID 31137480.