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]

History

FIH and the PHDs (HIF prolyl-hydroxylase) share some enzymatic properties, including cofactors and by-products, this has led to the assumption that PHDs and FIH are functionally redundant in their regulation of HIF. It has also been difficult to account for FIH's distinct evolutionary history as an oxygen sensor.^[1]

Inhibitors

1,4-DPCA (1,4-dihydrophenonthrolin-4-one-3carboxylicacid)^[3]

References

^ ^a ^b ^c 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.
^ 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.
^ Love, Ryan J.; Jones, Kim S. (December 2013). "Transient inhibition of connective tissue infiltration and collagen deposition into porous poly(lactic- co -glycolic acid) discs: Inhibition of Connective Tissue Growth into PLGA Discs". Journal of Biomedical Materials Research Part A. 101 (12): 3599–3606. doi:10.1002/jbm.a.34648. PMID 23766241.

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[PMC5887987-1] 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.

[3] Love, Ryan J.; Jones, Kim S. (December 2013). "Transient inhibition of connective tissue infiltration and collagen deposition into porous poly(lactic- co -glycolic acid) discs: Inhibition of Connective Tissue Growth into PLGA Discs". Journal of Biomedical Materials Research Part A. 101 (12): 3599–3606. doi:10.1002/jbm.a.34648. PMID 23766241.

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