Cytochrome P450 26A1 is a protein that in humans is encoded by the CYP26A1gene.[5][6][7]
Function
This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This endoplasmic reticulum protein acts on retinoids, including all-trans-retinoic acid (RA), with both 4-hydroxylation and 18-hydroxylation activities. This enzyme regulates the cellular level of retinoic acid which is involved in regulation of gene expression in both embryonic and adult tissues. Two alternatively spliced transcript variants of this gene, which encode the distinct isoforms, have been reported.[7]
CYP26A1 is over-expressed in colorectal cancer cells compared to normal colonic epithelium but is of no independent prognostic value in patients with colorectal cancer.[8]
Sonneveld E, van den Brink CE, van der Leede BM, Schulkes RK, Petkovich M, van der Burg B, van der Saag PT (August 1998). "Human retinoic acid (RA) 4-hydroxylase (CYP26) is highly specific for all-trans-RA and can be induced through RA receptors in human breast and colon carcinoma cells". Cell Growth & Differentiation. 9 (8): 629–37. PMID9716180.
Trofimova-Griffin ME, Juchau MR (November 1998). "Expression of cytochrome P450RAI (CYP26) in human fetal hepatic and cephalic tissues". Biochemical and Biophysical Research Communications. 252 (2): 487–91. doi:10.1006/bbrc.1998.9659. PMID9826557.
Popa C, Dicker AJ, Dahler AL, Saunders NA (September 1999). "Cytochrome P450, CYP26AI, is expressed at low levels in human epidermal keratinocytes and is not retinoic acid-inducible". The British Journal of Dermatology. 141 (3): 460–8. doi:10.1046/j.1365-2133.1999.03039.x. PMID10583049. S2CID19697736.
McSorley LC, Daly AK (August 2000). "Identification of human cytochrome P450 isoforms that contribute to all-trans-retinoic acid 4-hydroxylation". Biochemical Pharmacology. 60 (4): 517–26. doi:10.1016/S0006-2952(00)00356-7. PMID10874126.
Won JY, Nam EC, Yoo SJ, Kwon HJ, Um SJ, Han HS, Kim SH, Byun Y, Kim SY (August 2004). "The effect of cellular retinoic acid binding protein-I expression on the CYP26-mediated catabolism of all-trans retinoic acid and cell proliferation in head and neck squamous cell carcinoma". Metabolism. 53 (8): 1007–12. doi:10.1016/j.metabol.2003.12.015. PMID15281009.
Ozpolat B, Mehta K, Lopez-Berestein G (October 2005). "Regulation of a highly specific retinoic acid-4-hydroxylase (CYP26A1) enzyme and all-trans-retinoic acid metabolism in human intestinal, liver, endothelial, and acute promyelocytic leukemia cells". Leukemia & Lymphoma. 46 (10): 1497–506. doi:10.1080/10428190500174737. PMID16194896. S2CID12269201.
Rat E, Billaut-Laden I, Allorge D, Lo-Guidice JM, Tellier M, Cauffiez C, Jonckheere N, van Seuningen I, Lhermitte M, Romano A, Guéant JL, Broly F (June 2006). "Evidence for a functional genetic polymorphism of the human retinoic acid-metabolizing enzyme CYP26A1, an enzyme that may be involved in spina bifida". Birth Defects Research. Part A, Clinical and Molecular Teratology. 76 (6): 491–8. doi:10.1002/bdra.20275. PMID16933217.
Gomaa MS, Yee SW, Milbourne CE, Barbera MC, Simons C, Brancale A (August 2006). "Homology model of human retinoic acid metabolising enzyme cytochrome P450 26A1 (CYP26A1): active site architecture and ligand binding". Journal of Enzyme Inhibition and Medicinal Chemistry. 21 (4): 361–9. doi:10.1080/14756360600742014. PMID17059167. S2CID20519075.
