CYP4F8
| CYP4F8 | |||
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| Location (UCSC) | Chr 19: 15.62 – 15.63 Mb | Chr 17: 32.9 – 32.92 Mb | |||||||
| PubMed search | [3] | [4] | |||||||
| View/Edit Human | View/Edit Mouse |
Cytochrome P450 4F8 is a protein that in humans is encoded by the CYP4F8 gene.[5][6]
Function
This gene, CYP4F8, 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 protein localizes to the endoplasmic reticulum and functions as a 19-hydroxylase of the
In addition to its ability to metabolize and presumably thereby to inactivate or reduce the activity of PGH2 and PGH1, CYP4F8 adds
CYP4F8 has little activity in omega-hydroxylating
The fatty acid metabolizing activity, including the ability to form epoxides, of CYP4F8 is very similar to that of CYP4F12. However, it and CYP4F12 are not regarded as being major contributors in forming the cited epoxides in humans although they might do so in tissues where they are highly expressed.[8]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000186526 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000073424 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- PMID 10405341.
- ^ a b "Entrez Gene: CYP4F8 cytochrome P450, family 4, subfamily F, polypeptide 8".
- PMID 16112640.
- ^ PMID 26233909.
- ^ PMID 21945326.
- ^ S2CID 39465144.
- PMID 24345640.
- PMID 26621325.
- ^ PMID 25240260.
- PMID 24634501.
- PMID 18433732.
Further reading
- Simpson AE (March 1997). "The cytochrome P450 4 (CYP4) family". General Pharmacology. 28 (3): 351–9. PMID 9068972.
- Bylund J, Hidestrand M, Ingelman-Sundberg M, Oliw EH (July 2000). "Identification of CYP4F8 in human seminal vesicles as a prominent 19-hydroxylase of prostaglandin endoperoxides". The Journal of Biological Chemistry. 275 (29): 21844–9. PMID 10791960.
- Oliw EH, Stark K, Bylund J (August 2001). "Oxidation of prostaglandin H(2) and prostaglandin H(2) analogues by human cytochromes P450: analysis of omega-side chain hydroxy metabolites and four steroisomers of 5-hydroxyprostaglandin I(1) by mass spectrometry". Biochemical Pharmacology. 62 (4): 407–15. PMID 11448449.
- Stark K, Törmä H, Cristea M, Oliw EH (January 2003). "Expression of CYP4F8 (prostaglandin H 19-hydroxylase) in human epithelia and prominent induction in epidermis of psoriatic lesions". Archives of Biochemistry and Biophysics. 409 (1): 188–96. PMID 12464258.
- Stark K, Bylund J, Törmä H, Sahlén G, Oliw EH (January 2005). "On the mechanism of biosynthesis of 19-hydroxyprostaglandins of human seminal fluid and expression of cyclooxygenase-2, PGH 19-hydroxylase (CYP4F8) and microsomal PGE synthase-1 in seminal vesicles and vas deferens". Prostaglandins & Other Lipid Mediators. 75 (1–4): 47–64. PMID 15789615.
- Stark K, Wongsud B, Burman R, Oliw EH (September 2005). "Oxygenation of polyunsaturated long chain fatty acids by recombinant CYP4F8 and CYP4F12 and catalytic importance of Tyr-125 and Gly-328 of CYP4F8". Archives of Biochemistry and Biophysics. 441 (2): 174–81. PMID 16112640.