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{{PBB|geneid=4051}}
{{Infobox_gene}}
{{SI}}
'''Leukotriene-B(4) omega-hydroxylase 2''' is an [[enzyme]] that in humans is encoded by the ''CYP4F3'' [[gene]].<ref name="pmid8486631">{{cite journal | vauthors = Kikuta Y, Kusunose E, Endo K, Yamamoto S, Sogawa K, Fujii-Kuriyama Y, Kusunose M | title = A novel form of cytochrome P-450 family 4 in human polymorphonuclear leukocytes. cDNA cloning and expression of leukotriene B4 omega-hydroxylase | journal = The Journal of Biological Chemistry | volume = 268 | issue = 13 | pages = 9376–80 | date = May 1993 | pmid = 8486631 | pmc =  | doi =  }}</ref><ref name="pmid9539102">{{cite journal | vauthors = Kikuta Y, Kato M, Yamashita Y, Miyauchi Y, Tanaka K, Kamada N, Kusunose M | title = Human leukotriene B4 omega-hydroxylase (CYP4F3) gene: molecular cloning and chromosomal localization | journal = DNA and Cell Biology | volume = 17 | issue = 3 | pages = 221–30 | date = March 1998 | pmid = 9539102 | pmc =  | doi = 10.1089/dna.1998.17.221 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CYP4F3 cytochrome P450, family 4, subfamily F, polypeptide 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4051| accessdate = }}</ref>  CYP4F3 encodes two distinct enzymes, '''CYP4F3A''' and '''CYP4F3B''', which originate from the [[alternative splicing]] of a single pre-mRNA precursor molecule; selection of either isoform is tissue-specific with CYP3F3A being expressed mostly in [[leukocytes]] and CYP4F3B mostly in the liver.<ref name  ="Corcos_12012">{{cite journal | vauthors = Corcos L, Lucas D, Le Jossic-Corcos C, Dréano Y, Simon B, Plée-Gautier E, Amet Y, Salaün JP | title = Human cytochrome P450 4F3: structure, functions, and prospects | journal = Drug Metabolism and Drug Interactions | volume = 27 | issue = 2 | pages = 63–71 | year = 2012 | pmid = 22706230 | doi = 10.1515/dmdi-2011-0037 }}</ref>
{{EH}}


'''Cytochrome P450, family 4, subfamily F, polypeptide 3''', also known as '''CYP4F3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CYP4F3 cytochrome P450, family 4, subfamily F, polypeptide 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4051| accessdate = }}</ref>
== Function ==


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids, fatty acids and other lipids. CYP4F3 actually encodes two splice-variants, CYP4F3A and CYP4F3B, of the cytochrome P450 superfamily of enzymes. The gene is part of a cluster of cytochrome P450 genes on chromosome 19. Another member of this family, CYP4F8, is approximately 18 kb away.<ref name="entrez" /> Both variants localize on the [[endoplasmic reticulum]] and metabolize [[leukotriene B4]] and very likely [[5-hydroxyeicosatetraenoic acid]], [[5-oxo-eicosatetraenoic acid]], and [[12-hydroxyeicosatetraenoic acid]] by an [[omega oxidation]] reaction, i.e. by adding a [[hydroxyl]] residue to their terminal (i.e. C-20) carbon.<ref>{{cite journal | vauthors = Powell WS, Rokach J | title = Biosynthesis, biological effects, and receptors of hydroxyeicosatetraenoic acids (HETEs) and oxoeicosatetraenoic acids (oxo-ETEs) derived from arachidonic acid | journal = Biochimica et Biophysica Acta | volume = 1851 | issue = 4 | pages = 340–55 | date = April 2015 | pmid = 25449650 | doi = 10.1016/j.bbalip.2014.10.008 }}</ref> This addition starts the process of inactivating and degrading all of these well-known mediators of [[inflammation]] and/or [[allery]].<ref name = "Johnson_2015">{{cite journal | vauthors = Johnson AL, Edson KZ, Totah RA, Rettie AE | title = Cytochrome P450 ω-Hydroxylases in Inflammation and Cancer | journal = Advances in Pharmacology | volume = 74 | pages = 223–62 | year = 2015 | pmid = 26233909 | doi = 10.1016/bs.apha.2015.05.002 | pmc=4667791}}</ref> CYP3FA is the major enzyme accomplishing these omega oxidations in leukocytes.<ref name = "Johnson_2015"/> The hydroxylation-induced inactivation of these mediators, perhaps particularly of leukotriene B4, may underlie the proposed roles of these cytochromes in dampening inflammatory responses as well as the reported associations of certain CYP4F3 [[single nucleotide variant]]s (SNPs) with human [[Krohn's disease]] (SNPs are designated Rs1290617<ref name="url_Rs1290617 - SNPedia">{{cite web | url = http://www.snpedia.com/index.php/Rs1290617 | title = Rs1290617 | format = | work = SNPedia  | accessdate = }}</ref> and  rs1290620<ref name="url_Rs1290620">{{cite web | url = https://www.ncbi.nlm.nih.gov/projects/SNP/snp_ref.cgi?rs=1290620 | title = Reference SNP (refSNP) Cluster Report: rs1290620 | format = | work = | accessdate = }}</ref> and [[Celiac disease]] (rs1290622 and rs1290625).<ref name  ="Corcos_12012"/><ref name="pmid16835590">{{cite journal | vauthors = Curley CR, Monsuur AJ, Wapenaar MC, Rioux JD, Wijmenga C | title = A functional candidate screen for coeliac disease genes | journal = European Journal of Human Genetics | volume = 14 | issue = 11 | pages = 1215–22 | year = 2006 | pmid = 16835590 | doi = 10.1038/sj.ejhg.5201687 }}</ref><ref name="Costea_2014">{{cite journal | vauthors = Costea I, Mack DR, Lemaitre RN, Israel D, Marcil V, Ahmad A, Amre DK | title = Interactions between the dietary polyunsaturated fatty acid ratio and genetic factors determine susceptibility to pediatric Crohn's disease | journal = Gastroenterology | volume = 146 | issue = 4 | pages = 929–31 | date = April 2014 | pmid = 24406470 | doi = 10.1053/j.gastro.2013.12.034 }}</ref><ref name="Costea_2014"/><ref>{{cite journal | vauthors = Kikuta Y, Kusunose E, Sumimoto H, Mizukami Y, Takeshige K, Sakaki T, Yabusaki Y, Kusunose M | title = Purification and characterization of recombinant human neutrophil leukotriene B4 omega-hydroxylase (cytochrome P450 4F3) | journal = Archives of Biochemistry and Biophysics | volume = 355 | issue = 2 | pages = 201–5 | date = July 1998 | pmid = 9675028 | doi = 10.1006/abbi.1998.0724 }}</ref><ref name="pmid18433732">{{cite journal | vauthors = Hardwick JP | title = Cytochrome P450 omega hydroxylase (CYP4) function in fatty acid metabolism and metabolic diseases | journal = Biochemical Pharmacology | volume = 75 | issue = 12 | pages = 2263–75 | date = June 2008 | pmid = 18433732 | doi = 10.1016/j.bcp.2008.03.004 }}</ref>
{{PBB_Summary
| section_title =
| summary_text = This gene, CYP4F3, 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. The enzyme starts the process of inactivating and degrading leukotriene B4, a potent mediator of inflammation. This gene is part of a cluster of cytochrome P450 genes on chromosome 19. Another member of this family, CYP4F8, is approximately 18 kb away.<ref name="entrez">{{cite web | title = Entrez Gene: CYP4F3 cytochrome P450, family 4, subfamily F, polypeptide 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4051| accessdate = }}</ref>
}}


==References==
CYP4F3A and/or CYP43B also omega oxidize [[arachidonic acid]] to [[20-Hydroxyeicosatetraenoic acid]] (20-HETE) as well as [[epoxyeicosatrienoic acid]]s (EETs) to 20-hydroxy-EETs.<ref name = "Johnson_2015"/> 20-HETE regulates blood flow, vascularization, blood pressure, and kidney tubule absorption of ions in rodents and possibly humans;<ref name  ="Corcos_12012"/> it has also been proposed to be involved in regulating the growth of various types of human cancers (see [[20-Hydroxyeicosatetraenoic acid#cancer]]). EETS have a similar set of regulatory functions but often act in a manner opposite to 20-HETE (see [[epoxyeicosatrienoic acid#cancer]]); since, however, the activities of the 20-HEETs have not been well-defined, the function of EET omega oxidation is unclear.<ref name  ="Corcos_12012"/>
 
== References ==
{{reflist}}
{{reflist}}
==Further reading==
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Simpson AE | title = The cytochrome P450 4 (CYP4) family | journal = General Pharmacology | volume = 28 | issue = 3 | pages = 351–9 | date = March 1997 | pmid = 9068972 | doi = 10.1016/S0306-3623(96)00246-7 }}
| citations =
* {{cite journal | vauthors = Kikuta Y, Kusunose E, Kondo T, Yamamoto S, Kinoshita H, Kusunose M | title = Cloning and expression of a novel form of leukotriene B4 omega-hydroxylase from human liver | journal = FEBS Letters | volume = 348 | issue = 1 | pages = 70–4 | date = July 1994 | pmid = 8026587 | doi = 10.1016/0014-5793(94)00587-7 }}
*{{cite journal | author=Simpson AE |title=The cytochrome P450 4 (CYP4) family. |journal=Gen. Pharmacol. |volume=28 |issue= 3 |pages= 351–9 |year= 1997 |pmid= 9068972 |doi= }}
* {{cite journal | vauthors = Christmas P, Ursino SR, Fox JW, Soberman RJ | title = Expression of the CYP4F3 gene. tissue-specific splicing and alternative promoters generate high and low K(m) forms of leukotriene B(4) omega-hydroxylase | journal = The Journal of Biological Chemistry | volume = 274 | issue = 30 | pages = 21191–9 | date = July 1999 | pmid = 10409674 | doi = 10.1074/jbc.274.30.21191 }}
*{{cite journal | author=Kikuta Y, Kusunose E, Kondo T, ''et al.'' |title=Cloning and expression of a novel form of leukotriene B4 omega-hydroxylase from human liver. |journal=FEBS Lett. |volume=348 |issue= 1 |pages= 70–4 |year= 1994 |pmid= 8026587 |doi= }}
* {{cite journal | vauthors = Christmas P, Jones JP, Patten CJ, Rock DA, Zheng Y, Cheng SM, Weber BM, Carlesso N, Scadden DT, Rettie AE, Soberman RJ | title = Alternative splicing determines the function of CYP4F3 by switching substrate specificity | journal = The Journal of Biological Chemistry | volume = 276 | issue = 41 | pages = 38166–72 | date = October 2001 | pmid = 11461919 | doi = 10.1074/jbc.M104818200 }}
*{{cite journal  | author=Kikuta Y, Kusunose E, Endo K, ''et al.'' |title=A novel form of cytochrome P-450 family 4 in human polymorphonuclear leukocytes. cDNA cloning and expression of leukotriene B4 omega-hydroxylase. |journal=J. Biol. Chem. |volume=268 |issue= 13 |pages= 9376–80 |year= 1993 |pmid= 8486631 |doi=  }}
* {{cite journal | vauthors = Christmas P, Carlesso N, Shang H, Cheng SM, Weber BM, Preffer FI, Scadden DT, Soberman RJ | title = Myeloid expression of cytochrome P450 4F3 is determined by a lineage-specific alternative promoter | journal = The Journal of Biological Chemistry | volume = 278 | issue = 27 | pages = 25133–42 | date = July 2003 | pmid = 12709424 | doi = 10.1074/jbc.M302106200 }}
*{{cite journal  | author=Kikuta Y, Kato M, Yamashita Y, ''et al.'' |title=Human leukotriene B4 omega-hydroxylase (CYP4F3) gene: molecular cloning and chromosomal localization. |journal=DNA Cell Biol. |volume=17 |issue= 3 |pages= 221–30 |year= 1998 |pmid= 9539102 |doi=  }}
* {{cite journal | vauthors = Mizukami Y, Sumimoto H, Takeshige K | title = Induction of cytochrome CYP4F3A in all-trans-retinoic acid-treated HL60 cells | journal = Biochemical and Biophysical Research Communications | volume = 314 | issue = 1 | pages = 104–9 | date = January 2004 | pmid = 14715252 | doi = 10.1016/j.bbrc.2003.12.062 }}
*{{cite journal | author=Christmas P, Ursino SR, Fox JW, Soberman RJ |title=Expression of the CYP4F3 gene. tissue-specific splicing and alternative promoters generate high and low K(m) forms of leukotriene B(4) omega-hydroxylase. |journal=J. Biol. Chem. |volume=274 |issue= 30 |pages= 21191–9 |year= 1999 |pmid= 10409674 |doi= }}
* {{cite journal | vauthors = Christmas P, Tolentino K, Primo V, Berry KZ, Murphy RC, Chen M, Lee DM, Soberman RJ | title = Cytochrome P-450 4F18 is the leukotriene B4 omega-1/omega-2 hydroxylase in mouse polymorphonuclear leukocytes: identification as the functional orthologue of human polymorphonuclear leukocyte CYP4F3A in the down-regulation of responses to LTB4 | journal = The Journal of Biological Chemistry | volume = 281 | issue = 11 | pages = 7189–96 | date = March 2006 | pmid = 16380383 | doi = 10.1074/jbc.M513101200 }}
*{{cite journal | author=Christmas P, Jones JP, Patten CJ, ''et al.'' |title=Alternative splicing determines the function of CYP4F3 by switching substrate specificity. |journal=J. Biol. Chem. |volume=276 |issue= 41 |pages= 38166–72 |year= 2001 |pmid= 11461919 |doi= 10.1074/jbc.M104818200 }}
*{{cite journal | author=Christmas P, Carlesso N, Shang H, ''et al.'' |title=Myeloid expression of cytochrome P450 4F3 is determined by a lineage-specific alternative promoter. |journal=J. Biol. Chem. |volume=278 |issue= 27 |pages= 25133–42 |year= 2003 |pmid= 12709424 |doi= 10.1074/jbc.M302106200 }}
*{{cite journal | author=Mizukami Y, Sumimoto H, Takeshige K |title=Induction of cytochrome CYP4F3A in all-trans-retinoic acid-treated HL60 cells. |journal=Biochem. Biophys. Res. Commun. |volume=314 |issue= 1 |pages= 104–9 |year= 2004 |pmid= 14715252 |doi= }}
*{{cite journal | author=Christmas P, Tolentino K, Primo V, ''et al.'' |title=Cytochrome P-450 4F18 is the leukotriene B4 omega-1/omega-2 hydroxylase in mouse polymorphonuclear leukocytes: identification as the functional orthologue of human polymorphonuclear leukocyte CYP4F3A in the down-regulation of responses to LTB4. |journal=J. Biol. Chem. |volume=281 |issue= 11 |pages= 7189–96 |year= 2006 |pmid= 16380383 |doi= 10.1074/jbc.M513101200 }}
}}
{{refend}}
{{refend}}


{{SIB}}
{{Cytochrome P450}}
 
{{Leukotriene signaling modulators}}
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Latest revision as of 04:13, 27 October 2017

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Leukotriene-B(4) omega-hydroxylase 2 is an enzyme that in humans is encoded by the CYP4F3 gene.[1][2][3] CYP4F3 encodes two distinct enzymes, CYP4F3A and CYP4F3B, which originate from the alternative splicing of a single pre-mRNA precursor molecule; selection of either isoform is tissue-specific with CYP3F3A being expressed mostly in leukocytes and CYP4F3B mostly in the liver.[4]

Function

The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids, fatty acids and other lipids. CYP4F3 actually encodes two splice-variants, CYP4F3A and CYP4F3B, of the cytochrome P450 superfamily of enzymes. The gene is part of a cluster of cytochrome P450 genes on chromosome 19. Another member of this family, CYP4F8, is approximately 18 kb away.[3] Both variants localize on the endoplasmic reticulum and metabolize leukotriene B4 and very likely 5-hydroxyeicosatetraenoic acid, 5-oxo-eicosatetraenoic acid, and 12-hydroxyeicosatetraenoic acid by an omega oxidation reaction, i.e. by adding a hydroxyl residue to their terminal (i.e. C-20) carbon.[5] This addition starts the process of inactivating and degrading all of these well-known mediators of inflammation and/or allery.[6] CYP3FA is the major enzyme accomplishing these omega oxidations in leukocytes.[6] The hydroxylation-induced inactivation of these mediators, perhaps particularly of leukotriene B4, may underlie the proposed roles of these cytochromes in dampening inflammatory responses as well as the reported associations of certain CYP4F3 single nucleotide variants (SNPs) with human Krohn's disease (SNPs are designated Rs1290617[7] and rs1290620[8] and Celiac disease (rs1290622 and rs1290625).[4][9][10][10][11][12]

CYP4F3A and/or CYP43B also omega oxidize arachidonic acid to 20-Hydroxyeicosatetraenoic acid (20-HETE) as well as epoxyeicosatrienoic acids (EETs) to 20-hydroxy-EETs.[6] 20-HETE regulates blood flow, vascularization, blood pressure, and kidney tubule absorption of ions in rodents and possibly humans;[4] it has also been proposed to be involved in regulating the growth of various types of human cancers (see 20-Hydroxyeicosatetraenoic acid#cancer). EETS have a similar set of regulatory functions but often act in a manner opposite to 20-HETE (see epoxyeicosatrienoic acid#cancer); since, however, the activities of the 20-HEETs have not been well-defined, the function of EET omega oxidation is unclear.[4]

References

  1. ↑ Kikuta Y, Kusunose E, Endo K, Yamamoto S, Sogawa K, Fujii-Kuriyama Y, Kusunose M (May 1993). "A novel form of cytochrome P-450 family 4 in human polymorphonuclear leukocytes. cDNA cloning and expression of leukotriene B4 omega-hydroxylase". The Journal of Biological Chemistry. 268 (13): 9376–80. PMID 8486631.
  2. ↑ Kikuta Y, Kato M, Yamashita Y, Miyauchi Y, Tanaka K, Kamada N, Kusunose M (March 1998). "Human leukotriene B4 omega-hydroxylase (CYP4F3) gene: molecular cloning and chromosomal localization". DNA and Cell Biology. 17 (3): 221–30. doi:10.1089/dna.1998.17.221. PMID 9539102.
  3. ↑ 3.0 3.1 "Entrez Gene: CYP4F3 cytochrome P450, family 4, subfamily F, polypeptide 3".
  4. ↑ 4.0 4.1 4.2 4.3 Corcos L, Lucas D, Le Jossic-Corcos C, Dréano Y, Simon B, Plée-Gautier E, Amet Y, Salaün JP (2012). "Human cytochrome P450 4F3: structure, functions, and prospects". Drug Metabolism and Drug Interactions. 27 (2): 63–71. doi:10.1515/dmdi-2011-0037. PMID 22706230.
  5. ↑ Powell WS, Rokach J (April 2015). "Biosynthesis, biological effects, and receptors of hydroxyeicosatetraenoic acids (HETEs) and oxoeicosatetraenoic acids (oxo-ETEs) derived from arachidonic acid". Biochimica et Biophysica Acta. 1851 (4): 340–55. doi:10.1016/j.bbalip.2014.10.008. PMID 25449650.
  6. ↑ 6.0 6.1 6.2 Johnson AL, Edson KZ, Totah RA, Rettie AE (2015). "Cytochrome P450 ω-Hydroxylases in Inflammation and Cancer". Advances in Pharmacology. 74: 223–62. doi:10.1016/bs.apha.2015.05.002. PMC 4667791. PMID 26233909.
  7. ↑ "Rs1290617". SNPedia.
  8. ↑ "Reference SNP (refSNP) Cluster Report: rs1290620".
  9. ↑ Curley CR, Monsuur AJ, Wapenaar MC, Rioux JD, Wijmenga C (2006). "A functional candidate screen for coeliac disease genes". European Journal of Human Genetics. 14 (11): 1215–22. doi:10.1038/sj.ejhg.5201687. PMID 16835590.
  10. ↑ 10.0 10.1 Costea I, Mack DR, Lemaitre RN, Israel D, Marcil V, Ahmad A, Amre DK (April 2014). "Interactions between the dietary polyunsaturated fatty acid ratio and genetic factors determine susceptibility to pediatric Crohn's disease". Gastroenterology. 146 (4): 929–31. doi:10.1053/j.gastro.2013.12.034. PMID 24406470.
  11. ↑ Kikuta Y, Kusunose E, Sumimoto H, Mizukami Y, Takeshige K, Sakaki T, Yabusaki Y, Kusunose M (July 1998). "Purification and characterization of recombinant human neutrophil leukotriene B4 omega-hydroxylase (cytochrome P450 4F3)". Archives of Biochemistry and Biophysics. 355 (2): 201–5. doi:10.1006/abbi.1998.0724. PMID 9675028.
  12. ↑ Hardwick JP (June 2008). "Cytochrome P450 omega hydroxylase (CYP4) function in fatty acid metabolism and metabolic diseases". Biochemical Pharmacology. 75 (12): 2263–75. doi:10.1016/j.bcp.2008.03.004. PMID 18433732.

Further reading

  • Simpson AE (March 1997). "The cytochrome P450 4 (CYP4) family". General Pharmacology. 28 (3): 351–9. doi:10.1016/S0306-3623(96)00246-7. PMID 9068972.
  • Kikuta Y, Kusunose E, Kondo T, Yamamoto S, Kinoshita H, Kusunose M (July 1994). "Cloning and expression of a novel form of leukotriene B4 omega-hydroxylase from human liver". FEBS Letters. 348 (1): 70–4. doi:10.1016/0014-5793(94)00587-7. PMID 8026587.
  • Christmas P, Ursino SR, Fox JW, Soberman RJ (July 1999). "Expression of the CYP4F3 gene. tissue-specific splicing and alternative promoters generate high and low K(m) forms of leukotriene B(4) omega-hydroxylase". The Journal of Biological Chemistry. 274 (30): 21191–9. doi:10.1074/jbc.274.30.21191. PMID 10409674.
  • Christmas P, Jones JP, Patten CJ, Rock DA, Zheng Y, Cheng SM, Weber BM, Carlesso N, Scadden DT, Rettie AE, Soberman RJ (October 2001). "Alternative splicing determines the function of CYP4F3 by switching substrate specificity". The Journal of Biological Chemistry. 276 (41): 38166–72. doi:10.1074/jbc.M104818200. PMID 11461919.
  • Christmas P, Carlesso N, Shang H, Cheng SM, Weber BM, Preffer FI, Scadden DT, Soberman RJ (July 2003). "Myeloid expression of cytochrome P450 4F3 is determined by a lineage-specific alternative promoter". The Journal of Biological Chemistry. 278 (27): 25133–42. doi:10.1074/jbc.M302106200. PMID 12709424.
  • Mizukami Y, Sumimoto H, Takeshige K (January 2004). "Induction of cytochrome CYP4F3A in all-trans-retinoic acid-treated HL60 cells". Biochemical and Biophysical Research Communications. 314 (1): 104–9. doi:10.1016/j.bbrc.2003.12.062. PMID 14715252.
  • Christmas P, Tolentino K, Primo V, Berry KZ, Murphy RC, Chen M, Lee DM, Soberman RJ (March 2006). "Cytochrome P-450 4F18 is the leukotriene B4 omega-1/omega-2 hydroxylase in mouse polymorphonuclear leukocytes: identification as the functional orthologue of human polymorphonuclear leukocyte CYP4F3A in the down-regulation of responses to LTB4". The Journal of Biological Chemistry. 281 (11): 7189–96. doi:10.1074/jbc.M513101200. PMID 16380383.


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