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{{PBB|geneid=29785}}
{{PBB|geneid=29785}}
'''Cytochrome P450 2S1''' is a [[protein]] that in humans is encoded by the ''CYP2S1'' [[gene]].<ref name="pmid11181079">{{cite journal | author = Rylander T, Neve EP, Ingelman-Sundberg M, Oscarson M | title = Identification and tissue distribution of the novel human cytochrome P450 2S1 (CYP2S1) | journal = Biochem Biophys Res Commun | volume = 281 | issue = 2 | pages = 529–35 |date=Feb 2001 | pmid = 11181079 | pmc = | doi = 10.1006/bbrc.2001.4390 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CYP2S1 cytochrome P450, family 2, subfamily S, polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29785| accessdate = }}</ref>
'''Cytochrome P450 2S1''' is a [[protein]] that in humans is encoded by the ''CYP2S1'' [[gene]].<ref name="pmid11181079">{{cite journal | vauthors = Rylander T, Neve EP, Ingelman-Sundberg M, Oscarson M | title = Identification and tissue distribution of the novel human cytochrome P450 2S1 (CYP2S1) | journal = Biochemical and Biophysical Research Communications | volume = 281 | issue = 2 | pages = 529–35 | date = Feb 2001 | pmid = 11181079 | pmc = | doi = 10.1006/bbrc.2001.4390 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CYP2S1 cytochrome P450, family 2, subfamily S, polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29785| accessdate = }}</ref>


== Function ==
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
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| summary_text = 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 protein localizes to the endoplasmic reticulum. In rodents, the homologous protein has been shown to metabolize certain carcinogens; however, the specific function of the human protein has not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: CYP2S1 cytochrome P450, family 2, subfamily S, polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29785| accessdate = }}</ref>
}}


⚫
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 protein localizes to the endoplasmic reticulum. In rodents, the homologous protein has been shown to metabolize certain carcinogens; however, the specific function of the human protein has not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: CYP2S1 cytochrome P450, family 2, subfamily S, polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29785| accessdate = }}</ref>
⚫
CYP2S1 has recently been assigned [[epoxygenase]] activity. It metabolizes '''1)''' [[arachidonic acid]] to its various epoxides, i.e., the [[epoxyeicosatrienoic acid]]s (also termed EETs); '''2)''' [[docosahexaenoic acid]] to its various epoxides, i.e. the [[epoxydocosapentaenoic acid]]s (also termed EDPs); and '''3)''' linoleic acid to its various epoxides, i.e. [[vernolic acid]] (also termed leukotoxin) and [[coronaric acid]] (also termed isoleukotoxin).<ref>Basic Res Cardiol. 2013 Jan;108(1):319. doi: 10.1007/s00395-012-0319-8. Epub 2012 Dec 7.PMID: 23224081</ref> It seems likely, although not yet tested, that CYP231 will also prove able to metabolize other [[polyunsaturated fatty acid]]s to their epoxides; for example, the enzyme may metabolize [[eicosapentaenoic acid]] to epoxyeicosatetraenoic acids (also termed EEQs). Animal model studies implicate these epoxides in reducing [[hypertension]], protecting against [[Myocardial infarction]] and other insults to the heart, promoting the growth of various cancers, inhibiting [[inflammation]], stimulating blood vessel formation, and modulating [[Neurohormone]] release to block pain perception; limited studies suggest but have not proven that these epoxides may function similarly in humans (see [[epoxyeicosatrienoic acid]], [[epoxydocosapentaenoic acid]], and [[epoxygenase]] pages).<ref>Biochim Biophys Acta. 2015 Apr;1851(4):356-65. doi: 10.1016/j.bbalip.2014.07.020. Epub 2014 Aug 2. Review.PMID 25093613</ref> Vernolic and coronaric acids are potentially toxic, causing multiple organ failure and respiratory distress when injected into animals.<ref>Biochim Biophys Acta. 2015 Apr;1851(4):356-65. doi: 10.1016/j.bbalip.2014.07.020. Epub 2014 Aug 2. Review.PMID: 25093613</ref>


CYP2S1 has recently been assigned [[epoxygenase]] activity. It metabolizes '''1)''' [[arachidonic acid]] to its various epoxides, i.e., the [[epoxyeicosatrienoic acid]]s (also termed EETs); '''2)''' [[docosahexaenoic acid]] to its various epoxides, i.e. the [[epoxydocosapentaenoic acid]]s (also termed EDPs); and '''3)''' linoleic acid to its various epoxides, i.e. [[vernolic acid]] (also termed leukotoxin) and [[coronaric acid]] (also termed isoleukotoxin).<ref name = "Frömel_2013" >{{cite journal | vauthors = Frömel T, Kohlstedt K, Popp R, Yin X, Awwad K, Barbosa-Sicard E, Thomas AC, Lieberz R, Mayr M, Fleming I | title = Cytochrome P4502S1: a novel monocyte/macrophage fatty acid epoxygenase in human atherosclerotic plaques | journal = Basic Research in Cardiology | volume = 108 | issue = 1 | pages = 319 | date = Jan 2013 | pmid = 23224081 | doi = 10.1007/s00395-012-0319-8 }}</ref>
⚫
CYP2S1 has also been found to metabolize [[Prostaglandin G2]] and [[Prostaglandin H2]] to the biologically active product, [[12-Hydroxyheptadecatrienoic acid]] (i.e. 12(S)-hydroxyheptadeca-5Z,8E,10E-trienoic acid, also termed 12-HHT).<ref>Basic Res Cardiol. 2013 Jan;108(1):319. doi: 10.1007/s00395-012-0319-8. Epub 2012 Dec 7.PMID: 23224081</ref>


⚫
It seems likely, although not yet tested, that CYP231 will also prove able to metabolize other [[polyunsaturated fatty acid]]s to their epoxides; for example, the enzyme may metabolize [[eicosapentaenoic acid]] to epoxyeicosatetraenoic acids (also termed EEQs). Animal model studies implicate these epoxides in reducing [[hypertension]], protecting against [[Myocardial infarction]] and other insults to the heart, promoting the growth of various cancers, inhibiting [[inflammation]], stimulating blood vessel formation, and modulating [[Neurohormone]] release to block pain perception; limited studies suggest but have not proven that these epoxides may function similarly in humans (see [[epoxyeicosatrienoic acid]], [[epoxydocosapentaenoic acid]], and [[epoxygenase]] pages).<ref name = "Spector_2015">{{cite journal | vauthors = Spector AA, Kim HY | title = Cytochrome P450 epoxygenase pathway of polyunsaturated fatty acid metabolism | journal = Biochimica et Biophysica Acta | volume = 1851 | issue = 4 | pages = 356–65 | date = Apr 2015 | pmid = 25093613 | doi = 10.1016/j.bbalip.2014.07.020 }}</ref> Vernolic and coronaric acids are potentially toxic, causing multiple organ failure and respiratory distress when injected into animals.<ref name = "Spector_2015"/>
⚫
==References==

⚫
CYP2S1 has also been found to metabolize [[Prostaglandin G2]] and [[Prostaglandin H2]] to the biologically active product, [[12-Hydroxyheptadecatrienoic acid]] (i.e. 12(S)-hydroxyheptadeca-5Z,8E,10E-trienoic acid, also termed 12-HHT).<ref name = "Frömel_2013" />

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== References ==
{{reflist}}
{{reflist}}

==Further reading==
== Further reading ==
{{refbegin | 2}}
{{refbegin|33em}}
{{PBB_Further_reading
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* {{cite journal | vauthors = Adams MD, Kerlavage AR, Fleischmann RD, Fuldner RA, Bult CJ, Lee NH, Kirkness EF, Weinstock KG, Gocayne JD, White O | title = Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence | journal = Nature | volume = 377 | issue = 6547 Suppl | pages = 3–174 | date = Sep 1995 | pmid = 7566098 | doi = <!-- none available --> | url = http://www.columbia.edu/itc/biology/pollack/w4065/client_edit/readings/nature377_3.pdf | format = PDF }}
| citations =
⚫
* {{cite journal | vauthors = Smith G, Wolf CR, Deeni YY, Dawe RS, Evans AT, Comrie MM, Ferguson J, Ibbotson SH | title = Cutaneous expression of cytochrome P450 CYP2S1: individuality in regulation by therapeutic agents for psoriasis and other skin diseases | journal = Lancet | volume = 361 | issue = 9366 | pages = 1336–43 | date = Apr 2003 | pmid = 12711469 | doi = 10.1016/S0140-6736(03)13081-4 }}
⚫
*{{cite journal | author=Adams MD, Kerlavage AR, Fleischmann RD |title=Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence. |journal=Nature |volume=377 |issue= 6547 Suppl |pages= 3–174 |year= 1995 |pmid= 7566098 |doi=<!-- none available --> |url=http://www.columbia.edu/itc/biology/pollack/w4065/client_edit/readings/nature377_3.pdf | format=PDF |display-authors=etal}}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}}
* {{cite journal | vauthors = Saito S, Iida A, Sekine A, Kawauchi S, Higuchi S, Ogawa C, Nakamura Y | title = Catalog of 680 variations among eight cytochrome p450 ( CYP) genes, nine esterase genes, and two other genes in the Japanese population | journal = Journal of Human Genetics | volume = 48 | issue = 5 | pages = 249–70 | year = 2003 | pmid = 12721789 | doi = 10.1007/s10038-003-0021-7 }}
* {{cite journal | vauthors = Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A | title = The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment | journal = Genome Research | volume = 13 | issue = 10 | pages = 2265–70 | date = Oct 2003 | pmid = 12975309 | pmc = 403697 | doi = 10.1101/gr.1293003 }}
⚫
*{{cite journal | author=Smith G, Wolf CR, Deeni YY |title=Cutaneous expression of cytochrome P450 CYP2S1: individuality in regulation by therapeutic agents for psoriasis and other skin diseases. |journal=Lancet |volume=361 |issue= 9366 |pages= 1336–43 |year= 2003 |pmid= 12711469 |doi=10.1016/S0140-6736(03)13081-4 |display-authors=etal}}
*{{cite journal | author=Saito S, Iida A, Sekine A |title=Catalog of 680 variations among eight cytochrome p450 ( CYP) genes, nine esterase genes, and two other genes in the Japanese population. |journal=J. Hum. Genet. |volume=48 |issue= 5 |pages= 249–70 |year= 2003 |pmid= 12721789 |doi= 10.1007/s10038-003-0021-7 |display-authors=etal}}
* {{cite journal | vauthors = Rivera SP, Wang F, Saarikoski ST, Taylor RT, Chapman B, Zhang R, Hankinson O | title = A novel promoter element containing multiple overlapping xenobiotic and hypoxia response elements mediates induction of cytochrome P4502S1 by both dioxin and hypoxia | journal = The Journal of Biological Chemistry | volume = 282 | issue = 15 | pages = 10881–93 | date = Apr 2007 | pmid = 17277313 | doi = 10.1074/jbc.M609617200 }}
*{{cite journal | author=Clark HF, Gurney AL, Abaya E |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265–70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 | pmc=403697 |display-authors=etal}}
* {{cite journal | vauthors = Marek CJ, Tucker SJ, Koruth M, Wallace K, Wright MC | title = Expression of CYP2S1 in human hepatic stellate cells | journal = FEBS Letters | volume = 581 | issue = 4 | pages = 781–6 | date = Feb 2007 | pmid = 17280660 | doi = 10.1016/j.febslet.2007.01.056 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
* {{cite journal | vauthors = Hanzawa Y, Sasaki T, Hiratsuka M, Ishikawa M, Mizugaki M | title = Three novel single nucleotide polymorphisms (SNPs) of CYP2S1 gene in Japanese individuals | journal = Drug Metabolism and Pharmacokinetics | volume = 22 | issue = 2 | pages = 136–40 | date = Apr 2007 | pmid = 17495422 | doi = 10.2133/dmpk.22.136 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |display-authors=etal}}
* {{cite journal | vauthors = Jang YJ, Cha EY, Kim WY, Park SW, Shon JH, Lee SS, Shin JG | title = CYP2S1 gene polymorphisms in a Korean population | journal = Therapeutic Drug Monitoring | volume = 29 | issue = 3 | pages = 292–8 | date = Jun 2007 | pmid = 17529885 | doi = 10.1097/FTD.0b013e318058a4e0 }}
*{{cite journal | author=Rivera SP, Wang F, Saarikoski ST |title=A novel promoter element containing multiple overlapping xenobiotic and hypoxia response elements mediates induction of cytochrome P4502S1 by both dioxin and hypoxia. |journal=J. Biol. Chem. |volume=282 |issue= 15 |pages= 10881–93 |year= 2007 |pmid= 17277313 |doi= 10.1074/jbc.M609617200 |display-authors=etal}}
*{{cite journal | author=Marek CJ, Tucker SJ, Koruth M |title=Expression of CYP2S1 in human hepatic stellate cells. |journal=FEBS Lett. |volume=581 |issue= 4 |pages= 781–6 |year= 2007 |pmid= 17280660 |doi= 10.1016/j.febslet.2007.01.056 |display-authors=etal}}
*{{cite journal | author=Hanzawa Y, Sasaki T, Hiratsuka M |title=Three novel single nucleotide polymorphisms (SNPs) of CYP2S1 gene in Japanese individuals. |journal=Drug Metab. Pharmacokinet. |volume=22 |issue= 2 |pages= 136–40 |year= 2007 |pmid= 17495422 |doi=10.2133/dmpk.22.136 |display-authors=etal}}
*{{cite journal | author=Jang YJ, Cha EY, Kim WY |title=CYP2S1 gene polymorphisms in a Korean population. |journal=Therapeutic drug monitoring |volume=29 |issue= 3 |pages= 292–8 |year= 2007 |pmid= 17529885 |doi= 10.1097/FTD.0b013e318058a4e0 |display-authors=etal}}
}}
{{refend}}
{{refend}}
{{Cytochrome P450}}
{{Cytochrome P450}}


{{gene-19-stub}}
{{gene-19-stub}}

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Revision as of 20:18, 8 March 2016

Template:PBB Cytochrome P450 2S1 is a protein that in humans is encoded by the CYP2S1 gene.[1][2]

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 protein localizes to the endoplasmic reticulum. In rodents, the homologous protein has been shown to metabolize certain carcinogens; however, the specific function of the human protein has not been determined.[2]

CYP2S1 has recently been assigned epoxygenase activity. It metabolizes 1) arachidonic acid to its various epoxides, i.e., the epoxyeicosatrienoic acids (also termed EETs); 2) docosahexaenoic acid to its various epoxides, i.e. the epoxydocosapentaenoic acids (also termed EDPs); and 3) linoleic acid to its various epoxides, i.e. vernolic acid (also termed leukotoxin) and coronaric acid (also termed isoleukotoxin).[3]

It seems likely, although not yet tested, that CYP231 will also prove able to metabolize other polyunsaturated fatty acids to their epoxides; for example, the enzyme may metabolize eicosapentaenoic acid to epoxyeicosatetraenoic acids (also termed EEQs). Animal model studies implicate these epoxides in reducing hypertension, protecting against Myocardial infarction and other insults to the heart, promoting the growth of various cancers, inhibiting inflammation, stimulating blood vessel formation, and modulating Neurohormone release to block pain perception; limited studies suggest but have not proven that these epoxides may function similarly in humans (see epoxyeicosatrienoic acid, epoxydocosapentaenoic acid, and epoxygenase pages).[4] Vernolic and coronaric acids are potentially toxic, causing multiple organ failure and respiratory distress when injected into animals.[4]

CYP2S1 has also been found to metabolize Prostaglandin G2 and Prostaglandin H2 to the biologically active product, 12-Hydroxyheptadecatrienoic acid (i.e. 12(S)-hydroxyheptadeca-5Z,8E,10E-trienoic acid, also termed 12-HHT).[3]

References

  1. ^ Rylander T, Neve EP, Ingelman-Sundberg M, Oscarson M (Feb 2001). "Identification and tissue distribution of the novel human cytochrome P450 2S1 (CYP2S1)". Biochemical and Biophysical Research Communications. 281 (2): 529–35. doi:10.1006/bbrc.2001.4390. PMID 11181079.
  2. ^ a b "Entrez Gene: CYP2S1 cytochrome P450, family 2, subfamily S, polypeptide 1".
  3. ^ a b Frömel T, Kohlstedt K, Popp R, Yin X, Awwad K, Barbosa-Sicard E, Thomas AC, Lieberz R, Mayr M, Fleming I (Jan 2013). "Cytochrome P4502S1: a novel monocyte/macrophage fatty acid epoxygenase in human atherosclerotic plaques". Basic Research in Cardiology. 108 (1): 319. doi:10.1007/s00395-012-0319-8. PMID 23224081.
  4. ^ a b Spector AA, Kim HY (Apr 2015). "Cytochrome P450 epoxygenase pathway of polyunsaturated fatty acid metabolism". Biochimica et Biophysica Acta. 1851 (4): 356–65. doi:10.1016/j.bbalip.2014.07.020. PMID 25093613.

Further reading


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