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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''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 = February 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 = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29785| accessdate = }}</ref>  The gene is located in chromosome 19q13.2 within a cluster including other CYP2 family members such as [[CYP2A6]], [[CYP2A13]], [[CYP2B6]], and [[CYP2F1]].<ref name = "Saarikoski_2005">{{cite journal | vauthors = Saarikoski ST, Rivera SP, Hankinson O, Husgafvel-Pursiainen K | title = CYP2S1: a short review | journal = Toxicology and Applied Pharmacology | volume = 207 | issue = 2 Suppl | pages = 62–9 | date = September 2005 | pmid = 16054184 | doi = 10.1016/j.taap.2004.12.027 }}</ref>
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| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
==Expression==
{{GNF_Protein_box
CYP2S1 is highly expressed in epithelial tissues of the respiratory, gastrointestinal, urinary tracts, and skin and in [[leukocytes]] of the [[monocyte]]/[[macrophage]] and [[lymphocyte]] series; it is also expressed throughout [[Embryogenesis]] and, as discussed below, certain types of cancers.<ref name = "Saarikoski_2005"/>
| image =
 
| image_source =
== Function ==
| PDB =  
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 although its specific function(s) in humans has not been clearly determined.<ref name="entrez"/> In in vitro studies, the human enzyme has been found to metabolize [[all-trans-retinoic acid]] to 4-hydroxy-retinoic acid and 5, 6-epoxy-retinoic acid and therefore may play a role in processing retinoic acid in tissues where it is highly expressed such as the skin.<ref name = "Saarikoski_2005"/> CYP2S1 is significantly overexpressed and, perhaps directly related to this, its gene is significantly hypometylated (see [[gene methylation]] in the skin of Han Chinese patients with [[psoriasis]] suggesting that it plays a role in the development of this disease.<ref name="pmid26743604">{{cite journal | vauthors = Zhou F, Wang W, Shen C, Li H, Zuo X, Zheng X, Yue M, Zhang C, Yu L, Chen M, Zhu C, Yin X, Tang M, Li Y, Chen G, Wang Z, Liu S, Zhou Y, Zhang F, Zhang W, Li C, Yang S, Sun L, Zhang X | title = Epigenome-Wide Association Analysis Identified Nine Skin DNA Methylation Loci for Psoriasis | journal = The Journal of Investigative Dermatology | volume = 136 | issue = 4 | pages = 779–87 | year = 2016 | pmid = 26743604 | doi = 10.1016/j.jid.2015.12.029 }}</ref>
| Name = Cytochrome P450, family 2, subfamily S, polypeptide 1
| HGNCid = 15654
| Symbol = CYP2S1
| AltSymbols =;  
| OMIM =
| ECnumber = 
| Homologene = 75274
| MGIid = 1921384
| Function = {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0050381 |text = unspecific monooxygenase activity}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0016020 |text = membrane}}
  | Process = {{GNF_GO|id=GO:0006118 |text = electron transport}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 29785
    | Hs_Ensembl = ENSG00000167600
    | Hs_RefseqProtein = NP_085125
    | Hs_RefseqmRNA = NM_030622
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 46390955
    | Hs_GenLoc_end = 46405283
    | Hs_Uniprot = Q96SQ9
    | Mm_EntrezGene = 74134
    | Mm_Ensembl = ENSMUSG00000040703
    | Mm_RefseqmRNA = NM_028775
    | Mm_RefseqProtein = NP_083051
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 25511235
    | Mm_GenLoc_end = 25525307
    | Mm_Uniprot = Q8K027
  }}
}}
{{SI}}
{{EH}}


'''Cytochrome P450, family 2, subfamily S, polypeptide 1''', also known as '''CYP2S1''', is a human [[gene]].<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 been suggested to be involved in the growth and/or spread of certain tumors of [[epithelial cell]] origin: its higher expression in breast or colorectal cancer tissues appears associated  respectively with shorter survival times or poor prognoses, and it is more highly expressed in [[metastasis]] compared to primary tumor tissues of ovarian cancer.<ref name="Saarikoski_2005"/><ref>{{cite journal | vauthors = Murray GI, Patimalla S, Stewart KN, Miller ID, Heys SD | title = Profiling the expression of cytochrome P450 in breast cancer | journal = Histopathology | volume = 57 | issue = 2 | pages = 202–11 | date = August 2010 | pmid = 20716162 | doi = 10.1111/j.1365-2559.2010.03606.x }}</ref><ref>{{cite journal | vauthors = Kumarakulasingham M, Rooney PH, Dundas SR, Telfer C, Melvin WT, Curran S, Murray GI | title = Cytochrome p450 profile of colorectal cancer: identification of markers of prognosis | journal = Clinical Cancer Research | volume = 11 | issue = 10 | pages = 3758–65 | date = May 2005 | pmid = 15897573 | doi = 10.1158/1078-0432.CCR-04-1848 }}</ref><ref>{{cite journal | vauthors = Downie D, McFadyen MC, Rooney PH, Cruickshank ME, Parkin DE, Miller ID, Telfer C, Melvin WT, Murray GI | title = Profiling cytochrome P450 expression in ovarian cancer: identification of prognostic markers | journal = Clinical Cancer Research | volume = 11 | issue = 20 | pages = 7369–75 | date = October 2005 | pmid = 16243809 | doi = 10.1158/1078-0432.CCR-05-0466 }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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 = January 2013 | pmid = 23224081 | doi = 10.1007/s00395-012-0319-8 }}</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 the EET, EDP, and EEQ epoxides in regulating blood pressure, tissue blood flow, new blood vessel formation (i.e. [[angiogenesis]], pain perception, and the growth of various cancers; limited studies suggest but have not proven that these epoxides may function similarly in humans (see [[epoxyeicosatrienoic acid]], [[epoxydocosapentaenoic acid]], [[eicosatetraenoic 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 = April 2015 | pmid = 25093613 | doi = 10.1016/j.bbalip.2014.07.020 | pmc=4314516}}</ref> The CYP2S1-dependent production of EETs, which stimulate the growth of various types of cancer cells, including those of he colon (see epoxyeicosatrienoic acid#cancer), could contribute to the unfavorable effects of this CYP in the sited cancers.
{{PBB_Summary
| section_title =  
| 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>
}}


==References==
Vernolic and coronaric acids are potentially toxic, causing [[multiple organ failure]] and [[acute respiratory distress]] when injected into animals and suggested to be involved in causing these syndromes in humans.<ref name = "Spector_2015"/>
{{reflist}}
 
==Further reading==
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" />
{{refbegin | 2}}
 
{{PBB_Further_reading
== References ==
| citations =
{{reflist|33em}}
*{{cite journal  | author=Adams MD, Kerlavage AR, Fleischmann RD, ''et al.'' |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=  }}
*{{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 |year= 2001 |pmid= 11181079 |doi= 10.1006/bbrc.2001.4390 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |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 }}
*{{cite journal  | author=Smith G, Wolf CR, Deeni YY, ''et al.'' |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=  }}
*{{cite journal  | author=Saito S, Iida A, Sekine A, ''et al.'' |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 }}
*{{cite journal  | author=Clark HF, Gurney AL, Abaya E, ''et al.'' |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 }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |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 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |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 }}
*{{cite journal  | author=Rivera SP, Wang F, Saarikoski ST, ''et al.'' |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 }}
*{{cite journal  | author=Marek CJ, Tucker SJ, Koruth M, ''et al.'' |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 }}
*{{cite journal  | author=Hanzawa Y, Sasaki T, Hiratsuka M, ''et al.'' |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=  }}
*{{cite journal  | author=Jang YJ, Cha EY, Kim WY, ''et al.'' |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 }}
}}
{{refend}}


{{SIB}}
==External links==
* {{UCSC gene info|CYP2S1}}


{{WH}}
== Further reading ==
{{WikiDoc Sources}}
{{refbegin|33em}}
* {{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 = September 1995 | pmid = 7566098 | doi = <!-- none available --> | url = http://www.columbia.edu/itc/biology/pollack/w4065/client_edit/readings/nature377_3.pdf | format = PDF }}
* {{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 = April 2003 | pmid = 12711469 | doi = 10.1016/S0140-6736(03)13081-4 }}
* {{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 = 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 = April 2007 | pmid = 17277313 | doi = 10.1074/jbc.M609617200 }}
* {{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 = February 2007 | pmid = 17280660 | doi = 10.1016/j.febslet.2007.01.056 }}
* {{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 = April 2007 | pmid = 17495422 | doi = 10.2133/dmpk.22.136 }}
* {{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 = June 2007 | pmid = 17529885 | doi = 10.1097/FTD.0b013e318058a4e0 }}
{{refend}}
{{Cytochrome P450}}

Latest revision as of 03:16, 27 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Cytochrome P450 2S1 is a protein that in humans is encoded by the CYP2S1 gene.[1][2] The gene is located in chromosome 19q13.2 within a cluster including other CYP2 family members such as CYP2A6, CYP2A13, CYP2B6, and CYP2F1.[3]

Expression

CYP2S1 is highly expressed in epithelial tissues of the respiratory, gastrointestinal, urinary tracts, and skin and in leukocytes of the monocyte/macrophage and lymphocyte series; it is also expressed throughout Embryogenesis and, as discussed below, certain types of cancers.[3]

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 although its specific function(s) in humans has not been clearly determined.[2] In in vitro studies, the human enzyme has been found to metabolize all-trans-retinoic acid to 4-hydroxy-retinoic acid and 5, 6-epoxy-retinoic acid and therefore may play a role in processing retinoic acid in tissues where it is highly expressed such as the skin.[3] CYP2S1 is significantly overexpressed and, perhaps directly related to this, its gene is significantly hypometylated (see gene methylation in the skin of Han Chinese patients with psoriasis suggesting that it plays a role in the development of this disease.[4]

CYP2S1 has been suggested to be involved in the growth and/or spread of certain tumors of epithelial cell origin: its higher expression in breast or colorectal cancer tissues appears associated respectively with shorter survival times or poor prognoses, and it is more highly expressed in metastasis compared to primary tumor tissues of ovarian cancer.[3][5][6][7]

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).[8] 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 the EET, EDP, and EEQ epoxides in regulating blood pressure, tissue blood flow, new blood vessel formation (i.e. angiogenesis, pain perception, and the growth of various cancers; limited studies suggest but have not proven that these epoxides may function similarly in humans (see epoxyeicosatrienoic acid, epoxydocosapentaenoic acid, eicosatetraenoic acid, and epoxygenase pages).[9] The CYP2S1-dependent production of EETs, which stimulate the growth of various types of cancer cells, including those of he colon (see epoxyeicosatrienoic acid#cancer), could contribute to the unfavorable effects of this CYP in the sited cancers.

Vernolic and coronaric acids are potentially toxic, causing multiple organ failure and acute respiratory distress when injected into animals and suggested to be involved in causing these syndromes in humans.[9]

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).[8]

References

  1. ↑ Rylander T, Neve EP, Ingelman-Sundberg M, Oscarson M (February 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. ↑ 2.0 2.1 "Entrez Gene: CYP2S1 cytochrome P450, family 2, subfamily S, polypeptide 1".
  3. ↑ 3.0 3.1 3.2 3.3 Saarikoski ST, Rivera SP, Hankinson O, Husgafvel-Pursiainen K (September 2005). "CYP2S1: a short review". Toxicology and Applied Pharmacology. 207 (2 Suppl): 62–9. doi:10.1016/j.taap.2004.12.027. PMID 16054184.
  4. ↑ Zhou F, Wang W, Shen C, Li H, Zuo X, Zheng X, Yue M, Zhang C, Yu L, Chen M, Zhu C, Yin X, Tang M, Li Y, Chen G, Wang Z, Liu S, Zhou Y, Zhang F, Zhang W, Li C, Yang S, Sun L, Zhang X (2016). "Epigenome-Wide Association Analysis Identified Nine Skin DNA Methylation Loci for Psoriasis". The Journal of Investigative Dermatology. 136 (4): 779–87. doi:10.1016/j.jid.2015.12.029. PMID 26743604.
  5. ↑ Murray GI, Patimalla S, Stewart KN, Miller ID, Heys SD (August 2010). "Profiling the expression of cytochrome P450 in breast cancer". Histopathology. 57 (2): 202–11. doi:10.1111/j.1365-2559.2010.03606.x. PMID 20716162.
  6. ↑ Kumarakulasingham M, Rooney PH, Dundas SR, Telfer C, Melvin WT, Curran S, Murray GI (May 2005). "Cytochrome p450 profile of colorectal cancer: identification of markers of prognosis". Clinical Cancer Research. 11 (10): 3758–65. doi:10.1158/1078-0432.CCR-04-1848. PMID 15897573.
  7. ↑ Downie D, McFadyen MC, Rooney PH, Cruickshank ME, Parkin DE, Miller ID, Telfer C, Melvin WT, Murray GI (October 2005). "Profiling cytochrome P450 expression in ovarian cancer: identification of prognostic markers". Clinical Cancer Research. 11 (20): 7369–75. doi:10.1158/1078-0432.CCR-05-0466. PMID 16243809.
  8. ↑ 8.0 8.1 Frömel T, Kohlstedt K, Popp R, Yin X, Awwad K, Barbosa-Sicard E, Thomas AC, Lieberz R, Mayr M, Fleming I (January 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.
  9. ↑ 9.0 9.1 Spector AA, Kim HY (April 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. PMC 4314516. PMID 25093613.

External links

Further reading

  • Adams MD, Kerlavage AR, Fleischmann RD, Fuldner RA, Bult CJ, Lee NH, Kirkness EF, Weinstock KG, Gocayne JD, White O (September 1995). "Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence" (PDF). Nature. 377 (6547 Suppl): 3–174. PMID 7566098.
  • Smith G, Wolf CR, Deeni YY, Dawe RS, Evans AT, Comrie MM, Ferguson J, Ibbotson SH (April 2003). "Cutaneous expression of cytochrome P450 CYP2S1: individuality in regulation by therapeutic agents for psoriasis and other skin diseases". Lancet. 361 (9366): 1336–43. doi:10.1016/S0140-6736(03)13081-4. PMID 12711469.
  • Saito S, Iida A, Sekine A, Kawauchi S, Higuchi S, Ogawa C, Nakamura Y (2003). "Catalog of 680 variations among eight cytochrome p450 ( CYP) genes, nine esterase genes, and two other genes in the Japanese population". Journal of Human Genetics. 48 (5): 249–70. doi:10.1007/s10038-003-0021-7. PMID 12721789.
  • Rivera SP, Wang F, Saarikoski ST, Taylor RT, Chapman B, Zhang R, Hankinson O (April 2007). "A novel promoter element containing multiple overlapping xenobiotic and hypoxia response elements mediates induction of cytochrome P4502S1 by both dioxin and hypoxia". The Journal of Biological Chemistry. 282 (15): 10881–93. doi:10.1074/jbc.M609617200. PMID 17277313.
  • Marek CJ, Tucker SJ, Koruth M, Wallace K, Wright MC (February 2007). "Expression of CYP2S1 in human hepatic stellate cells". FEBS Letters. 581 (4): 781–6. doi:10.1016/j.febslet.2007.01.056. PMID 17280660.
  • Hanzawa Y, Sasaki T, Hiratsuka M, Ishikawa M, Mizugaki M (April 2007). "Three novel single nucleotide polymorphisms (SNPs) of CYP2S1 gene in Japanese individuals". Drug Metabolism and Pharmacokinetics. 22 (2): 136–40. doi:10.2133/dmpk.22.136. PMID 17495422.
  • Jang YJ, Cha EY, Kim WY, Park SW, Shon JH, Lee SS, Shin JG (June 2007). "CYP2S1 gene polymorphisms in a Korean population". Therapeutic Drug Monitoring. 29 (3): 292–8. doi:10.1097/FTD.0b013e318058a4e0. PMID 17529885.
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