AKR1C3: Difference between revisions

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{{Infobox gene}}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
'''Aldo-keto reductase family 1 member C3''' ('''AKR1C3'''), also known as '''17β-hydroxysteroid dehydrogenase type 5''' ('''17β-HSD5''', '''HSD17B5''') is a key [[steroidogenic]] [[enzyme]] that in humans is encoded by the ''AKR1C3'' [[gene]].<ref name="pmid7650035">{{cite journal | vauthors = Khanna M, Qin KN, Wang RW, Cheng KC | title = Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases | journal = The Journal of Biological Chemistry | volume = 270 | issue = 34 | pages = 20162–8 | date = Aug 1995 | pmid = 7650035 | pmc =  | doi = 10.1074/jbc.270.34.20162 }}</ref><ref name="pmid9792917">{{cite journal | vauthors = Matsuura K, Shiraishi H, Hara A, Sato K, Deyashiki Y, Ninomiya M, Sakai S | title = Identification of a principal mRNA species for human 3alpha-hydroxysteroid dehydrogenase isoform (AKR1C3) that exhibits high prostaglandin D2 11-ketoreductase activity | journal = Journal of Biochemistry | volume = 124 | issue = 5 | pages = 940–6 | date = Nov 1998 | pmid = 9792917 | pmc =  | doi = 10.1093/oxfordjournals.jbchem.a022211 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: AKR1C3 aldo-keto reductase family 1, member C3 (3-alpha hydroxysteroid dehydrogenase, type II)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8644| accessdate = }}</ref>
{{GNF_Protein_box
| image = PBB_Protein_AKR1C3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ry0.
| PDB = {{PDB2|1ry0}}, {{PDB2|1ry8}}, {{PDB2|1s1p}}, {{PDB2|1s1r}}, {{PDB2|1s2a}}, {{PDB2|1s2c}}, {{PDB2|1xf0}}, {{PDB2|1zq5}}, {{PDB2|2f38}}, {{PDB2|2fgb}}
| Name = Aldo-keto reductase family 1, member C3 (3-alpha hydroxysteroid dehydrogenase, type II)
| HGNCid = 386
| Symbol = AKR1C3
| AltSymbols =; DD3; HA1753; HAKRB; HAKRe; HSD17B5; KIAA0119; hluPGFS
| OMIM = 603966
| ECnumber =
| Homologene = 81636
| MGIid = 2145420
  | GeneAtlas_image1 = PBB_GE_AKR1C3_209160_at_tn.png
| GeneAtlas_image2 = PBB_GE_AKR1C3_211653_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004033 |text = aldo-keto reductase activity}} {{GNF_GO|id=GO:0004303 |text = estradiol 17-beta-dehydrogenase activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0047017 |text = prostaglandin-F synthase activity}} {{GNF_GO|id=GO:0047026 |text = 3-alpha-hydroxysteroid dehydrogenase (A-specific) activity}} {{GNF_GO|id=GO:0047115 |text = trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006693 |text = prostaglandin metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 8644
    | Hs_Ensembl = ENSG00000196139
    | Hs_RefseqProtein = NP_003730
    | Hs_RefseqmRNA = NM_003739
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 10
    | Hs_GenLoc_start = 5125985
    | Hs_GenLoc_end = 5139878
    | Hs_Uniprot = P42330
    | Mm_EntrezGene = 105349
    | Mm_Ensembl = ENSMUSG00000021214
    | Mm_RefseqmRNA = NM_134066
    | Mm_RefseqProtein = NP_598827
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 13
    | Mm_GenLoc_start = 4131870
    | Mm_GenLoc_end = 4149877
    | Mm_Uniprot = Q3U538
  }}
}}
'''Aldo-keto reductase family 1, member C3 (3-alpha hydroxysteroid dehydrogenase, type II)''', also known as '''AKR1C3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AKR1C3 aldo-keto reductase family 1, member C3 (3-alpha hydroxysteroid dehydrogenase, type II)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8644| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
==Function==
{{PBB_Summary
This gene encodes a member of the [[aldo-keto reductase|aldo/keto reductase superfamily]], which consists of more than 40 known enzymes and proteins. These enzymes catalyze the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors. The enzymes display overlapping but distinct substrate specificity. This enzyme catalyzes the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ), and the oxidation of 9alpha,11beta-PGF2 to PGD2. It may play an important role in the pathogenesis of allergic diseases such as asthma, and may also have a role in controlling cell growth and/or differentiation. This gene shares high sequence identity with three other gene members and is clustered with those three genes at chromosome 10p15-p14.<ref name="entrez" />
| section_title =  
 
| summary_text = This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. These enzymes catalyze the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors. The enzymes display overlapping but distinct substrate specificity. This enzyme catalyzes the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ), and the oxidation of 9alpha,11beta-PGF2 to PGD2. It may play an important role in the pathogenesis of allergic diseases such as asthma, and may also have a role in controlling cell growth and/or differentiation. This gene shares high sequence identity with three other gene members and is clustered with those three genes at chromosome 10p15-p14.<ref name="entrez">{{cite web | title = Entrez Gene: AKR1C3 aldo-keto reductase family 1, member C3 (3-alpha hydroxysteroid dehydrogenase, type II)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8644| accessdate = }}</ref>
==Pathology==
}}
AKR1C3 is overexpressed in [[prostate cancer]] (PCa) and is associated with the development of [[castration-resistant prostate cancer]] (CRPC). In addition, AKR1C3 overexpression may serve as a promising [[biomarker]] for prostate cancer [[tumor progression|progression]].<ref>{{cite journal | vauthors = Tian Y, Zhao L, Zhang H, Liu X, Zhao L, Zhao X, Li Y, Li J | title = AKR1C3 overexpression may serve as a promising biomarker for prostate cancer progression | journal = Diagnostic Pathology | volume = 9 | issue = 1 | pages = 42 | year = 2014 | pmid = 24571686 | pmc = 3939640 | doi = 10.1186/1746-1596-9-42 }}</ref>


==References==
==References==
{{reflist|2}}
{{Reflist}}
==Further reading==
{{Clear}}
{{refbegin | 2}}
 
{{PBB_Further_reading
==External links==
| citations =
* {{UCSC gene info|AKR1C3}}
*{{cite journal  | author=Lin SX, Shi R, Qiu W, ''et al.'' |title=Structural basis of the multispecificity demonstrated by 17beta-hydroxysteroid dehydrogenase types 1 and 5. |journal=Mol. Cell. Endocrinol. |volume=248 |issue= 1-2 |pages= 38-46 |year= 2006 |pmid= 16480815 |doi= 10.1016/j.mce.2005.11.035 }}
 
*{{cite journal | author=Khanna M, Qin KN, Cheng KC |title=Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans. |journal=J. Steroid Biochem. Mol. Biol. |volume=53 |issue= 1-6 |pages= 41-6 |year= 1995 |pmid= 7626489 |doi= }}
== Further reading ==
*{{cite journal | author=Khanna M, Qin KN, Wang RW, Cheng KC |title=Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases. |journal=J. Biol. Chem. |volume=270 |issue= 34 |pages= 20162-8 |year= 1995 |pmid= 7650035 |doi= }}
{{refbegin|33em}}
*{{cite journal | author=Nagase T, Miyajima N, Tanaka A, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1. |journal=DNA Res. |volume=2 |issue= 1 |pages= 37-43 |year= 1995 |pmid= 7788527 |doi= }}
* {{cite journal | vauthors = Lin SX, Shi R, Qiu W, Azzi A, Zhu DW, Dabbagh HA, Zhou M | title = Structural basis of the multispecificity demonstrated by 17beta-hydroxysteroid dehydrogenase types 1 and 5 | journal = Molecular and Cellular Endocrinology | volume = 248 | issue = 1-2 | pages = 38–46 | date = Mar 2006 | pmid = 16480815 | doi = 10.1016/j.mce.2005.11.035 }}
*{{cite journal | author=Khanna M, Qin KN, Klisak I, ''et al.'' |title=Localization of multiple human dihydrodiol dehydrogenase (DDH1 and DDH2) and chlordecone reductase (CHDR) genes in chromosome 10 by the polymerase chain reaction and fluorescence in situ hybridization. |journal=Genomics |volume=25 |issue= 2 |pages= 588-90 |year= 1995 |pmid= 7789999 |doi= }}
* {{cite journal | vauthors = Khanna M, Qin KN, Cheng KC | title = Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans | journal = The Journal of Steroid Biochemistry and Molecular Biology | volume = 53 | issue = 1-6 | pages = 41–6 | date = Jun 1995 | pmid = 7626489 | doi = 10.1016/0960-0760(95)00019-V }}
*{{cite journal | author=Qin KN, New MI, Cheng KC |title=Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase. |journal=J. Steroid Biochem. Mol. Biol. |volume=46 |issue= 6 |pages= 673-9 |year= 1994 |pmid= 8274401 |doi= }}
* {{cite journal | vauthors = Nagase T, Miyajima N, Tanaka A, Sazuka T, Seki N, Sato S, Tabata S, Ishikawa K, Kawarabayasi Y, Kotani H | title = Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1 | journal = DNA Research | volume = 2 | issue = 1 | pages = 37–43 | year = 1995 | pmid = 7788527 | doi = 10.1093/dnares/2.1.37 }}
*{{cite journal | author=Bennett MJ, Schlegel BP, Jez JM, ''et al.'' |title=Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+. |journal=Biochemistry |volume=35 |issue= 33 |pages= 10702-11 |year= 1996 |pmid= 8718859 |doi= 10.1021/bi9604688 }}
* {{cite journal | vauthors = Khanna M, Qin KN, Klisak I, Belkin S, Sparkes RS, Cheng KC | title = Localization of multiple human dihydrodiol dehydrogenase (DDH1 and DDH2) and chlordecone reductase (CHDR) genes in chromosome 10 by the polymerase chain reaction and fluorescence in situ hybridization | journal = Genomics | volume = 25 | issue = 2 | pages = 588–90 | date = Jan 1995 | pmid = 7789999 | doi = 10.1016/0888-7543(95)80066-U }}
*{{cite journal | author=Lin HK, Jez JM, Schlegel BP, ''et al.'' |title=Expression and characterization of recombinant type 2 3 alpha-hydroxysteroid dehydrogenase (HSD) from human prostate: demonstration of bifunctional 3 alpha/17 beta-HSD activity and cellular distribution. |journal=Mol. Endocrinol. |volume=11 |issue= 13 |pages= 1971-84 |year= 1998 |pmid= 9415401 |doi= }}
* {{cite journal | vauthors = Qin KN, New MI, Cheng KC | title = Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase | journal = The Journal of Steroid Biochemistry and Molecular Biology | volume = 46 | issue = 6 | pages = 673–9 | date = Dec 1993 | pmid = 8274401 | doi = 10.1016/0960-0760(93)90308-J }}
*{{cite journal  | author=Matsuura K, Shiraishi H, Hara A, ''et al.'' |title=Identification of a principal mRNA species for human 3alpha-hydroxysteroid dehydrogenase isoform (AKR1C3) that exhibits high prostaglandin D2 11-ketoreductase activity. |journal=J. Biochem. |volume=124 |issue= 5 |pages= 940-6 |year= 1999 |pmid= 9792917 |doi= }}
* {{cite journal | vauthors = Bennett MJ, Schlegel BP, Jez JM, Penning TM, Lewis M | title = Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+ | journal = Biochemistry | volume = 35 | issue = 33 | pages = 10702–11 | date = Aug 1996 | pmid = 8718859 | doi = 10.1021/bi9604688 }}
*{{cite journal | author=Mills KI, Gilkes AF, Sweeney M, ''et al.'' |title=Identification of a retinoic acid responsive aldoketoreductase expressed in HL60 leukaemic cells. |journal=FEBS Lett. |volume=440 |issue= 1-2 |pages= 158-62 |year= 1999 |pmid= 9862446 |doi= }}
* {{cite journal | vauthors = Lin HK, Jez JM, Schlegel BP, Peehl DM, Pachter JA, Penning TM | title = Expression and characterization of recombinant type 2 3 alpha-hydroxysteroid dehydrogenase (HSD) from human prostate: demonstration of bifunctional 3 alpha/17 beta-HSD activity and cellular distribution | journal = Molecular Endocrinology | volume = 11 | issue = 13 | pages = 1971–84 | date = Dec 1997 | pmid = 9415401 | doi = 10.1210/me.11.13.1971 }}
*{{cite journal | author=Dufort I, Rheault P, Huang XF, ''et al.'' |title=Characteristics of a highly labile human type 5 17beta-hydroxysteroid dehydrogenase. |journal=Endocrinology |volume=140 |issue= 2 |pages= 568-74 |year= 1999 |pmid= 9927279 |doi= }}
* {{cite journal | vauthors = Mills KI, Gilkes AF, Sweeney M, Choudhry MA, Woodgate LJ, Bunce CM, Brown G, Burnett AK | title = Identification of a retinoic acid responsive aldoketoreductase expressed in HL60 leukaemic cells | journal = FEBS Letters | volume = 440 | issue = 1-2 | pages = 158–62 | date = Nov 1998 | pmid = 9862446 | doi = 10.1016/S0014-5793(98)01435-5 }}
*{{cite journal | author=Rheault P, Dufort I, Soucy P, Luu-The V |title=Assignment of HSD17B5 encoding type 5 17 beta-hydroxysteroid dehydrogenase to human chromosome bands 10p15-->p14 and mouse chromosome 13 region A2 by in situ hybridization: identification of a new syntenic relationship. |journal=Cytogenet. Cell Genet. |volume=84 |issue= 3-4 |pages= 241-2 |year= 1999 |pmid= 10393440 |doi=  }}
* {{cite journal | vauthors = Dufort I, Rheault P, Huang XF, Soucy P, Luu-The V | title = Characteristics of a highly labile human type 5 17beta-hydroxysteroid dehydrogenase | journal = Endocrinology | volume = 140 | issue = 2 | pages = 568–74 | date = Feb 1999 | pmid = 9927279 | doi = 10.1210/en.140.2.568 }}
*{{cite journal | author=Griffin LD, Mellon SH |title=Selective serotonin reuptake inhibitors directly alter activity of neurosteroidogenic enzymes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 23 |pages= 13512-7 |year= 1999 |pmid= 10557352 |doi= }}
* {{cite journal | vauthors = Rheault P, Dufort I, Soucy P, Luu-The V | title = Assignment of HSD17B5 encoding type 5 17 beta-hydroxysteroid dehydrogenase to human chromosome bands 10p15-->p14 and mouse chromosome 13 region A2 by in situ hybridization: identification of a new syntenic relationship | journal = Cytogenetics and Cell Genetics | volume = 84 | issue = 3-4 | pages = 241–2 | year = 1999 | pmid = 10393440 | doi = 10.1159/000015267 }}
*{{cite journal | author=Suzuki-Yamamoto T, Nishizawa M, Fukui M, ''et al.'' |title=cDNA cloning, expression and characterization of human prostaglandin F synthase. |journal=FEBS Lett. |volume=462 |issue= 3 |pages= 335-40 |year= 2000 |pmid= 10622721 |doi=  }}
* {{cite journal | vauthors = Griffin LD, Mellon SH | title = Selective serotonin reuptake inhibitors directly alter activity of neurosteroidogenic enzymes | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 96 | issue = 23 | pages = 13512–7 | date = Nov 1999 | pmid = 10557352 | pmc = 23979 | doi = 10.1073/pnas.96.23.13512 }}
*{{cite journal | author=Nishizawa M, Nakajima T, Yasuda K, ''et al.'' |title=Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes. |journal=Genes Cells |volume=5 |issue= 2 |pages= 111-25 |year= 2000 |pmid= 10672042 |doi=  }}
* {{cite journal | vauthors = Suzuki-Yamamoto T, Nishizawa M, Fukui M, Okuda-Ashitaka E, Nakajima T, Ito S, Watanabe K | title = cDNA cloning, expression and characterization of human prostaglandin F synthase | journal = FEBS Letters | volume = 462 | issue = 3 | pages = 335–40 | date = Dec 1999 | pmid = 10622721 | doi = 10.1016/S0014-5793(99)01551-3 }}
*{{cite journal | author=Penning TM, Burczynski ME, Jez JM, ''et al.'' |title=Human 3alpha-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones. |journal=Biochem. J. |volume=351 |issue= Pt 1 |pages= 67-77 |year= 2001 |pmid= 10998348 |doi=  }}
* {{cite journal | vauthors = Nishizawa M, Nakajima T, Yasuda K, Kanzaki H, Sasaguri Y, Watanabe K, Ito S | title = Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes | journal = Genes to Cells | volume = 5 | issue = 2 | pages = 111–25 | date = Feb 2000 | pmid = 10672042 | doi = 10.1046/j.1365-2443.2000.00310.x }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
* {{cite journal | vauthors = Penning TM, Burczynski ME, Jez JM, Hung CF, Lin HK, Ma H, Moore M, Palackal N, Ratnam K | title = Human 3alpha-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones | journal = The Biochemical Journal | volume = 351 | issue = Pt 1 | pages = 67–77 | date = Oct 2000 | pmid = 10998348 | pmc = 1221336 | doi = 10.1042/0264-6021:3510067 }}
*{{cite journal | author=Penning TM, Burczynski ME, Jez JM, ''et al.'' |title=Structure-function aspects and inhibitor design of type 5 17beta-hydroxysteroid dehydrogenase (AKR1C3). |journal=Mol. Cell. Endocrinol. |volume=171 |issue= 1-2 |pages= 137-49 |year= 2001 |pmid= 11165022 |doi= }}
* {{cite journal | vauthors = Hartley JL, Temple GF, Brasch MA | title = DNA cloning using in vitro site-specific recombination | journal = Genome Research | volume = 10 | issue = 11 | pages = 1788–95 | date = Nov 2000 | pmid = 11076863 | pmc = 310948 | doi = 10.1101/gr.143000 }}
*{{cite journal  | author=Simpson JC, Wellenreuther R, Poustka A, ''et al.'' |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287-92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 }}
* {{cite journal | vauthors = Penning TM, Burczynski ME, Jez JM, Lin HK, Ma H, Moore M, Ratnam K, Palackal N | title = Structure-function aspects and inhibitor design of type 5 17beta-hydroxysteroid dehydrogenase (AKR1C3) | journal = Molecular and Cellular Endocrinology | volume = 171 | issue = 1-2 | pages = 137–49 | date = Jan 2001 | pmid = 11165022 | doi = 10.1016/S0303-7207(00)00426-3 }}
*{{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 | vauthors = Simpson JC, Wellenreuther R, Poustka A, Pepperkok R, Wiemann S | title = Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing | journal = EMBO Reports | volume = 1 | issue = 3 | pages = 287–92 | date = Sep 2000 | pmid = 11256614 | pmc = 1083732 | doi = 10.1093/embo-reports/kvd058 }}
}}
{{refend}}
{{refend}}


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[[Category:EC 1.1.1]]

Latest revision as of 17:56, 29 August 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

Aldo-keto reductase family 1 member C3 (AKR1C3), also known as 17β-hydroxysteroid dehydrogenase type 5 (17β-HSD5, HSD17B5) is a key steroidogenic enzyme that in humans is encoded by the AKR1C3 gene.[1][2][3]

Function

This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. These enzymes catalyze the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors. The enzymes display overlapping but distinct substrate specificity. This enzyme catalyzes the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ), and the oxidation of 9alpha,11beta-PGF2 to PGD2. It may play an important role in the pathogenesis of allergic diseases such as asthma, and may also have a role in controlling cell growth and/or differentiation. This gene shares high sequence identity with three other gene members and is clustered with those three genes at chromosome 10p15-p14.[3]

Pathology

AKR1C3 is overexpressed in prostate cancer (PCa) and is associated with the development of castration-resistant prostate cancer (CRPC). In addition, AKR1C3 overexpression may serve as a promising biomarker for prostate cancer progression.[4]

References

  1. ↑ Khanna M, Qin KN, Wang RW, Cheng KC (Aug 1995). "Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases". The Journal of Biological Chemistry. 270 (34): 20162–8. doi:10.1074/jbc.270.34.20162. PMID 7650035.
  2. ↑ Matsuura K, Shiraishi H, Hara A, Sato K, Deyashiki Y, Ninomiya M, Sakai S (Nov 1998). "Identification of a principal mRNA species for human 3alpha-hydroxysteroid dehydrogenase isoform (AKR1C3) that exhibits high prostaglandin D2 11-ketoreductase activity". Journal of Biochemistry. 124 (5): 940–6. doi:10.1093/oxfordjournals.jbchem.a022211. PMID 9792917.
  3. ↑ 3.0 3.1 "Entrez Gene: AKR1C3 aldo-keto reductase family 1, member C3 (3-alpha hydroxysteroid dehydrogenase, type II)".
  4. ↑ Tian Y, Zhao L, Zhang H, Liu X, Zhao L, Zhao X, Li Y, Li J (2014). "AKR1C3 overexpression may serve as a promising biomarker for prostate cancer progression". Diagnostic Pathology. 9 (1): 42. doi:10.1186/1746-1596-9-42. PMC 3939640. PMID 24571686.

External links

Further reading

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