Biology:AKR1C3
From HandWiki
Aldo-keto reductase family 1 member C3 (AKR1C3), also known as 17β-hydroxysteroid dehydrogenase type 5 (17β-HSD5, HSD17B5) or 3α-hydroxysteroid dehydrogenase type 2 (3α-HSD2)[1][2][3] is a steroidogenic enzyme that in humans is encoded by the AKR1C3 gene.[4][5][6]
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 D2, prostaglandin H2, and phenanthrenequinone, and the oxidation of prostaglandin F2α to prostaglandin D2.[6] It is also capable of metabolizing estrogen and progesterone.[7]
AKR1C3 may play an important role in the development 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.[6]
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.[8]
Isozymes of aldo-keto reductase family 1 member C
See also
References
- ↑ "Human 3-alpha hydroxysteroid dehydrogenase type 3 (3α-HSD3): the V54L mutation restricting the steroid alternative binding and enhancing the 20α-HSD activity". The Journal of Steroid Biochemistry and Molecular Biology 141: 135–143. May 2014. doi:10.1016/j.jsbmb.2014.01.003. PMID 24434280.
- ↑ "Steroid enzyme and receptor expression and regulations in breast tumor samples - A statistical evaluation of public data". The Journal of Steroid Biochemistry and Molecular Biology 196. February 2020. doi:10.1016/j.jsbmb.2019.105494. PMID 31610224.
- ↑ "Alternative androgen pathways". WikiJournal of Medicine 10: 29. 3 April 2023. doi:10.15347/WJM/2023.003. https://upload.wikimedia.org/wikiversity/en/a/a7/Alternative_androgens_pathways.pdf.
This article incorporates text from this source, which is available under the CC BY 4.0 license.
- ↑ "Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases". The Journal of Biological Chemistry 270 (34): 20162–20168. August 1995. doi:10.1074/jbc.270.34.20162. PMID 7650035.
- ↑ "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): 940–946. November 1998. doi:10.1093/oxfordjournals.jbchem.a022211. PMID 9792917.
- ↑ 6.0 6.1 6.2 EntrezGene 8644 AKR1C3 aldo-keto reductase family 1 member C3 [ Homo sapiens (human) ]
- ↑ "The Use of Whole Exome Sequencing in a Cohort of Transgender Individuals to Identify Rare Genetic Variants". Scientific Reports 9 (1). December 2019. doi:10.1038/s41598-019-53500-y. PMID 31882810. Bibcode: 2019NatSR...920099T. "Table 4".
- ↑ "AKR1C3 overexpression may serve as a promising biomarker for prostate cancer progression". Diagnostic Pathology 9 (1). February 2014. doi:10.1186/1746-1596-9-42. PMID 24571686.
External links
- Human AKR1C3 genome location and AKR1C3 gene details page in the UCSC Genome Browser.
Further reading
- "Structural basis of the multispecificity demonstrated by 17beta-hydroxysteroid dehydrogenase types 1 and 5". Molecular and Cellular Endocrinology 248 (1–2): 38–46. March 2006. doi:10.1016/j.mce.2005.11.035. PMID 16480815.
- "Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans". The Journal of Steroid Biochemistry and Molecular Biology 53 (1–6): 41–46. June 1995. doi:10.1016/0960-0760(95)00019-V. PMID 7626489.
- "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". DNA Research 2 (1): 37–43. 1995. doi:10.1093/dnares/2.1.37. PMID 7788527.
- "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". Genomics 25 (2): 588–590. January 1995. doi:10.1016/0888-7543(95)80066-U. PMID 7789999.
- "Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase". The Journal of Steroid Biochemistry and Molecular Biology 46 (6): 673–679. December 1993. doi:10.1016/0960-0760(93)90308-J. PMID 8274401.
- "Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+". Biochemistry 35 (33): 10702–10711. August 1996. doi:10.1021/bi9604688. PMID 8718859.
- "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". Molecular Endocrinology 11 (13): 1971–1984. December 1997. doi:10.1210/mend.11.13.0026. PMID 9415401.
- "Identification of a retinoic acid responsive aldoketoreductase expressed in HL60 leukaemic cells". FEBS Letters 440 (1–2): 158–162. November 1998. doi:10.1016/S0014-5793(98)01435-5. PMID 9862446. Bibcode: 1998FEBSL.440..158M.
- "Characteristics of a highly labile human type 5 17beta-hydroxysteroid dehydrogenase". Endocrinology 140 (2): 568–574. February 1999. doi:10.1210/endo.140.2.6531. PMID 9927279.
- "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". Cytogenetics and Cell Genetics 84 (3–4): 241–242. 1999. doi:10.1159/000015267. PMID 10393440.
- "Selective serotonin reuptake inhibitors directly alter activity of neurosteroidogenic enzymes". Proceedings of the National Academy of Sciences of the United States of America 96 (23): 13512–13517. November 1999. doi:10.1073/pnas.96.23.13512. PMID 10557352. Bibcode: 1999PNAS...9613512G.
- "cDNA cloning, expression and characterization of human prostaglandin F synthase". FEBS Letters 462 (3): 335–340. December 1999. doi:10.1016/S0014-5793(99)01551-3. PMID 10622721.
- "Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes". Genes to Cells 5 (2): 111–125. February 2000. doi:10.1046/j.1365-2443.2000.00310.x. PMID 10672042.
- "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". The Biochemical Journal 351 (Pt 1): 67–77. October 2000. doi:10.1042/bj3510067. PMID 10998348.
- "DNA cloning using in vitro site-specific recombination". Genome Research 10 (11): 1788–1795. November 2000. doi:10.1101/gr.143000. PMID 11076863.
- "Structure-function aspects and inhibitor design of type 5 17beta-hydroxysteroid dehydrogenase (AKR1C3)". Molecular and Cellular Endocrinology 171 (1–2): 137–149. January 2001. doi:10.1016/S0303-7207(00)00426-3. PMID 11165022.
- "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Reports 1 (3): 287–292. September 2000. doi:10.1093/embo-reports/kvd058. PMID 11256614.
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