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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. -->
'''17β-Hydroxysteroid dehydrogenase 2''' ('''17β-HSD2''') is an [[enzyme]] of the [[17β-hydroxysteroid dehydrogenase]] (17β-HSD) family that in humans is encoded by the ''HSD17B2'' [[gene]].<ref name="pmid7759109">{{cite journal | vauthors = Durocher F, Morissette J, Labrie Y, Labrie F, Simard J | title = Mapping of the HSD17B2 gene encoding type II 17 beta-hydroxysteroid dehydrogenase close to D16S422 on chromosome 16q24.1-q24.2 | journal = Genomics | volume = 25 | issue = 3 | pages = 724–6 | date = Feb 1995 | pmid = 7759109 | pmc =  | doi = 10.1016/0888-7543(95)80017-G }}</ref><ref name="pmid19027726">{{cite journal | vauthors = Persson B, Kallberg Y, Bray JE, Bruford E, Dellaporta SL, Favia AD, Duarte RG, Jörnvall H, Kavanagh KL, Kedishvili N, Kisiela M, Maser E, Mindnich R, Orchard S, Penning TM, Thornton JM, Adamski J, Oppermann U | title = The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative | journal = Chemico-Biological Interactions | volume = 178 | issue = 1-3 | pages = 94–8 | date = Mar 2009 | pmid = 19027726 | pmc = 2896744 | doi = 10.1016/j.cbi.2008.10.040 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: HSD17B2 hydroxysteroid (17-beta) dehydrogenase 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3294| accessdate = }}</ref>
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Hydroxysteroid (17-beta) dehydrogenase 2
| HGNCid = 5211
| Symbol = HSD17B2
| AltSymbols =; EDH17B2; HSD17
| OMIM = 109685
| ECnumber = 
| Homologene = 31076
| MGIid = 1096386
| GeneAtlas_image1 = PBB_GE_HSD17B2_204818_at_tn.png
| Function = {{GNF_GO|id=GO:0004303 |text = estradiol 17-beta-dehydrogenase activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}}
| Component = {{GNF_GO|id=GO:0005789 |text = endoplasmic reticulum membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
  | Process = {{GNF_GO|id=GO:0006703 |text = estrogen biosynthetic process}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3294
    | Hs_Ensembl = ENSG00000086696
    | Hs_RefseqProtein = NP_002144
    | Hs_RefseqmRNA = NM_002153
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 16
    | Hs_GenLoc_start = 80626364
    | Hs_GenLoc_end = 80689638
    | Hs_Uniprot = P37059
    | Mm_EntrezGene = 15486
    | Mm_Ensembl = ENSMUSG00000031844
    | Mm_RefseqmRNA = NM_008290
    | Mm_RefseqProtein = NP_032316
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 120587923
    | Mm_GenLoc_end = 120645004
    | Mm_Uniprot = Q91X35
  }}
}}
'''Hydroxysteroid (17-beta) dehydrogenase 2''', also known as '''HSD17B2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HSD17B2 hydroxysteroid (17-beta) dehydrogenase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3294| accessdate = }}</ref>


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==Function==
{{PBB_Summary
17β-HSD2 is involved in inactivation of [[androgen]]s and [[estrogen]]s,<ref name="pmid16413960">{{cite journal | vauthors = Moeller G, Adamski J | title = Multifunctionality of human 17beta-hydroxysteroid dehydrogenases | journal = Mol. Cell. Endocrinol. | volume = 248 | issue = 1-2 | pages = 47–55 | year = 2006 | pmid = 16413960 | doi = 10.1016/j.mce.2005.11.031 | quote = 17β-HSD types 1–3, the key enzymes in homeostasis of steroid hormones (Andersson, 1995, Blomquist, 1995) seem to have their role solely in steroid metabolism catalysing reactions on steroid substrates only. [...] 17β-HSD2, an enzyme with broad tissue distribution (Casey et al., 1994), plays its major role in the inactivation of potent steroid hormones oxidising estradiol and testosterone to estrone and androstenedione, respectively (Wu et al., 1993). Beside this, 17β-oxidation of intermediates of steroid metabolism, e.g. 5α-androstane-3α,17β-diol, dihydrotestosterone and Δ5-androstene-3β,17β-diol is described (for review see Mindnich et al. (2004b). Additionally, human 17β-HSD type 2 has high 20α-HSD activity with progestins (Puranen et al., 1999).}}</ref> being accurately describable as "[[antiandrogen]]ic" and "[[antiestrogen]]ic",<ref name="pmid27994658">{{cite journal | vauthors = Wang CT, Li CF, Wu WJ, Huang CN, Li CC, Li WM, Chan TC, Liang PI, Hsing CH, Liao KM | title = High Expression of 17β-hydroxysteroid Dehydrogenase Type 2 is Associated with a Better Prognosis in Urothelial Carcinoma of the Urinary Tract | journal = Journal of Cancer | volume = 7 | issue = 15 | pages = 2221–2230 | year = 2016 | pmid = 27994658 | pmc = 5166531 | doi = 10.7150/jca.16777 | quote = "HSD17B2 has both anti-estrogenic and anti-androgenic functions." }}</ref> and is the key 17β-HSD isozyme in androgen and estrogen inactivation.<ref name="pmid16413960" />{{Additional citation needed|date=July 2017}} Specific reactions catalyzed by 17β-HSD2 include [[estradiol]] to [[estrone]], [[testosterone]] to [[4-androstenedione|androstenedione]], and [[5-androstenediol|androstenediol]] to {{abbrlink|DHEA|dehydroepiandrosterone}}.<ref name="pmid16413960" /><ref name="pmid15130507">{{cite journal | vauthors = Mindnich R, Möller G, Adamski J | title = The role of 17 beta-hydroxysteroid dehydrogenases | journal = Mol. Cell. Endocrinol. | volume = 218 | issue = 1-2 | pages = 7–20 | year = 2004 | pmid = 15130507 | doi = 10.1016/j.mce.2003.12.006 | url = }}</ref> In addition to 17β-HSD activity, this enzyme also shows high [[20α-hydroxysteroid dehydrogenase]] activity and can activate the weak [[progestogen]] [[20α-hydroxyprogesterone]] into the potent progestogen [[progesterone]].<ref name="pmid16413960" /><ref name="pmid15130507" />
| section_title =  
 
| summary_text =  
==Expression==
}}
17β-HSD2 is widely expressed throughout the body including in the [[placenta]], [[liver]], [[intestine]]s, [[endometrium]], [[kidney]], [[pancreas]], [[breast]], [[prostate]], [[bone]], and many other [[tissue (biology)|tissue]]s.<ref name="pmid28430630">{{cite journal | vauthors = Hilborn E, Stål O, Jansson A | title = Estrogen and androgen-converting enzymes 17β-hydroxysteroid dehydrogenase and their involvement in cancer: with a special focus on 17β-hydroxysteroid dehydrogenase type 1, 2, and breast cancer | journal = Oncotarget | volume = 8 | issue = 18 | pages = 30552–30562 | date = May 2017 | pmid = 28430630 | pmc = 5444764 | doi = 10.18632/oncotarget.15547 }}</ref><ref name="Elsevier2016">{{cite book | title = Hormones, Brain and Behavior| chapter-url = https://books.google.com/books?id=NT8oCwAAQBAJ&pg=RA3-PA69 | date = 9 November 2016 | publisher = Elsevier Science | isbn = 978-0-12-803608-2 |pages = 69 | volume = 4: Clinical Important Effects of Hormones on Brain and Behavior | editor-first1 = Stafford | editor-last1 = Lightman | chapter = 4.02: Disorders of Sexual Development in Males: Molecular Genetics, Epigenetics, Gender Identity, and Cognition | first1 = Yuan-Shan | last1 = Zhu | first2 = Julianne L. | last2 = Imperato-McGinley | name-list-format = vanc }}</ref>
 
==Clinical significance==
[[Genetic polymorphism|Polymorphism]]s in HSD17B2 have been associated with [[breast cancer]] and [[prostate cancer]].<ref name="pmid19027824">{{cite journal | vauthors = Moeller G, Adamski J | title = Integrated view on 17beta-hydroxysteroid dehydrogenases | journal = Mol. Cell. Endocrinol. | volume = 301 | issue = 1-2 | pages = 7–19 | year = 2009 | pmid = 19027824 | doi = 10.1016/j.mce.2008.10.040 | url = }}</ref> 17β-HSD2 activity has also been associated with [[endometriosis]] and [[osteoporosis]],<ref name="pmid20108182">{{cite journal | vauthors = Bulun SE, Cheng YH, Pavone ME, Yin P, Imir G, Utsunomiya H, Thung S, Xue Q, Marsh EE, Tokunaga H, Ishikawa H, Kurita T, Su EJ | title = 17Beta-hydroxysteroid dehydrogenase-2 deficiency and progesterone resistance in endometriosis | journal = Semin. Reprod. Med. | volume = 28 | issue = 1 | pages = 44–50 | year = 2010 | pmid = 20108182 | pmc = 4511594 | doi = 10.1055/s-0029-1242992 | url = }}</ref> and [[enzyme inhibitor|inhibitor]]s of the enzyme are of potential interest in the treatment of the latter condition.<ref name="pmid21193039">{{cite journal | vauthors = Marchais-Oberwinkler S, Henn C, Möller G, Klein T, Negri M, Oster A, Spadaro A, Werth R, Wetzel M, Xu K, Frotscher M, Hartmann RW, Adamski J | title = 17β-Hydroxysteroid dehydrogenases (17β-HSDs) as therapeutic targets: protein structures, functions, and recent progress in inhibitor development | journal = J. Steroid Biochem. Mol. Biol. | volume = 125 | issue = 1-2 | pages = 66–82 | year = 2011 | pmid = 21193039 | doi = 10.1016/j.jsbmb.2010.12.013 | url = }}</ref><ref name="pmid26230882">{{cite journal | vauthors = Soubhye J, Alard IC, van Antwerpen P, Dufrasne F | title = Type 2 17-β hydroxysteroid dehydrogenase as a novel target for the treatment of osteoporosis | journal = Future Med Chem | volume = 7 | issue = 11 | pages = 1431–56 | year = 2015 | pmid = 26230882 | doi = 10.4155/fmc.15.74 | url = }}</ref> [[Inactivating mutation]]s resulting in a syndrome of [[congenital]] [[deficiency (medicine)|deficiency]] of 17β-HSD2 have not been reported to date.<ref name="Jameson1998">{{cite book|author=J. Larry Jameson|title=Principles of Molecular Medicine|url=https://books.google.com/books?id=UhjyBwAAQBAJ&pg=PA549|date=13 July 1998|publisher=Springer Science & Business Media|isbn=978-1-59259-726-0|pages=549–}}</ref>


==References==
==References==
{{reflist|2}}
{{Reflist|2}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Labrie Y, Durocher F, Lachance Y, Turgeon C, Simard J, Labrie C, Labrie F | title = The human type II 17 beta-hydroxysteroid dehydrogenase gene encodes two alternatively spliced mRNA species | journal = DNA and Cell Biology | volume = 14 | issue = 10 | pages = 849–61 | date = Oct 1995 | pmid = 7546291 | doi = 10.1089/dna.1995.14.849 }}
| citations =
* {{cite journal | vauthors = Andersson S, Geissler WM, Patel S, Wu L | title = The molecular biology of androgenic 17 beta-hydroxysteroid dehydrogenases | journal = The Journal of Steroid Biochemistry and Molecular Biology | volume = 53 | issue = 1-6 | pages = 37–9 | date = Jun 1995 | pmid = 7626483 | doi = 10.1016/0960-0760(95)00039-3 }}
*{{cite journal | author=Labrie Y, Durocher F, Lachance Y, ''et al.'' |title=The human type II 17 beta-hydroxysteroid dehydrogenase gene encodes two alternatively spliced mRNA species. |journal=DNA Cell Biol. |volume=14 |issue= 10 |pages= 849-61 |year= 1995 |pmid= 7546291 |doi= }}
* {{cite journal | vauthors = Carsol JL, Martin PM, de Launoit Y | title = Characterization of 17 beta-hydroxysteroid dehydrogenase activity and mRNA abundance in human meningioma tumors | journal = Neuroendocrinology | volume = 60 | issue = 4 | pages = 445–51 | date = Oct 1994 | pmid = 7824086 | doi = 10.1159/000126779 }}
*{{cite journal | author=Andersson S, Geissler WM, Patel S, Wu L |title=The molecular biology of androgenic 17 beta-hydroxysteroid dehydrogenases. |journal=J. Steroid Biochem. Mol. Biol. |volume=53 |issue= 1-6 |pages= 37-9 |year= 1995 |pmid= 7626483 |doi= }}
* {{cite journal | vauthors = Wu L, Einstein M, Geissler WM, Chan HK, Elliston KO, Andersson S | title = Expression cloning and characterization of human 17 beta-hydroxysteroid dehydrogenase type 2, a microsomal enzyme possessing 20 alpha-hydroxysteroid dehydrogenase activity | journal = The Journal of Biological Chemistry | volume = 268 | issue = 17 | pages = 12964–9 | date = Jun 1993 | pmid = 8099587 | doi =  }}
*{{cite journal | author=Durocher F, Morissette J, Labrie Y, ''et al.'' |title=Mapping of the HSD17B2 gene encoding type II 17 beta-hydroxysteroid dehydrogenase close to D16S422 on chromosome 16q24.1-q24.2. |journal=Genomics |volume=25 |issue= 3 |pages= 724-6 |year= 1995 |pmid= 7759109 |doi= }}
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1-2 | pages = 171–4 | date = Jan 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
*{{cite journal | author=Carsol JL, Martin PM, de Launoit Y |title=Characterization of 17 beta-hydroxysteroid dehydrogenase activity and mRNA abundance in human meningioma tumors. |journal=Neuroendocrinology |volume=60 |issue= 4 |pages= 445-51 |year= 1995 |pmid= 7824086 |doi=  }}
* {{cite journal | vauthors = Zhang Y, Word RA, Fesmire S, Carr BR, Rainey WE | title = Human ovarian expression of 17 beta-hydroxysteroid dehydrogenase types 1, 2, and 3 | journal = The Journal of Clinical Endocrinology and Metabolism | volume = 81 | issue = 10 | pages = 3594–8 | date = Oct 1996 | pmid = 8855807 | doi = 10.1210/jc.81.10.3594 }}
*{{cite journal | author=Wu L, Einstein M, Geissler WM, ''et al.'' |title=Expression cloning and characterization of human 17 beta-hydroxysteroid dehydrogenase type 2, a microsomal enzyme possessing 20 alpha-hydroxysteroid dehydrogenase activity. |journal=J. Biol. Chem. |volume=268 |issue= 17 |pages= 12964-9 |year= 1993 |pmid= 8099587 |doi= }}
* {{cite journal | vauthors = Moghrabi N, Head JR, Andersson S | title = Cell type-specific expression of 17 beta-hydroxysteroid dehydrogenase type 2 in human placenta and fetal liver | journal = The Journal of Clinical Endocrinology and Metabolism | volume = 82 | issue = 11 | pages = 3872–8 | date = Nov 1997 | pmid = 9360554 | doi = 10.1210/jc.82.11.3872 }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1-2 | pages = 149–56 | date = Oct 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
*{{cite journal | author=Zhang Y, Word RA, Fesmire S, ''et al.'' |title=Human ovarian expression of 17 beta-hydroxysteroid dehydrogenase types 1, 2, and 3. |journal=J. Clin. Endocrinol. Metab. |volume=81 |issue= 10 |pages= 3594-8 |year= 1996 |pmid= 8855807 |doi= }}
* {{cite journal | vauthors = Corbould AM, Judd SJ, Rodgers RJ | title = Expression of types 1, 2, and 3 17 beta-hydroxysteroid dehydrogenase in subcutaneous abdominal and intra-abdominal adipose tissue of women | journal = The Journal of Clinical Endocrinology and Metabolism | volume = 83 | issue = 1 | pages = 187–94 | date = Jan 1998 | pmid = 9435439 | doi = 10.1210/jc.83.1.187 }}
*{{cite journal | author=Moghrabi N, Head JR, Andersson S |title=Cell type-specific expression of 17 beta-hydroxysteroid dehydrogenase type 2 in human placenta and fetal liver. |journal=J. Clin. Endocrinol. Metab. |volume=82 |issue= 11 |pages= 3872-8 |year= 1997 |pmid= 9360554 |doi= }}
* {{cite journal | vauthors = Dong Y, Qiu QQ, Debear J, Lathrop WF, Bertolini DR, Tamburini PP | title = 17Beta-hydroxysteroid dehydrogenases in human bone cells | journal = Journal of Bone and Mineral Research | volume = 13 | issue = 10 | pages = 1539–46 | date = Oct 1998 | pmid = 9783542 | doi = 10.1359/jbmr.1998.13.10.1539 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
* {{cite journal | vauthors = Kitawaki J, Koshiba H, Ishihara H, Kusuki I, Tsukamoto K, Honjo H | title = Progesterone induction of 17beta-hydroxysteroid dehydrogenase type 2 during the secretory phase occurs in the endometrium of estrogen-dependent benign diseases but not in normal endometrium | journal = The Journal of Clinical Endocrinology and Metabolism | volume = 85 | issue = 9 | pages = 3292–6 | date = Sep 2000 | pmid = 10999824 | doi = 10.1210/jc.85.9.3292 }}
*{{cite journal | author=Corbould AM, Judd SJ, Rodgers RJ |title=Expression of types 1, 2, and 3 17 beta-hydroxysteroid dehydrogenase in subcutaneous abdominal and intra-abdominal adipose tissue of women. |journal=J. Clin. Endocrinol. Metab. |volume=83 |issue= 1 |pages= 187-94 |year= 1998 |pmid= 9435439 |doi= }}
* {{cite journal | vauthors = Sano T, Hirasawa G, Takeyama J, Darnel AD, Suzuki T, Moriya T, Kato K, Sekine H, Ohara S, Shimosegawa T, Nakamura J, Yoshihama M, Harada N, Sasano H | title = 17 beta-Hydroxysteroid dehydrogenase type 2 expression and enzyme activity in the human gastrointestinal tract | journal = Clinical Science | volume = 101 | issue = 5 | pages = 485–91 | date = Nov 2001 | pmid = 11672453 | doi = 10.1042/CS20010052 }}
*{{cite journal | author=Dong Y, Qiu QQ, Debear J, ''et al.'' |title=17Beta-hydroxysteroid dehydrogenases in human bone cells. |journal=J. Bone Miner. Res. |volume=13 |issue= 10 |pages= 1539-46 |year= 1999 |pmid= 9783542 |doi= }}
* {{cite journal | vauthors = Lu ML, Huang YW, Lin SX | title = Purification, reconstitution, and steady-state kinetics of the trans-membrane 17 beta-hydroxysteroid dehydrogenase 2 | journal = The Journal of Biological Chemistry | volume = 277 | issue = 25 | pages = 22123–30 | date = Jun 2002 | pmid = 11940569 | doi = 10.1074/jbc.M111726200 }}
*{{cite journal | author=Kitawaki J, Koshiba H, Ishihara H, ''et al.'' |title=Progesterone induction of 17beta-hydroxysteroid dehydrogenase type 2 during the secretory phase occurs in the endometrium of estrogen-dependent benign diseases but not in normal endometrium. |journal=J. Clin. Endocrinol. Metab. |volume=85 |issue= 9 |pages= 3292-6 |year= 2000 |pmid= 10999824 |doi= }}
* {{cite journal | vauthors = Provost PR, Blomquist CH, Drolet R, Flamand N, Tremblay Y | title = Androgen inactivation in human lung fibroblasts: variations in levels of 17 beta-hydroxysteroid dehydrogenase type 2 and 5 alpha-reductase activity compatible with androgen inactivation | journal = The Journal of Clinical Endocrinology and Metabolism | volume = 87 | issue = 8 | pages = 3883–92 | date = Aug 2002 | pmid = 12161528 | doi = 10.1210/jc.87.8.3883 }}
*{{cite journal | author=Sano T, Hirasawa G, Takeyama J, ''et al.'' |title=17 beta-Hydroxysteroid dehydrogenase type 2 expression and enzyme activity in the human gastrointestinal tract. |journal=Clin. Sci. |volume=101 |issue= 5 |pages= 485-91 |year= 2001 |pmid= 11672453 |doi= }}
* {{cite journal | vauthors = Oliveira IO, Lhullier C, Brum IS, Spritzer PM | title = Gene expression of type 2 17 beta hydroxysteroid dehydrogenase in scalp hairs of hirsute women | journal = Steroids | volume = 68 | issue = 7-8 | pages = 641–9 | date = Sep 2003 | pmid = 12957669 | doi = 10.1016/S0039-128X(03)00093-X }}
*{{cite journal | author=Lu ML, Huang YW, Lin SX |title=Purification, reconstitution, and steady-state kinetics of the trans-membrane 17 beta-hydroxysteroid dehydrogenase 2. |journal=J. Biol. Chem. |volume=277 |issue= 25 |pages= 22123-30 |year= 2002 |pmid= 11940569 |doi= 10.1074/jbc.M111726200 }}
* {{cite journal | vauthors = Oduwole OO, Mäkinen JM, Isomaa VV, Karttunen TJ, Vihko PT | title = Sex steroid metabolism in human gastric mucosa: 17 beta-hydroxysteroid dehydrogenase type 2 in normal, inflamed and neoplastic gastric tissues | journal = Anticancer Research | volume = 23 | issue = 5A | pages = 3889–97 | year = 2004 | pmid = 14666693 | doi = }}
*{{cite journal | author=Provost PR, Blomquist CH, Drolet R, ''et al.'' |title=Androgen inactivation in human lung fibroblasts: variations in levels of 17 beta-hydroxysteroid dehydrogenase type 2 and 5 alpha-reductase activity compatible with androgen inactivation. |journal=J. Clin. Endocrinol. Metab. |volume=87 |issue= 8 |pages= 3883-92 |year= 2002 |pmid= 12161528 |doi= }}
* {{cite journal | vauthors = Matsuzaki S, Canis M, Pouly JL, Déchelotte PJ, Mage G | title = Analysis of aromatase and 17beta-hydroxysteroid dehydrogenase type 2 messenger ribonucleic acid expression in deep endometriosis and eutopic endometrium using laser capture microdissection | journal = Fertility and Sterility | volume = 85 | issue = 2 | pages = 308–13 | date = Feb 2006 | pmid = 16595205 | doi = 10.1016/j.fertnstert.2005.08.017 }}
*{{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=Oliveira IO, Lhullier C, Brum IS, Spritzer PM |title=Gene expression of type 2 17 beta hydroxysteroid dehydrogenase in scalp hairs of hirsute women. |journal=Steroids |volume=68 |issue= 7-8 |pages= 641-9 |year= 2004 |pmid= 12957669 |doi=  }}
*{{cite journal  | author=Oduwole OO, Mäkinen JM, Isomaa VV, ''et al.'' |title=Sex steroid metabolism in human gastric mucosa: 17 beta-hydroxysteroid dehydrogenase type 2 in normal, inflamed and neoplastic gastric tissues. |journal=Anticancer Res. |volume=23 |issue= 5A |pages= 3889-97 |year= 2004 |pmid= 14666693 |doi=  }}
*{{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=Matsuzaki S, Canis M, Pouly JL, ''et al.'' |title=Analysis of aromatase and 17beta-hydroxysteroid dehydrogenase type 2 messenger ribonucleic acid expression in deep endometriosis and eutopic endometrium using laser capture microdissection. |journal=Fertil. Steril. |volume=85 |issue= 2 |pages= 308-13 |year= 2006 |pmid= 16595205 |doi= 10.1016/j.fertnstert.2005.08.017 }}
}}
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Latest revision as of 02:02, 27 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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17β-Hydroxysteroid dehydrogenase 2 (17β-HSD2) is an enzyme of the 17β-hydroxysteroid dehydrogenase (17β-HSD) family that in humans is encoded by the HSD17B2 gene.[1][2][3]

Function

17β-HSD2 is involved in inactivation of androgens and estrogens,[4] being accurately describable as "antiandrogenic" and "antiestrogenic",[5] and is the key 17β-HSD isozyme in androgen and estrogen inactivation.[4][additional citation(s) needed] Specific reactions catalyzed by 17β-HSD2 include estradiol to estrone, testosterone to androstenedione, and androstenediol to DHEA.[4][6] In addition to 17β-HSD activity, this enzyme also shows high 20α-hydroxysteroid dehydrogenase activity and can activate the weak progestogen 20α-hydroxyprogesterone into the potent progestogen progesterone.[4][6]

Expression

17β-HSD2 is widely expressed throughout the body including in the placenta, liver, intestines, endometrium, kidney, pancreas, breast, prostate, bone, and many other tissues.[7][8]

Clinical significance

Polymorphisms in HSD17B2 have been associated with breast cancer and prostate cancer.[9] 17β-HSD2 activity has also been associated with endometriosis and osteoporosis,[10] and inhibitors of the enzyme are of potential interest in the treatment of the latter condition.[11][12] Inactivating mutations resulting in a syndrome of congenital deficiency of 17β-HSD2 have not been reported to date.[13]

References

  1. ↑ Durocher F, Morissette J, Labrie Y, Labrie F, Simard J (Feb 1995). "Mapping of the HSD17B2 gene encoding type II 17 beta-hydroxysteroid dehydrogenase close to D16S422 on chromosome 16q24.1-q24.2". Genomics. 25 (3): 724–6. doi:10.1016/0888-7543(95)80017-G. PMID 7759109.
  2. ↑ Persson B, Kallberg Y, Bray JE, Bruford E, Dellaporta SL, Favia AD, Duarte RG, Jörnvall H, Kavanagh KL, Kedishvili N, Kisiela M, Maser E, Mindnich R, Orchard S, Penning TM, Thornton JM, Adamski J, Oppermann U (Mar 2009). "The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative". Chemico-Biological Interactions. 178 (1–3): 94–8. doi:10.1016/j.cbi.2008.10.040. PMC 2896744. PMID 19027726.
  3. ↑ "Entrez Gene: HSD17B2 hydroxysteroid (17-beta) dehydrogenase 2".
  4. ↑ 4.0 4.1 4.2 4.3 Moeller G, Adamski J (2006). "Multifunctionality of human 17beta-hydroxysteroid dehydrogenases". Mol. Cell. Endocrinol. 248 (1–2): 47–55. doi:10.1016/j.mce.2005.11.031. PMID 16413960. 17β-HSD types 1–3, the key enzymes in homeostasis of steroid hormones (Andersson, 1995, Blomquist, 1995) seem to have their role solely in steroid metabolism catalysing reactions on steroid substrates only. [...] 17β-HSD2, an enzyme with broad tissue distribution (Casey et al., 1994), plays its major role in the inactivation of potent steroid hormones oxidising estradiol and testosterone to estrone and androstenedione, respectively (Wu et al., 1993). Beside this, 17β-oxidation of intermediates of steroid metabolism, e.g. 5α-androstane-3α,17β-diol, dihydrotestosterone and Δ5-androstene-3β,17β-diol is described (for review see Mindnich et al. (2004b). Additionally, human 17β-HSD type 2 has high 20α-HSD activity with progestins (Puranen et al., 1999).
  5. ↑ Wang CT, Li CF, Wu WJ, Huang CN, Li CC, Li WM, Chan TC, Liang PI, Hsing CH, Liao KM (2016). "High Expression of 17β-hydroxysteroid Dehydrogenase Type 2 is Associated with a Better Prognosis in Urothelial Carcinoma of the Urinary Tract". Journal of Cancer. 7 (15): 2221–2230. doi:10.7150/jca.16777. PMC 5166531. PMID 27994658. HSD17B2 has both anti-estrogenic and anti-androgenic functions.
  6. ↑ 6.0 6.1 Mindnich R, Möller G, Adamski J (2004). "The role of 17 beta-hydroxysteroid dehydrogenases". Mol. Cell. Endocrinol. 218 (1–2): 7–20. doi:10.1016/j.mce.2003.12.006. PMID 15130507.
  7. ↑ Hilborn E, Stål O, Jansson A (May 2017). "Estrogen and androgen-converting enzymes 17β-hydroxysteroid dehydrogenase and their involvement in cancer: with a special focus on 17β-hydroxysteroid dehydrogenase type 1, 2, and breast cancer". Oncotarget. 8 (18): 30552–30562. doi:10.18632/oncotarget.15547. PMC 5444764. PMID 28430630.
  8. ↑ Zhu Y, Imperato-McGinley JL (9 November 2016). "4.02: Disorders of Sexual Development in Males: Molecular Genetics, Epigenetics, Gender Identity, and Cognition". In Lightman S. Hormones, Brain and Behavior. 4: Clinical Important Effects of Hormones on Brain and Behavior. Elsevier Science. p. 69. ISBN 978-0-12-803608-2.
  9. ↑ Moeller G, Adamski J (2009). "Integrated view on 17beta-hydroxysteroid dehydrogenases". Mol. Cell. Endocrinol. 301 (1–2): 7–19. doi:10.1016/j.mce.2008.10.040. PMID 19027824.
  10. ↑ Bulun SE, Cheng YH, Pavone ME, Yin P, Imir G, Utsunomiya H, Thung S, Xue Q, Marsh EE, Tokunaga H, Ishikawa H, Kurita T, Su EJ (2010). "17Beta-hydroxysteroid dehydrogenase-2 deficiency and progesterone resistance in endometriosis". Semin. Reprod. Med. 28 (1): 44–50. doi:10.1055/s-0029-1242992. PMC 4511594. PMID 20108182.
  11. ↑ Marchais-Oberwinkler S, Henn C, Möller G, Klein T, Negri M, Oster A, Spadaro A, Werth R, Wetzel M, Xu K, Frotscher M, Hartmann RW, Adamski J (2011). "17β-Hydroxysteroid dehydrogenases (17β-HSDs) as therapeutic targets: protein structures, functions, and recent progress in inhibitor development". J. Steroid Biochem. Mol. Biol. 125 (1–2): 66–82. doi:10.1016/j.jsbmb.2010.12.013. PMID 21193039.
  12. ↑ Soubhye J, Alard IC, van Antwerpen P, Dufrasne F (2015). "Type 2 17-β hydroxysteroid dehydrogenase as a novel target for the treatment of osteoporosis". Future Med Chem. 7 (11): 1431–56. doi:10.4155/fmc.15.74. PMID 26230882.
  13. ↑ J. Larry Jameson (13 July 1998). Principles of Molecular Medicine. Springer Science & Business Media. pp. 549–. ISBN 978-1-59259-726-0.

Further reading

  • Labrie Y, Durocher F, Lachance Y, Turgeon C, Simard J, Labrie C, Labrie F (Oct 1995). "The human type II 17 beta-hydroxysteroid dehydrogenase gene encodes two alternatively spliced mRNA species". DNA and Cell Biology. 14 (10): 849–61. doi:10.1089/dna.1995.14.849. PMID 7546291.
  • Andersson S, Geissler WM, Patel S, Wu L (Jun 1995). "The molecular biology of androgenic 17 beta-hydroxysteroid dehydrogenases". The Journal of Steroid Biochemistry and Molecular Biology. 53 (1–6): 37–9. doi:10.1016/0960-0760(95)00039-3. PMID 7626483.
  • Carsol JL, Martin PM, de Launoit Y (Oct 1994). "Characterization of 17 beta-hydroxysteroid dehydrogenase activity and mRNA abundance in human meningioma tumors". Neuroendocrinology. 60 (4): 445–51. doi:10.1159/000126779. PMID 7824086.
  • Wu L, Einstein M, Geissler WM, Chan HK, Elliston KO, Andersson S (Jun 1993). "Expression cloning and characterization of human 17 beta-hydroxysteroid dehydrogenase type 2, a microsomal enzyme possessing 20 alpha-hydroxysteroid dehydrogenase activity". The Journal of Biological Chemistry. 268 (17): 12964–9. PMID 8099587.
  • Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Zhang Y, Word RA, Fesmire S, Carr BR, Rainey WE (Oct 1996). "Human ovarian expression of 17 beta-hydroxysteroid dehydrogenase types 1, 2, and 3". The Journal of Clinical Endocrinology and Metabolism. 81 (10): 3594–8. doi:10.1210/jc.81.10.3594. PMID 8855807.
  • Moghrabi N, Head JR, Andersson S (Nov 1997). "Cell type-specific expression of 17 beta-hydroxysteroid dehydrogenase type 2 in human placenta and fetal liver". The Journal of Clinical Endocrinology and Metabolism. 82 (11): 3872–8. doi:10.1210/jc.82.11.3872. PMID 9360554.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Corbould AM, Judd SJ, Rodgers RJ (Jan 1998). "Expression of types 1, 2, and 3 17 beta-hydroxysteroid dehydrogenase in subcutaneous abdominal and intra-abdominal adipose tissue of women". The Journal of Clinical Endocrinology and Metabolism. 83 (1): 187–94. doi:10.1210/jc.83.1.187. PMID 9435439.
  • Dong Y, Qiu QQ, Debear J, Lathrop WF, Bertolini DR, Tamburini PP (Oct 1998). "17Beta-hydroxysteroid dehydrogenases in human bone cells". Journal of Bone and Mineral Research. 13 (10): 1539–46. doi:10.1359/jbmr.1998.13.10.1539. PMID 9783542.
  • Kitawaki J, Koshiba H, Ishihara H, Kusuki I, Tsukamoto K, Honjo H (Sep 2000). "Progesterone induction of 17beta-hydroxysteroid dehydrogenase type 2 during the secretory phase occurs in the endometrium of estrogen-dependent benign diseases but not in normal endometrium". The Journal of Clinical Endocrinology and Metabolism. 85 (9): 3292–6. doi:10.1210/jc.85.9.3292. PMID 10999824.
  • Sano T, Hirasawa G, Takeyama J, Darnel AD, Suzuki T, Moriya T, Kato K, Sekine H, Ohara S, Shimosegawa T, Nakamura J, Yoshihama M, Harada N, Sasano H (Nov 2001). "17 beta-Hydroxysteroid dehydrogenase type 2 expression and enzyme activity in the human gastrointestinal tract". Clinical Science. 101 (5): 485–91. doi:10.1042/CS20010052. PMID 11672453.
  • Lu ML, Huang YW, Lin SX (Jun 2002). "Purification, reconstitution, and steady-state kinetics of the trans-membrane 17 beta-hydroxysteroid dehydrogenase 2". The Journal of Biological Chemistry. 277 (25): 22123–30. doi:10.1074/jbc.M111726200. PMID 11940569.
  • Provost PR, Blomquist CH, Drolet R, Flamand N, Tremblay Y (Aug 2002). "Androgen inactivation in human lung fibroblasts: variations in levels of 17 beta-hydroxysteroid dehydrogenase type 2 and 5 alpha-reductase activity compatible with androgen inactivation". The Journal of Clinical Endocrinology and Metabolism. 87 (8): 3883–92. doi:10.1210/jc.87.8.3883. PMID 12161528.
  • Oliveira IO, Lhullier C, Brum IS, Spritzer PM (Sep 2003). "Gene expression of type 2 17 beta hydroxysteroid dehydrogenase in scalp hairs of hirsute women". Steroids. 68 (7–8): 641–9. doi:10.1016/S0039-128X(03)00093-X. PMID 12957669.
  • Oduwole OO, Mäkinen JM, Isomaa VV, Karttunen TJ, Vihko PT (2004). "Sex steroid metabolism in human gastric mucosa: 17 beta-hydroxysteroid dehydrogenase type 2 in normal, inflamed and neoplastic gastric tissues". Anticancer Research. 23 (5A): 3889–97. PMID 14666693.
  • Matsuzaki S, Canis M, Pouly JL, Déchelotte PJ, Mage G (Feb 2006). "Analysis of aromatase and 17beta-hydroxysteroid dehydrogenase type 2 messenger ribonucleic acid expression in deep endometriosis and eutopic endometrium using laser capture microdissection". Fertility and Sterility. 85 (2): 308–13. doi:10.1016/j.fertnstert.2005.08.017. PMID 16595205.
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