Expression of liver-specific member of the 3 beta-hydroxysteroid dehydrogenase family, an isoform possessing an almost exclusive 3-ketosteroid reductase activity
We have recently characterized two types of rat 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4 isomerase (3 beta-HSD) isoenzymes expressed in adrenals and gonads. In addition, we have cloned a third type of cDNA encoding a predicted type III 3 beta-HSD protein specifically expressed in the male...
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| Veröffentlicht in: | The Journal of biological chemistry 1992-03, Vol.267 (7), p.4513-4517 |
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| container_title | The Journal of biological chemistry |
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| creator | de Launoit, Y Zhao, H F Bélanger, A Labrie, F Simard, J |
| description | We have recently characterized two types of rat 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4 isomerase (3 beta-HSD)
isoenzymes expressed in adrenals and gonads. In addition, we have cloned a third type of cDNA encoding a predicted type III
3 beta-HSD protein specifically expressed in the male rat liver which shares 80% similarity with the two other isoenzymes.
Transient expression in human HeLa cells of the cDNAs reveals that the type III 3 beta-HSD protein does not display oxidative
activity for the classical substrates of 3 beta-HSD, in contrast to the type I 3 beta-HSD isoenzyme. However, in the presence
of NADH, type III isoenzyme, in common with the type I isoform, converts 5 alpha-androstane-3,17-dione (A-dione) and 5 alpha-dihydrotestosterone
(DHT) to the corresponding 3 beta-hydroxysteroids. In fact, the type I and the type III isoenzymes have the same affinity
for DHT with Km values of 5.05 and 6.16 microM, respectively. When NADPH is used as cofactor, the affinity for DHT of the
type III isoform becomes higher than that of the type I isoform with Km values of 0.12 and 1.18 microM, respectively. The
type III isoform is thus a 3-ketoreductase using NADPH as preferred cofactor which is responsible for the conversion of 3-keto-saturated
steroids such as DHT and A-dione into less active steroids. |
| doi_str_mv | 10.1016/S0021-9258(18)42863-3 |
| format | Article |
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isoenzymes expressed in adrenals and gonads. In addition, we have cloned a third type of cDNA encoding a predicted type III
3 beta-HSD protein specifically expressed in the male rat liver which shares 80% similarity with the two other isoenzymes.
Transient expression in human HeLa cells of the cDNAs reveals that the type III 3 beta-HSD protein does not display oxidative
activity for the classical substrates of 3 beta-HSD, in contrast to the type I 3 beta-HSD isoenzyme. However, in the presence
of NADH, type III isoenzyme, in common with the type I isoform, converts 5 alpha-androstane-3,17-dione (A-dione) and 5 alpha-dihydrotestosterone
(DHT) to the corresponding 3 beta-hydroxysteroids. In fact, the type I and the type III isoenzymes have the same affinity
for DHT with Km values of 5.05 and 6.16 microM, respectively. When NADPH is used as cofactor, the affinity for DHT of the
type III isoform becomes higher than that of the type I isoform with Km values of 0.12 and 1.18 microM, respectively. The
type III isoform is thus a 3-ketoreductase using NADPH as preferred cofactor which is responsible for the conversion of 3-keto-saturated
steroids such as DHT and A-dione into less active steroids.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)42863-3</identifier><identifier>PMID: 1537836</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>3 beta -hydroxysteroid dehydrogenase ; 3-Hydroxysteroid Dehydrogenases - genetics ; 3-Hydroxysteroid Dehydrogenases - metabolism ; activity ; Animals ; Catalysis ; characterization ; Chromatography, High Pressure Liquid ; Chromatography, Thin Layer ; Dihydrotestosterone - metabolism ; DNA - genetics ; Etiocholanolone - analogs & derivatives ; Etiocholanolone - metabolism ; Gene Expression ; HeLa Cells ; Humans ; Isoenzymes - genetics ; Isoenzymes - metabolism ; Kinetics ; liver ; Liver - enzymology ; Male ; NAD - metabolism ; NADP - metabolism ; oxidation ; Oxidation-Reduction ; Rats</subject><ispartof>The Journal of biological chemistry, 1992-03, Vol.267 (7), p.4513-4517</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c409t-dba7de1ea7aaaf883b30d19ea1a77ce4d84e1912f75a310648857072faf1b753</citedby><cites>FETCH-LOGICAL-c409t-dba7de1ea7aaaf883b30d19ea1a77ce4d84e1912f75a310648857072faf1b753</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1537836$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>de Launoit, Y</creatorcontrib><creatorcontrib>Zhao, H F</creatorcontrib><creatorcontrib>Bélanger, A</creatorcontrib><creatorcontrib>Labrie, F</creatorcontrib><creatorcontrib>Simard, J</creatorcontrib><title>Expression of liver-specific member of the 3 beta-hydroxysteroid dehydrogenase family, an isoform possessing an almost exclusive 3-ketosteroid reductase activity</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>We have recently characterized two types of rat 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4 isomerase (3 beta-HSD)
isoenzymes expressed in adrenals and gonads. In addition, we have cloned a third type of cDNA encoding a predicted type III
3 beta-HSD protein specifically expressed in the male rat liver which shares 80% similarity with the two other isoenzymes.
Transient expression in human HeLa cells of the cDNAs reveals that the type III 3 beta-HSD protein does not display oxidative
activity for the classical substrates of 3 beta-HSD, in contrast to the type I 3 beta-HSD isoenzyme. However, in the presence
of NADH, type III isoenzyme, in common with the type I isoform, converts 5 alpha-androstane-3,17-dione (A-dione) and 5 alpha-dihydrotestosterone
(DHT) to the corresponding 3 beta-hydroxysteroids. In fact, the type I and the type III isoenzymes have the same affinity
for DHT with Km values of 5.05 and 6.16 microM, respectively. When NADPH is used as cofactor, the affinity for DHT of the
type III isoform becomes higher than that of the type I isoform with Km values of 0.12 and 1.18 microM, respectively. The
type III isoform is thus a 3-ketoreductase using NADPH as preferred cofactor which is responsible for the conversion of 3-keto-saturated
steroids such as DHT and A-dione into less active steroids.</description><subject>3 beta -hydroxysteroid dehydrogenase</subject><subject>3-Hydroxysteroid Dehydrogenases - genetics</subject><subject>3-Hydroxysteroid Dehydrogenases - metabolism</subject><subject>activity</subject><subject>Animals</subject><subject>Catalysis</subject><subject>characterization</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Chromatography, Thin Layer</subject><subject>Dihydrotestosterone - metabolism</subject><subject>DNA - genetics</subject><subject>Etiocholanolone - analogs & derivatives</subject><subject>Etiocholanolone - metabolism</subject><subject>Gene Expression</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Isoenzymes - genetics</subject><subject>Isoenzymes - metabolism</subject><subject>Kinetics</subject><subject>liver</subject><subject>Liver - enzymology</subject><subject>Male</subject><subject>NAD - metabolism</subject><subject>NADP - metabolism</subject><subject>oxidation</subject><subject>Oxidation-Reduction</subject><subject>Rats</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcFu1DAURSMEKkPhEypZLBBIBPxiJ3aWqCotUiUWdMHOcpzniSGJg-2UyefwpyQzBZZ4Y-vd--6VfLLsAug7oFC9_0JpAXldlPI1yDe8kBXL2aNsB1SujxK-Ps52fy1Ps2cxfqPr4TWcZWdQMiFZtct-XR2mgDE6PxJvSe_uMeRxQuOsM2TAocGwCalDwkiDSefd0gZ_WGLC4F1LWjwO9jjqiMTqwfXLW6JH4qK3Pgxk8jFuDeN-m-p-8DERPJh-jmsbYfl3TP5PWsB2NmlL0ia5e5eW59kTq_uILx7u8-zu49Xd5U1--_n60-WH29xwWqe8bbRoEVALrbWVkjWMtlCjBi2EQd5KjlBDYUWpGdCKS1kKKgqrLTSiZOfZq1PsFPyPGWNSg4sG-16P6OeoRCFBMkn_a4SKc1HxejWWJ6MJ6w8EtGoKbtBhUUDVhlAdEaqNjwKpjggVW_cuHgrmZsD239aJ2aq_POmd23c_XUDVOG86HFRRCSUUL4Gx39QEpzU</recordid><startdate>19920305</startdate><enddate>19920305</enddate><creator>de Launoit, Y</creator><creator>Zhao, H F</creator><creator>Bélanger, A</creator><creator>Labrie, F</creator><creator>Simard, J</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19920305</creationdate><title>Expression of liver-specific member of the 3 beta-hydroxysteroid dehydrogenase family, an isoform possessing an almost exclusive 3-ketosteroid reductase activity</title><author>de Launoit, Y ; Zhao, H F ; Bélanger, A ; Labrie, F ; Simard, J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c409t-dba7de1ea7aaaf883b30d19ea1a77ce4d84e1912f75a310648857072faf1b753</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>3 beta -hydroxysteroid dehydrogenase</topic><topic>3-Hydroxysteroid Dehydrogenases - genetics</topic><topic>3-Hydroxysteroid Dehydrogenases - metabolism</topic><topic>activity</topic><topic>Animals</topic><topic>Catalysis</topic><topic>characterization</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Chromatography, Thin Layer</topic><topic>Dihydrotestosterone - metabolism</topic><topic>DNA - genetics</topic><topic>Etiocholanolone - analogs & derivatives</topic><topic>Etiocholanolone - metabolism</topic><topic>Gene Expression</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Isoenzymes - genetics</topic><topic>Isoenzymes - metabolism</topic><topic>Kinetics</topic><topic>liver</topic><topic>Liver - enzymology</topic><topic>Male</topic><topic>NAD - metabolism</topic><topic>NADP - metabolism</topic><topic>oxidation</topic><topic>Oxidation-Reduction</topic><topic>Rats</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>de Launoit, Y</creatorcontrib><creatorcontrib>Zhao, H F</creatorcontrib><creatorcontrib>Bélanger, A</creatorcontrib><creatorcontrib>Labrie, F</creatorcontrib><creatorcontrib>Simard, J</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>de Launoit, Y</au><au>Zhao, H F</au><au>Bélanger, A</au><au>Labrie, F</au><au>Simard, J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Expression of liver-specific member of the 3 beta-hydroxysteroid dehydrogenase family, an isoform possessing an almost exclusive 3-ketosteroid reductase activity</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1992-03-05</date><risdate>1992</risdate><volume>267</volume><issue>7</issue><spage>4513</spage><epage>4517</epage><pages>4513-4517</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>We have recently characterized two types of rat 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4 isomerase (3 beta-HSD)
isoenzymes expressed in adrenals and gonads. In addition, we have cloned a third type of cDNA encoding a predicted type III
3 beta-HSD protein specifically expressed in the male rat liver which shares 80% similarity with the two other isoenzymes.
Transient expression in human HeLa cells of the cDNAs reveals that the type III 3 beta-HSD protein does not display oxidative
activity for the classical substrates of 3 beta-HSD, in contrast to the type I 3 beta-HSD isoenzyme. However, in the presence
of NADH, type III isoenzyme, in common with the type I isoform, converts 5 alpha-androstane-3,17-dione (A-dione) and 5 alpha-dihydrotestosterone
(DHT) to the corresponding 3 beta-hydroxysteroids. In fact, the type I and the type III isoenzymes have the same affinity
for DHT with Km values of 5.05 and 6.16 microM, respectively. When NADPH is used as cofactor, the affinity for DHT of the
type III isoform becomes higher than that of the type I isoform with Km values of 0.12 and 1.18 microM, respectively. The
type III isoform is thus a 3-ketoreductase using NADPH as preferred cofactor which is responsible for the conversion of 3-keto-saturated
steroids such as DHT and A-dione into less active steroids.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1537836</pmid><doi>10.1016/S0021-9258(18)42863-3</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_pubmed_primary_1537836 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | 3 beta -hydroxysteroid dehydrogenase 3-Hydroxysteroid Dehydrogenases - genetics 3-Hydroxysteroid Dehydrogenases - metabolism activity Animals Catalysis characterization Chromatography, High Pressure Liquid Chromatography, Thin Layer Dihydrotestosterone - metabolism DNA - genetics Etiocholanolone - analogs & derivatives Etiocholanolone - metabolism Gene Expression HeLa Cells Humans Isoenzymes - genetics Isoenzymes - metabolism Kinetics liver Liver - enzymology Male NAD - metabolism NADP - metabolism oxidation Oxidation-Reduction Rats |
| title | Expression of liver-specific member of the 3 beta-hydroxysteroid dehydrogenase family, an isoform possessing an almost exclusive 3-ketosteroid reductase activity |
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