Isolation and Characterization of a Rat Luteal cDNA Encoding 20α-Hydroxysteroid Dehydrogenase
We report the isolation and characterization of a full length cDNA encoding rat 20αhydroxysteroid dehydrogenase derived from rat corpus luteum RNA. The predicted amino acid sequence of the protein encoded by the 20αHSD clone is composed of 323 amino acids possessing an approximate molecular weight o...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1994-06, Vol.201 (3), p.1289-1295 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Mao, J. Duan, W.R. Albarracin, C.T. Parmer, T.G. Gibori, G. |
| description | We report the isolation and characterization of a full length cDNA encoding rat 20αhydroxysteroid dehydrogenase derived from rat corpus luteum RNA. The predicted amino acid sequence of the protein encoded by the 20αHSD clone is composed of 323 amino acids possessing an approximate molecular weight of 37 kDa. The sequence of peptides derived from the purified protein was found in the translated sequence of the open reading frame. cDNA and amino acid sequence indicate that the rat ovarian 20αHSD belongs to the aldo-keto reductase family of enzymes. Northern analysis revealed a 1.2 Kb 20αHSD mRNA in corpora lutea undergoing luteolysis. Prolactin reduced markedly 20αHSD mRNA expression. No signal was detected in other tissues examined, demonstrating the specific expression of this enzyme in the corpus luteum. |
| doi_str_mv | 10.1006/bbrc.1994.1844 |
| format | Article |
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The predicted amino acid sequence of the protein encoded by the 20αHSD clone is composed of 323 amino acids possessing an approximate molecular weight of 37 kDa. The sequence of peptides derived from the purified protein was found in the translated sequence of the open reading frame. cDNA and amino acid sequence indicate that the rat ovarian 20αHSD belongs to the aldo-keto reductase family of enzymes. Northern analysis revealed a 1.2 Kb 20αHSD mRNA in corpora lutea undergoing luteolysis. Prolactin reduced markedly 20αHSD mRNA expression. 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The predicted amino acid sequence of the protein encoded by the 20αHSD clone is composed of 323 amino acids possessing an approximate molecular weight of 37 kDa. The sequence of peptides derived from the purified protein was found in the translated sequence of the open reading frame. cDNA and amino acid sequence indicate that the rat ovarian 20αHSD belongs to the aldo-keto reductase family of enzymes. Northern analysis revealed a 1.2 Kb 20αHSD mRNA in corpora lutea undergoing luteolysis. Prolactin reduced markedly 20αHSD mRNA expression. No signal was detected in other tissues examined, demonstrating the specific expression of this enzyme in the corpus luteum.</description><subject>20-Hydroxysteroid Dehydrogenases - chemistry</subject><subject>20-Hydroxysteroid Dehydrogenases - genetics</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Cloning, Molecular</subject><subject>Corpus Luteum - physiology</subject><subject>DNA, Complementary - genetics</subject><subject>Female</subject><subject>Gene Expression - drug effects</subject><subject>Gene Library</subject><subject>Molecular Sequence Data</subject><subject>Prolactin - pharmacology</subject><subject>Rats</subject><subject>RNA, Messenger - genetics</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Solubility</subject><subject>Tissue Distribution</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMFq3DAQhkVpSbZpr70FdOrN25FtWdIxbJImsLRQGsipQh6NExWvlUjekO1b9UX6TLXZJbfS0wwz3_wwH2MfBCwFQPOpbRMuhTH1Uui6fsUWAgwUpYD6NVvARBSlEbfH7G3OPwGEqBtzxI40lLVU1YL9uM6xd2OIA3eD56t7lxyOlMKv_TB23PFvbuTr7Uiu53j-5YxfDBh9GO54CX9-F1c7n-LzLk9XMXh-Tvfz4I4Gl-kde9O5PtP7Qz1hN5cX31dXxfrr5-vV2brASsFYKFRIRB0q6Ay0XrSidEpr56FTNbVSTA-ZUkopdNd0jZHoprZFkIgeTXXCPu5zH1J83FIe7SZkpL53A8VttqqRqqmk_C8oGi0brasJXO5BTDHnRJ19SGHj0s4KsLN5O5u3s3k7m58OTg_J23ZD_gU_qJ72er-nycNToGQzBhqQfEiEo_Ux_Cv6L5HKk1g</recordid><startdate>19940630</startdate><enddate>19940630</enddate><creator>Mao, J.</creator><creator>Duan, W.R.</creator><creator>Albarracin, C.T.</creator><creator>Parmer, T.G.</creator><creator>Gibori, G.</creator><general>Elsevier Inc</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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19940630</creationdate><title>Isolation and Characterization of a Rat Luteal cDNA Encoding 20α-Hydroxysteroid Dehydrogenase</title><author>Mao, J. ; Duan, W.R. ; Albarracin, C.T. ; Parmer, T.G. ; Gibori, G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c370t-7c7ceeefc70f90bd1b12a788ad0f74eb512109255518f6f695ca518bc05ccdc93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>20-Hydroxysteroid Dehydrogenases - chemistry</topic><topic>20-Hydroxysteroid Dehydrogenases - genetics</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Cloning, Molecular</topic><topic>Corpus Luteum - physiology</topic><topic>DNA, Complementary - genetics</topic><topic>Female</topic><topic>Gene Expression - drug effects</topic><topic>Gene Library</topic><topic>Molecular Sequence Data</topic><topic>Prolactin - pharmacology</topic><topic>Rats</topic><topic>RNA, Messenger - genetics</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>Solubility</topic><topic>Tissue Distribution</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mao, J.</creatorcontrib><creatorcontrib>Duan, W.R.</creatorcontrib><creatorcontrib>Albarracin, C.T.</creatorcontrib><creatorcontrib>Parmer, T.G.</creatorcontrib><creatorcontrib>Gibori, G.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mao, J.</au><au>Duan, W.R.</au><au>Albarracin, C.T.</au><au>Parmer, T.G.</au><au>Gibori, G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation and Characterization of a Rat Luteal cDNA Encoding 20α-Hydroxysteroid Dehydrogenase</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1994-06-30</date><risdate>1994</risdate><volume>201</volume><issue>3</issue><spage>1289</spage><epage>1295</epage><pages>1289-1295</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>We report the isolation and characterization of a full length cDNA encoding rat 20αhydroxysteroid dehydrogenase derived from rat corpus luteum RNA. The predicted amino acid sequence of the protein encoded by the 20αHSD clone is composed of 323 amino acids possessing an approximate molecular weight of 37 kDa. The sequence of peptides derived from the purified protein was found in the translated sequence of the open reading frame. cDNA and amino acid sequence indicate that the rat ovarian 20αHSD belongs to the aldo-keto reductase family of enzymes. Northern analysis revealed a 1.2 Kb 20αHSD mRNA in corpora lutea undergoing luteolysis. Prolactin reduced markedly 20αHSD mRNA expression. No signal was detected in other tissues examined, demonstrating the specific expression of this enzyme in the corpus luteum.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>8024573</pmid><doi>10.1006/bbrc.1994.1844</doi><tpages>7</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1994-06, Vol.201 (3), p.1289-1295 |
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| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | 20-Hydroxysteroid Dehydrogenases - chemistry 20-Hydroxysteroid Dehydrogenases - genetics Amino Acid Sequence Animals Base Sequence Cloning, Molecular Corpus Luteum - physiology DNA, Complementary - genetics Female Gene Expression - drug effects Gene Library Molecular Sequence Data Prolactin - pharmacology Rats RNA, Messenger - genetics Sequence Alignment Sequence Homology, Amino Acid Solubility Tissue Distribution |
| title | Isolation and Characterization of a Rat Luteal cDNA Encoding 20α-Hydroxysteroid Dehydrogenase |
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