Protease‐nexin I as an androgen‐dependent secretory product of the murine seminal vesicle
A search for inhibitors of urokinase‐type plasminogen activator (uPA) in the male and female murine genital tracts revealed high levels of a uPA ligand in the seminal vesicle. This ligand is functionally, biochemically and immunologically indistinguishable from protease‐nexin I (PN‐I), a serpin liga...
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Veröffentlicht in: | The EMBO journal 1993-05, Vol.12 (5), p.1871-1878 |
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creator | Vassalli, J.D. Huarte, J. Bosco, D. Sappino, A.P. Sappino, N. Velardi, A. Wohlwend, A. Ernø, H. Monard, D. Belin, D. |
description | A search for inhibitors of urokinase‐type plasminogen activator (uPA) in the male and female murine genital tracts revealed high levels of a uPA ligand in the seminal vesicle. This ligand is functionally, biochemically and immunologically indistinguishable from protease‐nexin I (PN‐I), a serpin ligand of thrombin and uPA previously detected only in mesenchymal cells and astrocytes. A survey of murine tissues indicates that PN‐I mRNA is most abundant in seminal vesicles, where it represents 0.2–0.4% of the mRNAs. PN‐I is synthesized in the epithelium of the seminal vesicle, as determined by in situ hybridization, and is secreted in the lumen of the gland. PN‐I levels are much lower in immature animals, and strongly decreased upon castration. Testosterone treatment of castrated males rapidly restores PN‐I mRNA levels, indicating that PN‐I gene expression is under androgen control. |
doi_str_mv | 10.1002/j.1460-2075.1993.tb05835.x |
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This ligand is functionally, biochemically and immunologically indistinguishable from protease‐nexin I (PN‐I), a serpin ligand of thrombin and uPA previously detected only in mesenchymal cells and astrocytes. A survey of murine tissues indicates that PN‐I mRNA is most abundant in seminal vesicles, where it represents 0.2–0.4% of the mRNAs. PN‐I is synthesized in the epithelium of the seminal vesicle, as determined by in situ hybridization, and is secreted in the lumen of the gland. PN‐I levels are much lower in immature animals, and strongly decreased upon castration. Testosterone treatment of castrated males rapidly restores PN‐I mRNA levels, indicating that PN‐I gene expression is under androgen control.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1002/j.1460-2075.1993.tb05835.x</identifier><identifier>PMID: 8491179</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>London: Nature Publishing Group</publisher><subject>Amyloid beta-Protein Precursor ; Animals ; Base Sequence ; Biological and medical sciences ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cells, Cultured ; DNA ; Female ; Fundamental and applied biological sciences. Psychology ; Hormone metabolism and regulation ; Humans ; Male ; Mammalian male genital system ; Mice ; Molecular Sequence Data ; Plasminogen Inactivators - genetics ; Plasminogen Inactivators - metabolism ; Protease Nexins ; Rats ; Receptors, Cell Surface ; RNA, Messenger - genetics ; Seminal Vesicles - metabolism ; Sequence Homology, Nucleic Acid ; Serpins - metabolism ; Testosterone - physiology ; Tumor Cells, Cultured ; Urokinase-Type Plasminogen Activator - antagonists & inhibitors ; Vertebrates: reproduction</subject><ispartof>The EMBO journal, 1993-05, Vol.12 (5), p.1871-1878</ispartof><rights>1993 European Molecular Biology Organization</rights><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5735-6c63309597c51a34c735ec8655e9127ef7ed69ee857b9fa47f363b1183923a93</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC413407/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC413407/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4710668$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8491179$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vassalli, J.D.</creatorcontrib><creatorcontrib>Huarte, J.</creatorcontrib><creatorcontrib>Bosco, D.</creatorcontrib><creatorcontrib>Sappino, A.P.</creatorcontrib><creatorcontrib>Sappino, N.</creatorcontrib><creatorcontrib>Velardi, A.</creatorcontrib><creatorcontrib>Wohlwend, A.</creatorcontrib><creatorcontrib>Ernø, H.</creatorcontrib><creatorcontrib>Monard, D.</creatorcontrib><creatorcontrib>Belin, D.</creatorcontrib><title>Protease‐nexin I as an androgen‐dependent secretory product of the murine seminal vesicle</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><description>A search for inhibitors of urokinase‐type plasminogen activator (uPA) in the male and female murine genital tracts revealed high levels of a uPA ligand in the seminal vesicle. This ligand is functionally, biochemically and immunologically indistinguishable from protease‐nexin I (PN‐I), a serpin ligand of thrombin and uPA previously detected only in mesenchymal cells and astrocytes. A survey of murine tissues indicates that PN‐I mRNA is most abundant in seminal vesicles, where it represents 0.2–0.4% of the mRNAs. PN‐I is synthesized in the epithelium of the seminal vesicle, as determined by in situ hybridization, and is secreted in the lumen of the gland. PN‐I levels are much lower in immature animals, and strongly decreased upon castration. Testosterone treatment of castrated males rapidly restores PN‐I mRNA levels, indicating that PN‐I gene expression is under androgen control.</description><subject>Amyloid beta-Protein Precursor</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Cells, Cultured</subject><subject>DNA</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hormone metabolism and regulation</subject><subject>Humans</subject><subject>Male</subject><subject>Mammalian male genital system</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Plasminogen Inactivators - genetics</subject><subject>Plasminogen Inactivators - metabolism</subject><subject>Protease Nexins</subject><subject>Rats</subject><subject>Receptors, Cell Surface</subject><subject>RNA, Messenger - genetics</subject><subject>Seminal Vesicles - metabolism</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Serpins - metabolism</subject><subject>Testosterone - physiology</subject><subject>Tumor Cells, Cultured</subject><subject>Urokinase-Type Plasminogen Activator - antagonists & inhibitors</subject><subject>Vertebrates: reproduction</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkd-K1DAYxYMo67j6CEIR8a41af41ghe7y6orK3qxtxIy6dfdDG0yJu06c-cj-Iw-ialTBr0UAgn5nZMcvoPQC4IrgnH9elMRJnBZY8krohStxjXmDeXV7gFaHdFDtMK1ICUjjXqMnqS0wTjLJDlBJw1ThEi1Ql-_xDCCSfDrx08PO-eLq8Kkwvi82hhuwWfQwhZ8C34sEtgIY4j7YhtDO9mxCF0x3kExTNF5yHxw3vTFPSRne3iKHnWmT_Bs2U_RzbvLm4sP5fXn91cXZ9el5ZLyUlhBKVZcScuJoczmS7CN4BwUqSV0ElqhABou16ozTHZU0DUhDVU1NYqeoreHZ7fTeoDW5qTR9Hob3WDiXgfj9L_Euzt9G-41I5Rhmf2vFn8M3yZIox5cstD3xkOYkpY5JRVsFr45CG0MKUXojn8QrOdq9EbP89fz_PVcjV6q0btsfv53yqN16SLzlws3yZq-i8Zbl44yJgkWosmys4Psu-th_x8B9OWn849_zvQ30-2vqA</recordid><startdate>199305</startdate><enddate>199305</enddate><creator>Vassalli, J.D.</creator><creator>Huarte, J.</creator><creator>Bosco, D.</creator><creator>Sappino, A.P.</creator><creator>Sappino, N.</creator><creator>Velardi, A.</creator><creator>Wohlwend, A.</creator><creator>Ernø, H.</creator><creator>Monard, D.</creator><creator>Belin, D.</creator><general>Nature Publishing Group</general><scope>IQODW</scope><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>7X8</scope><scope>5PM</scope></search><sort><creationdate>199305</creationdate><title>Protease‐nexin I as an androgen‐dependent secretory product of the murine seminal vesicle</title><author>Vassalli, J.D. ; Huarte, J. ; Bosco, D. ; Sappino, A.P. ; Sappino, N. ; Velardi, A. ; Wohlwend, A. ; Ernø, H. ; Monard, D. ; Belin, D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5735-6c63309597c51a34c735ec8655e9127ef7ed69ee857b9fa47f363b1183923a93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Amyloid beta-Protein Precursor</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>Cells, Cultured</topic><topic>DNA</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hormone metabolism and regulation</topic><topic>Humans</topic><topic>Male</topic><topic>Mammalian male genital system</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Plasminogen Inactivators - genetics</topic><topic>Plasminogen Inactivators - metabolism</topic><topic>Protease Nexins</topic><topic>Rats</topic><topic>Receptors, Cell Surface</topic><topic>RNA, Messenger - genetics</topic><topic>Seminal Vesicles - metabolism</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Serpins - metabolism</topic><topic>Testosterone - physiology</topic><topic>Tumor Cells, Cultured</topic><topic>Urokinase-Type Plasminogen Activator - antagonists & inhibitors</topic><topic>Vertebrates: reproduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vassalli, J.D.</creatorcontrib><creatorcontrib>Huarte, J.</creatorcontrib><creatorcontrib>Bosco, D.</creatorcontrib><creatorcontrib>Sappino, A.P.</creatorcontrib><creatorcontrib>Sappino, N.</creatorcontrib><creatorcontrib>Velardi, A.</creatorcontrib><creatorcontrib>Wohlwend, A.</creatorcontrib><creatorcontrib>Ernø, H.</creatorcontrib><creatorcontrib>Monard, D.</creatorcontrib><creatorcontrib>Belin, D.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vassalli, J.D.</au><au>Huarte, J.</au><au>Bosco, D.</au><au>Sappino, A.P.</au><au>Sappino, N.</au><au>Velardi, A.</au><au>Wohlwend, A.</au><au>Ernø, H.</au><au>Monard, D.</au><au>Belin, D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protease‐nexin I as an androgen‐dependent secretory product of the murine seminal vesicle</atitle><jtitle>The EMBO journal</jtitle><addtitle>EMBO J</addtitle><date>1993-05</date><risdate>1993</risdate><volume>12</volume><issue>5</issue><spage>1871</spage><epage>1878</epage><pages>1871-1878</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>A search for inhibitors of urokinase‐type plasminogen activator (uPA) in the male and female murine genital tracts revealed high levels of a uPA ligand in the seminal vesicle. This ligand is functionally, biochemically and immunologically indistinguishable from protease‐nexin I (PN‐I), a serpin ligand of thrombin and uPA previously detected only in mesenchymal cells and astrocytes. A survey of murine tissues indicates that PN‐I mRNA is most abundant in seminal vesicles, where it represents 0.2–0.4% of the mRNAs. PN‐I is synthesized in the epithelium of the seminal vesicle, as determined by in situ hybridization, and is secreted in the lumen of the gland. PN‐I levels are much lower in immature animals, and strongly decreased upon castration. Testosterone treatment of castrated males rapidly restores PN‐I mRNA levels, indicating that PN‐I gene expression is under androgen control.</abstract><cop>London</cop><pub>Nature Publishing Group</pub><pmid>8491179</pmid><doi>10.1002/j.1460-2075.1993.tb05835.x</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amyloid beta-Protein Precursor Animals Base Sequence Biological and medical sciences Carrier Proteins - genetics Carrier Proteins - metabolism Cells, Cultured DNA Female Fundamental and applied biological sciences. Psychology Hormone metabolism and regulation Humans Male Mammalian male genital system Mice Molecular Sequence Data Plasminogen Inactivators - genetics Plasminogen Inactivators - metabolism Protease Nexins Rats Receptors, Cell Surface RNA, Messenger - genetics Seminal Vesicles - metabolism Sequence Homology, Nucleic Acid Serpins - metabolism Testosterone - physiology Tumor Cells, Cultured Urokinase-Type Plasminogen Activator - antagonists & inhibitors Vertebrates: reproduction |
title | Protease‐nexin I as an androgen‐dependent secretory product of the murine seminal vesicle |
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