Cloning, nucleotide sequencing and expression of cDNAs encoding mouse urokinase‐type plasminogen activator
Controlled extracellular proteolysis is catalyzed in part by the secretion of plasminogen activators. As a step in the study of the expression of these enzymes in mouse tissues, we have isolated five cDNAs encoding the mouse urokinase‐type plasminogen activator from a cDNA library prepared with size...
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Veröffentlicht in: | European journal of biochemistry 1985-04, Vol.148 (2), p.225-232 |
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container_title | European journal of biochemistry |
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creator | BELIN, Dominique VASSALLI, Jean‐Dominique COMBÉPINE, Chantal GODEAU, François NAGAMINE, Yoshikuni REICH, Edward KOCHER, Hans P. DUVOISIN, Robert M. |
description | Controlled extracellular proteolysis is catalyzed in part by the secretion of plasminogen activators. As a step in the study of the expression of these enzymes in mouse tissues, we have isolated five cDNAs encoding the mouse urokinase‐type plasminogen activator from a cDNA library prepared with size‐selected mRNA from MSV‐transformed 3T3 cells. The longest cDNA insert contains the entire coding region of mouse urokinase, 58 base pairs of the 5′ non‐coding region, and the entire 3′ non‐coding region, which is 942 base pairs long. The deduced protein sequence, which starts with a signal peptide of 20 amino acids, shows extensive homology to that of human and porcine urokinase. However, in contrast to these enzymes, mouse urokinase contains no N‐glycosylation site. Bacteria harbouring one of the recombinant plasmids synthesize and secrete into their periplasm a protease indistinguishable from mouse urokinase. |
doi_str_mv | 10.1111/j.1432-1033.1985.tb08829.x |
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As a step in the study of the expression of these enzymes in mouse tissues, we have isolated five cDNAs encoding the mouse urokinase‐type plasminogen activator from a cDNA library prepared with size‐selected mRNA from MSV‐transformed 3T3 cells. The longest cDNA insert contains the entire coding region of mouse urokinase, 58 base pairs of the 5′ non‐coding region, and the entire 3′ non‐coding region, which is 942 base pairs long. The deduced protein sequence, which starts with a signal peptide of 20 amino acids, shows extensive homology to that of human and porcine urokinase. However, in contrast to these enzymes, mouse urokinase contains no N‐glycosylation site. Bacteria harbouring one of the recombinant plasmids synthesize and secrete into their periplasm a protease indistinguishable from mouse urokinase.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1985.tb08829.x</identifier><identifier>PMID: 2985383</identifier><identifier>CODEN: EJBCAI</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Biological and medical sciences ; Biotechnology ; Cloning, Molecular ; DNA - isolation & purification ; DNA Transposable Elements ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation ; Genetic engineering ; Genetic technics ; Methods. Procedures. Technologies ; Mice ; Molecular cloning ; Nucleic Acid Hybridization ; Plasminogen Activators - genetics ; Urokinase-Type Plasminogen Activator - genetics</subject><ispartof>European journal of biochemistry, 1985-04, Vol.148 (2), p.225-232</ispartof><rights>1986 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5175-69856bd29a3f336fa75799cc245e60f1df824da68ccd54cb7fa9acd53d75c4bd3</citedby><cites>FETCH-LOGICAL-c5175-69856bd29a3f336fa75799cc245e60f1df824da68ccd54cb7fa9acd53d75c4bd3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8446083$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2985383$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>BELIN, Dominique</creatorcontrib><creatorcontrib>VASSALLI, Jean‐Dominique</creatorcontrib><creatorcontrib>COMBÉPINE, Chantal</creatorcontrib><creatorcontrib>GODEAU, François</creatorcontrib><creatorcontrib>NAGAMINE, Yoshikuni</creatorcontrib><creatorcontrib>REICH, Edward</creatorcontrib><creatorcontrib>KOCHER, Hans P.</creatorcontrib><creatorcontrib>DUVOISIN, Robert M.</creatorcontrib><title>Cloning, nucleotide sequencing and expression of cDNAs encoding mouse urokinase‐type plasminogen activator</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>Controlled extracellular proteolysis is catalyzed in part by the secretion of plasminogen activators. As a step in the study of the expression of these enzymes in mouse tissues, we have isolated five cDNAs encoding the mouse urokinase‐type plasminogen activator from a cDNA library prepared with size‐selected mRNA from MSV‐transformed 3T3 cells. The longest cDNA insert contains the entire coding region of mouse urokinase, 58 base pairs of the 5′ non‐coding region, and the entire 3′ non‐coding region, which is 942 base pairs long. The deduced protein sequence, which starts with a signal peptide of 20 amino acids, shows extensive homology to that of human and porcine urokinase. However, in contrast to these enzymes, mouse urokinase contains no N‐glycosylation site. Bacteria harbouring one of the recombinant plasmids synthesize and secrete into their periplasm a protease indistinguishable from mouse urokinase.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Cloning, Molecular</subject><subject>DNA - isolation & purification</subject><subject>DNA Transposable Elements</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation</subject><subject>Genetic engineering</subject><subject>Genetic technics</subject><subject>Methods. Procedures. Technologies</subject><subject>Mice</subject><subject>Molecular cloning</subject><subject>Nucleic Acid Hybridization</subject><subject>Plasminogen Activators - genetics</subject><subject>Urokinase-Type Plasminogen Activator - genetics</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkMtu1DAYhS0EKkPhEZAshFg1wfckbFAZWkCqYAGsLceXykNip3FCZ3Y8As_Ik-Aw0ezxxpbPOb-PPwBeYFTivF7vSswoKTCitMRNzcupRXVNmnL_AGxO0kOwQQizgjRcPAZPUtohhEQjqjNwRnKK1nQDum0Xgw-3FzDMurNx8sbCZO9mG3S-hioYaPfDaFPyMcDooH7_-TLBLEezGPo4JwvnMf7wQSX759fv6TBYOHQq9T7EWxug0pP_qaY4PgWPnOqSfbbu5-D79dW37cfi5suHT9vLm0JzXPFC5HKiNaRR1FEqnKp41TRaE8atQA4bVxNmlKi1NpzptnKqUflITcU1aw09B6-Oc4cx5p-kSfY-adt1KthcV2KGMwdBs_HN0ajHmNJonRxG36vxIDGSC2q5kwtPufCUC2q5opb7HH6-vjK3vTWn6Mo26y9XXSWtOjeqjDSdbDVjAv2zvT3a7n1nD_9RQF5fvftKCKd_Ae-Qnx0</recordid><startdate>198504</startdate><enddate>198504</enddate><creator>BELIN, Dominique</creator><creator>VASSALLI, Jean‐Dominique</creator><creator>COMBÉPINE, Chantal</creator><creator>GODEAU, François</creator><creator>NAGAMINE, Yoshikuni</creator><creator>REICH, Edward</creator><creator>KOCHER, Hans P.</creator><creator>DUVOISIN, Robert M.</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</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>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>198504</creationdate><title>Cloning, nucleotide sequencing and expression of cDNAs encoding mouse urokinase‐type plasminogen activator</title><author>BELIN, Dominique ; VASSALLI, Jean‐Dominique ; COMBÉPINE, Chantal ; GODEAU, François ; NAGAMINE, Yoshikuni ; REICH, Edward ; KOCHER, Hans P. ; DUVOISIN, Robert M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5175-69856bd29a3f336fa75799cc245e60f1df824da68ccd54cb7fa9acd53d75c4bd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Cloning, Molecular</topic><topic>DNA - isolation & purification</topic><topic>DNA Transposable Elements</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression Regulation</topic><topic>Genetic engineering</topic><topic>Genetic technics</topic><topic>Methods. Procedures. Technologies</topic><topic>Mice</topic><topic>Molecular cloning</topic><topic>Nucleic Acid Hybridization</topic><topic>Plasminogen Activators - genetics</topic><topic>Urokinase-Type Plasminogen Activator - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>BELIN, Dominique</creatorcontrib><creatorcontrib>VASSALLI, Jean‐Dominique</creatorcontrib><creatorcontrib>COMBÉPINE, Chantal</creatorcontrib><creatorcontrib>GODEAU, François</creatorcontrib><creatorcontrib>NAGAMINE, Yoshikuni</creatorcontrib><creatorcontrib>REICH, Edward</creatorcontrib><creatorcontrib>KOCHER, Hans P.</creatorcontrib><creatorcontrib>DUVOISIN, Robert M.</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>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>BELIN, Dominique</au><au>VASSALLI, Jean‐Dominique</au><au>COMBÉPINE, Chantal</au><au>GODEAU, François</au><au>NAGAMINE, Yoshikuni</au><au>REICH, Edward</au><au>KOCHER, Hans P.</au><au>DUVOISIN, Robert M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning, nucleotide sequencing and expression of cDNAs encoding mouse urokinase‐type plasminogen activator</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1985-04</date><risdate>1985</risdate><volume>148</volume><issue>2</issue><spage>225</spage><epage>232</epage><pages>225-232</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><coden>EJBCAI</coden><abstract>Controlled extracellular proteolysis is catalyzed in part by the secretion of plasminogen activators. As a step in the study of the expression of these enzymes in mouse tissues, we have isolated five cDNAs encoding the mouse urokinase‐type plasminogen activator from a cDNA library prepared with size‐selected mRNA from MSV‐transformed 3T3 cells. The longest cDNA insert contains the entire coding region of mouse urokinase, 58 base pairs of the 5′ non‐coding region, and the entire 3′ non‐coding region, which is 942 base pairs long. The deduced protein sequence, which starts with a signal peptide of 20 amino acids, shows extensive homology to that of human and porcine urokinase. However, in contrast to these enzymes, mouse urokinase contains no N‐glycosylation site. Bacteria harbouring one of the recombinant plasmids synthesize and secrete into their periplasm a protease indistinguishable from mouse urokinase.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>2985383</pmid><doi>10.1111/j.1432-1033.1985.tb08829.x</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Animals Base Sequence Biological and medical sciences Biotechnology Cloning, Molecular DNA - isolation & purification DNA Transposable Elements Fundamental and applied biological sciences. Psychology Gene Expression Regulation Genetic engineering Genetic technics Methods. Procedures. Technologies Mice Molecular cloning Nucleic Acid Hybridization Plasminogen Activators - genetics Urokinase-Type Plasminogen Activator - genetics |
title | Cloning, nucleotide sequencing and expression of cDNAs encoding mouse urokinase‐type plasminogen activator |
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