Production of an atrial natriuretic peptide variant that is specific for type A receptor
Receptor‐specific variants of atrial natriuretic peptide (ANP) were selected from libraries of filamentous phage particles that displayed single copies of random ANP mutants fused to gene III protein. These ANP variants were differentially selected by binding to immobilized natriuretic peptide recep...
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| Veröffentlicht in: | The EMBO journal 1994-06, Vol.13 (11), p.2508-2515 |
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| creator | Cunningham, B.C. Lowe, D.G. Li, B. Bennett, B.D. Wells, J.A. |
| description | Receptor‐specific variants of atrial natriuretic peptide (ANP) were selected from libraries of filamentous phage particles that displayed single copies of random ANP mutants fused to gene III protein. These ANP variants were differentially selected by binding to immobilized natriuretic peptide receptor A (NPR‐A) over competing receptor C (NPR‐C) in solution. This method also selected ANP variants with improved secretion expression in Escherichia coli. Several of the identified mutations were combined to produce an efficiently expressed ANP analog that was as potent as wild‐type ANP in stimulating NPR‐A guanylyl cyclase activity but resistant to inactivation mediated by NPR‐C. Such NPR‐A‐selective analogs should be useful for correlating the various activities of ANP to the relevant receptor and may also be more potent therapeutics in the targeting of NPR‐A. |
| doi_str_mv | 10.1002/j.1460-2075.1994.tb06540.x |
| format | Article |
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These ANP variants were differentially selected by binding to immobilized natriuretic peptide receptor A (NPR‐A) over competing receptor C (NPR‐C) in solution. This method also selected ANP variants with improved secretion expression in Escherichia coli. Several of the identified mutations were combined to produce an efficiently expressed ANP analog that was as potent as wild‐type ANP in stimulating NPR‐A guanylyl cyclase activity but resistant to inactivation mediated by NPR‐C. 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Technologies ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutation - genetics ; Protein engineering ; Receptors, Atrial Natriuretic Factor - metabolism ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - isolation & purification ; Recombinant Fusion Proteins - metabolism ; Sensitivity and Specificity</subject><ispartof>The EMBO journal, 1994-06, Vol.13 (11), p.2508-2515</ispartof><rights>1994 European Molecular Biology Organization</rights><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5070-98b100930f38e69afc2f216243eb33c8fb08ee787520d426b6662c7959274c903</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/PMC395124/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC395124/$$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=4111590$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8013451$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cunningham, B.C.</creatorcontrib><creatorcontrib>Lowe, D.G.</creatorcontrib><creatorcontrib>Li, B.</creatorcontrib><creatorcontrib>Bennett, B.D.</creatorcontrib><creatorcontrib>Wells, J.A.</creatorcontrib><title>Production of an atrial natriuretic peptide variant that is specific for type A receptor</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><description>Receptor‐specific variants of atrial natriuretic peptide (ANP) were selected from libraries of filamentous phage particles that displayed single copies of random ANP mutants fused to gene III protein. These ANP variants were differentially selected by binding to immobilized natriuretic peptide receptor A (NPR‐A) over competing receptor C (NPR‐C) in solution. This method also selected ANP variants with improved secretion expression in Escherichia coli. Several of the identified mutations were combined to produce an efficiently expressed ANP analog that was as potent as wild‐type ANP in stimulating NPR‐A guanylyl cyclase activity but resistant to inactivation mediated by NPR‐C. Such NPR‐A‐selective analogs should be useful for correlating the various activities of ANP to the relevant receptor and may also be more potent therapeutics in the targeting of NPR‐A.</description><subject>Amino Acid Sequence</subject><subject>Atrial Natriuretic Factor - chemistry</subject><subject>Atrial Natriuretic Factor - genetics</subject><subject>Atrial Natriuretic Factor - metabolism</subject><subject>Bacteriophages - genetics</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>DNA Mutational Analysis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Library</subject><subject>Genetic Techniques</subject><subject>Genetic Vectors - genetics</subject><subject>Humans</subject><subject>Methods. Procedures. Technologies</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Mutation - genetics</subject><subject>Protein engineering</subject><subject>Receptors, Atrial Natriuretic Factor - metabolism</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - isolation & purification</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Sensitivity and Specificity</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkEtP3DAUhS1URKdTfgKShbpNev1MXInFgCgUUcGilbqzHI8NHoUksj2U-fdNmNEIll3dK51z7uND6JRASQDo11VJuISCQiVKohQvcwNScChfDtBsL31AM6CSFJzU6iP6lNIKAERdkSN0VANhXJAZ-nMf--Xa5tB3uPfYdNjkGEyLu6muo8vB4sENOSwdfjaj1GWcH03GIeE0OBv8aPB9xHkzOLzA0dnR3cfP6NCbNrnjXZ2j398vf11cF7d3Vz8uFreFFVBBoepmfEkx8Kx2UhlvqadEUs5cw5itfQO1c1VdCQpLTmUjpaS2UkLRilsFbI7OtnOHdfPkltZ1OZpWDzE8mbjRvQn6vdKFR_3QP2umBBnXzNG3bd7GPqXo_D5KQE-09UpPSPWEVE-09Y62fhnDJ2-X76M7vKP-ZaebZE3ro-lsSHsbJ4SI1x8WW9vf0LrNfxygL3-e37z27B-d0J3v</recordid><startdate>199406</startdate><enddate>199406</enddate><creator>Cunningham, B.C.</creator><creator>Lowe, D.G.</creator><creator>Li, B.</creator><creator>Bennett, B.D.</creator><creator>Wells, J.A.</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>5PM</scope></search><sort><creationdate>199406</creationdate><title>Production of an atrial natriuretic peptide variant that is specific for type A receptor</title><author>Cunningham, B.C. ; Lowe, D.G. ; Li, B. ; Bennett, B.D. ; Wells, J.A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5070-98b100930f38e69afc2f216243eb33c8fb08ee787520d426b6662c7959274c903</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>Atrial Natriuretic Factor - chemistry</topic><topic>Atrial Natriuretic Factor - genetics</topic><topic>Atrial Natriuretic Factor - metabolism</topic><topic>Bacteriophages - genetics</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>DNA Mutational Analysis</topic><topic>Fundamental and applied biological sciences. 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Technologies</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Site-Directed</topic><topic>Mutation - genetics</topic><topic>Protein engineering</topic><topic>Receptors, Atrial Natriuretic Factor - metabolism</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - isolation & purification</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Sensitivity and Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cunningham, B.C.</creatorcontrib><creatorcontrib>Lowe, D.G.</creatorcontrib><creatorcontrib>Li, B.</creatorcontrib><creatorcontrib>Bennett, B.D.</creatorcontrib><creatorcontrib>Wells, J.A.</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>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cunningham, B.C.</au><au>Lowe, D.G.</au><au>Li, B.</au><au>Bennett, B.D.</au><au>Wells, J.A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Production of an atrial natriuretic peptide variant that is specific for type A receptor</atitle><jtitle>The EMBO journal</jtitle><addtitle>EMBO J</addtitle><date>1994-06</date><risdate>1994</risdate><volume>13</volume><issue>11</issue><spage>2508</spage><epage>2515</epage><pages>2508-2515</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>Receptor‐specific variants of atrial natriuretic peptide (ANP) were selected from libraries of filamentous phage particles that displayed single copies of random ANP mutants fused to gene III protein. These ANP variants were differentially selected by binding to immobilized natriuretic peptide receptor A (NPR‐A) over competing receptor C (NPR‐C) in solution. This method also selected ANP variants with improved secretion expression in Escherichia coli. Several of the identified mutations were combined to produce an efficiently expressed ANP analog that was as potent as wild‐type ANP in stimulating NPR‐A guanylyl cyclase activity but resistant to inactivation mediated by NPR‐C. Such NPR‐A‐selective analogs should be useful for correlating the various activities of ANP to the relevant receptor and may also be more potent therapeutics in the targeting of NPR‐A.</abstract><cop>London</cop><pub>Nature Publishing Group</pub><pmid>8013451</pmid><doi>10.1002/j.1460-2075.1994.tb06540.x</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry; EZB Electronic Journals Library |
| subjects | Amino Acid Sequence Atrial Natriuretic Factor - chemistry Atrial Natriuretic Factor - genetics Atrial Natriuretic Factor - metabolism Bacteriophages - genetics Base Sequence Biological and medical sciences Biotechnology DNA Mutational Analysis Fundamental and applied biological sciences. Psychology Gene Library Genetic Techniques Genetic Vectors - genetics Humans Methods. Procedures. Technologies Molecular Sequence Data Mutagenesis, Site-Directed Mutation - genetics Protein engineering Receptors, Atrial Natriuretic Factor - metabolism Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - isolation & purification Recombinant Fusion Proteins - metabolism Sensitivity and Specificity |
| title | Production of an atrial natriuretic peptide variant that is specific for type A receptor |
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