MOLECULAR CLONING OF THE GUINEA-PIG IL-5 RECEPTOR α AND β SUBUNITS AND RECONSTITUTION OF A HIGH AFFINITY RECEPTOR
The functional IL-5 receptor is a heteromeric complex consisting of an α and β subunit. The cloning, sequencing and expression of guinea-pig IL-5Rα and β subunits is described. The guinea-pig IL-5Rα subunit cDNA encodes a protein of Mr47kDa, which is 72 and 66% homologous to the human and murine ort...
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| Veröffentlicht in: | Cytokine (Philadelphia, Pa.) Pa.), 2000-07, Vol.12 (7), p.858-866 |
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| creator | Scott, Clay W Logsdon, Naomi J. Wilkins, Deidre E. Norris, Tyrrell E. Sobotka-Briner, Cindy Hubbs, Stephen Graham, Alexander |
| description | The functional IL-5 receptor is a heteromeric complex consisting of an α and β subunit. The cloning, sequencing and expression of guinea-pig IL-5Rα and β subunits is described. The guinea-pig IL-5Rα subunit cDNA encodes a protein of Mr47kDa, which is 72 and 66% homologous to the human and murine orthologs, respectively. Three guinea-pig IL-5Rβ subunit cDNA clones were isolated, which differ in the N-terminus and are 56–64% homologous to the human and murine IL-5Rβ subunits. Expressing human IL-5Rαβ and guinea-pig IL-5Rαβ1in the baculovirus-insect cell system resulted in recombinant receptors which bound hIL-5 with high affinity (Kd=0.19 and 0.11nM, respectively). Expressing just gpIL-5Rα was not sufficient to demonstrate binding. This contrasts with the human receptor, where hIL-5Rα alone can bind hIL-5 with high affinity. gpIL-5Rαβ1bound both hIL-5 and mIL-5 with comparable affinity (Ki=0.10 and 0.06nM), similar to that seen with hIL-5Rαβ. Thus, both the heteromeric hIL-5R and gpIL-5Rαβ1can bind multiple IL-5 orthologs with high affinity whereas the murine IL-5R is selective for the murine ligand. |
| doi_str_mv | 10.1006/cyto.1999.0657 |
| format | Article |
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The cloning, sequencing and expression of guinea-pig IL-5Rα and β subunits is described. The guinea-pig IL-5Rα subunit cDNA encodes a protein of Mr47kDa, which is 72 and 66% homologous to the human and murine orthologs, respectively. Three guinea-pig IL-5Rβ subunit cDNA clones were isolated, which differ in the N-terminus and are 56–64% homologous to the human and murine IL-5Rβ subunits. Expressing human IL-5Rαβ and guinea-pig IL-5Rαβ1in the baculovirus-insect cell system resulted in recombinant receptors which bound hIL-5 with high affinity (Kd=0.19 and 0.11nM, respectively). Expressing just gpIL-5Rα was not sufficient to demonstrate binding. This contrasts with the human receptor, where hIL-5Rα alone can bind hIL-5 with high affinity. gpIL-5Rαβ1bound both hIL-5 and mIL-5 with comparable affinity (Ki=0.10 and 0.06nM), similar to that seen with hIL-5Rαβ. Thus, both the heteromeric hIL-5R and gpIL-5Rαβ1can bind multiple IL-5 orthologs with high affinity whereas the murine IL-5R is selective for the murine ligand.</description><identifier>ISSN: 1043-4666</identifier><identifier>EISSN: 1096-0023</identifier><identifier>DOI: 10.1006/cyto.1999.0657</identifier><identifier>PMID: 10880229</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Amino Acid Sequence ; Animals ; Cell Line ; Cloning, Molecular ; cytokine/eosinophil/guinea-pig/interleukin 5/IL-5R ; Gene Expression ; Guinea Pigs ; Humans ; Interleukin-5 - metabolism ; Molecular Sequence Data ; Protein Binding ; Protein Isoforms - genetics ; Protein Isoforms - metabolism ; Receptors, Interleukin - genetics ; Receptors, Interleukin - metabolism ; Receptors, Interleukin-5 ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Sequence Analysis, DNA ; Spodoptera - cytology</subject><ispartof>Cytokine (Philadelphia, Pa.), 2000-07, Vol.12 (7), p.858-866</ispartof><rights>2000 Academic Press</rights><rights>Copyright 2000 Academic Press.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c340t-bfca1e8e5b9b8ddc228bdb6a57ef11ea9d68c147d2baa008b6b8ff1a2b4d7a8d3</citedby><cites>FETCH-LOGICAL-c340t-bfca1e8e5b9b8ddc228bdb6a57ef11ea9d68c147d2baa008b6b8ff1a2b4d7a8d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/cyto.1999.0657$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27929,27930,46000</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10880229$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Scott, Clay W</creatorcontrib><creatorcontrib>Logsdon, Naomi J.</creatorcontrib><creatorcontrib>Wilkins, Deidre E.</creatorcontrib><creatorcontrib>Norris, Tyrrell E.</creatorcontrib><creatorcontrib>Sobotka-Briner, Cindy</creatorcontrib><creatorcontrib>Hubbs, Stephen</creatorcontrib><creatorcontrib>Graham, Alexander</creatorcontrib><title>MOLECULAR CLONING OF THE GUINEA-PIG IL-5 RECEPTOR α AND β SUBUNITS AND RECONSTITUTION OF A HIGH AFFINITY RECEPTOR</title><title>Cytokine (Philadelphia, Pa.)</title><addtitle>Cytokine</addtitle><description>The functional IL-5 receptor is a heteromeric complex consisting of an α and β subunit. The cloning, sequencing and expression of guinea-pig IL-5Rα and β subunits is described. The guinea-pig IL-5Rα subunit cDNA encodes a protein of Mr47kDa, which is 72 and 66% homologous to the human and murine orthologs, respectively. Three guinea-pig IL-5Rβ subunit cDNA clones were isolated, which differ in the N-terminus and are 56–64% homologous to the human and murine IL-5Rβ subunits. Expressing human IL-5Rαβ and guinea-pig IL-5Rαβ1in the baculovirus-insect cell system resulted in recombinant receptors which bound hIL-5 with high affinity (Kd=0.19 and 0.11nM, respectively). Expressing just gpIL-5Rα was not sufficient to demonstrate binding. This contrasts with the human receptor, where hIL-5Rα alone can bind hIL-5 with high affinity. gpIL-5Rαβ1bound both hIL-5 and mIL-5 with comparable affinity (Ki=0.10 and 0.06nM), similar to that seen with hIL-5Rαβ. Thus, both the heteromeric hIL-5R and gpIL-5Rαβ1can bind multiple IL-5 orthologs with high affinity whereas the murine IL-5R is selective for the murine ligand.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Cell Line</subject><subject>Cloning, Molecular</subject><subject>cytokine/eosinophil/guinea-pig/interleukin 5/IL-5R</subject><subject>Gene Expression</subject><subject>Guinea Pigs</subject><subject>Humans</subject><subject>Interleukin-5 - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Protein Binding</subject><subject>Protein Isoforms - genetics</subject><subject>Protein Isoforms - metabolism</subject><subject>Receptors, Interleukin - genetics</subject><subject>Receptors, Interleukin - metabolism</subject><subject>Receptors, Interleukin-5</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Sequence Analysis, DNA</subject><subject>Spodoptera - cytology</subject><issn>1043-4666</issn><issn>1096-0023</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kE1vmzAYgK1pU9Omve44-bQbmW3AmCOjhFhiECVw6MnyFxJTEjKcTOrPWn9If1OhiaZddrItP-8jvQ8AnzFaYIToN_186hc4juMFomH0AdxiFFMPIeJ_nO6B7wWU0hm4c-4nQij2o-gGzDBiDBES3wL3oyqytCmSDUyLquRlDqslrFcZzBteZom35jnkhRfCTZZm67rawNc_MCkf4esL3Dbfm5LX2_f3-F-V25rXTc2rcrIkcMXzFUyWSz5ST38N9-BTK3fOPlzPOWiWWZ2uvKLKeZoUnvYDdPJUqyW2zIYqVswYTQhTRlEZRrbF2MrYUKZxEBmipESIKapY22JJVGAiyYw_B18v3uPQ_zpbdxL7zmm728mD7c9ORJiQkAT-CC4uoB565wbbiuPQ7eXwLDASU2YxZRZTZjFlHge-XM1ntbfmH_zSdQTYBbDjfr87OwinO3vQ1nSD1Sdh-u5_7jcsooWG</recordid><startdate>20000701</startdate><enddate>20000701</enddate><creator>Scott, Clay W</creator><creator>Logsdon, Naomi J.</creator><creator>Wilkins, Deidre E.</creator><creator>Norris, Tyrrell E.</creator><creator>Sobotka-Briner, Cindy</creator><creator>Hubbs, Stephen</creator><creator>Graham, Alexander</creator><general>Elsevier Ltd</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>7X8</scope></search><sort><creationdate>20000701</creationdate><title>MOLECULAR CLONING OF THE GUINEA-PIG IL-5 RECEPTOR α AND β SUBUNITS AND RECONSTITUTION OF A HIGH AFFINITY RECEPTOR</title><author>Scott, Clay W ; Logsdon, Naomi J. ; Wilkins, Deidre E. ; Norris, Tyrrell E. ; Sobotka-Briner, Cindy ; Hubbs, Stephen ; Graham, Alexander</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c340t-bfca1e8e5b9b8ddc228bdb6a57ef11ea9d68c147d2baa008b6b8ff1a2b4d7a8d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Cell Line</topic><topic>Cloning, Molecular</topic><topic>cytokine/eosinophil/guinea-pig/interleukin 5/IL-5R</topic><topic>Gene Expression</topic><topic>Guinea Pigs</topic><topic>Humans</topic><topic>Interleukin-5 - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Protein Binding</topic><topic>Protein Isoforms - genetics</topic><topic>Protein Isoforms - metabolism</topic><topic>Receptors, Interleukin - genetics</topic><topic>Receptors, Interleukin - metabolism</topic><topic>Receptors, Interleukin-5</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Sequence Analysis, DNA</topic><topic>Spodoptera - cytology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Scott, Clay W</creatorcontrib><creatorcontrib>Logsdon, Naomi J.</creatorcontrib><creatorcontrib>Wilkins, Deidre E.</creatorcontrib><creatorcontrib>Norris, Tyrrell E.</creatorcontrib><creatorcontrib>Sobotka-Briner, Cindy</creatorcontrib><creatorcontrib>Hubbs, Stephen</creatorcontrib><creatorcontrib>Graham, Alexander</creatorcontrib><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><jtitle>Cytokine (Philadelphia, Pa.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Scott, Clay W</au><au>Logsdon, Naomi J.</au><au>Wilkins, Deidre E.</au><au>Norris, Tyrrell E.</au><au>Sobotka-Briner, Cindy</au><au>Hubbs, Stephen</au><au>Graham, Alexander</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>MOLECULAR CLONING OF THE GUINEA-PIG IL-5 RECEPTOR α AND β SUBUNITS AND RECONSTITUTION OF A HIGH AFFINITY RECEPTOR</atitle><jtitle>Cytokine (Philadelphia, Pa.)</jtitle><addtitle>Cytokine</addtitle><date>2000-07-01</date><risdate>2000</risdate><volume>12</volume><issue>7</issue><spage>858</spage><epage>866</epage><pages>858-866</pages><issn>1043-4666</issn><eissn>1096-0023</eissn><abstract>The functional IL-5 receptor is a heteromeric complex consisting of an α and β subunit. The cloning, sequencing and expression of guinea-pig IL-5Rα and β subunits is described. The guinea-pig IL-5Rα subunit cDNA encodes a protein of Mr47kDa, which is 72 and 66% homologous to the human and murine orthologs, respectively. Three guinea-pig IL-5Rβ subunit cDNA clones were isolated, which differ in the N-terminus and are 56–64% homologous to the human and murine IL-5Rβ subunits. Expressing human IL-5Rαβ and guinea-pig IL-5Rαβ1in the baculovirus-insect cell system resulted in recombinant receptors which bound hIL-5 with high affinity (Kd=0.19 and 0.11nM, respectively). Expressing just gpIL-5Rα was not sufficient to demonstrate binding. This contrasts with the human receptor, where hIL-5Rα alone can bind hIL-5 with high affinity. gpIL-5Rαβ1bound both hIL-5 and mIL-5 with comparable affinity (Ki=0.10 and 0.06nM), similar to that seen with hIL-5Rαβ. Thus, both the heteromeric hIL-5R and gpIL-5Rαβ1can bind multiple IL-5 orthologs with high affinity whereas the murine IL-5R is selective for the murine ligand.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>10880229</pmid><doi>10.1006/cyto.1999.0657</doi><tpages>9</tpages></addata></record> |
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| subjects | Amino Acid Sequence Animals Cell Line Cloning, Molecular cytokine/eosinophil/guinea-pig/interleukin 5/IL-5R Gene Expression Guinea Pigs Humans Interleukin-5 - metabolism Molecular Sequence Data Protein Binding Protein Isoforms - genetics Protein Isoforms - metabolism Receptors, Interleukin - genetics Receptors, Interleukin - metabolism Receptors, Interleukin-5 Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Sequence Analysis, DNA Spodoptera - cytology |
| title | MOLECULAR CLONING OF THE GUINEA-PIG IL-5 RECEPTOR α AND β SUBUNITS AND RECONSTITUTION OF A HIGH AFFINITY RECEPTOR |
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