Structure-function analysis of interleukin-6 utilizing human/murine chimeric molecules. Involvement of two separate domains in receptor binding
As an approach to understanding the interaction of interleukin-6 (IL-6) and its 80-kDa receptor (gp80), we have constructed chimeric human/murine IL-6-molecules, which were expressed in Escherichia coli and analyzed for biological activity and receptor binding. This experimental strategy was based o...
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| Veröffentlicht in: | The Journal of biological chemistry 1993-07, Vol.268 (20), p.15285-15290 |
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| container_issue | 20 |
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| container_title | The Journal of biological chemistry |
| container_volume | 268 |
| creator | VAN DAM, M MÜLLBERG, J SCHOOLTINK, H STOYAN, T BRAKENHOFF, J. P. J GRAEVE, L HEINRICH, P. C ROSE-JOHN, S |
| description | As an approach to understanding the interaction of interleukin-6 (IL-6) and its 80-kDa receptor (gp80), we have constructed
chimeric human/murine IL-6-molecules, which were expressed in Escherichia coli and analyzed for biological activity and receptor
binding. This experimental strategy was based on the observation that human IL-6 acts on human and murine cells, whereas murine
IL-6 stimulates only murine cells. The regions to be exchanged were chosen according to the four antiparallel helix model
of the hematopoietic cytokine family. All 14 chimeras constructed showed biological activity on murine cells. From the differential
biological activities on human cells we deduced that three out of four domains of IL-6 are involved in species specificity,
whereas only two domains are necessary for specific recognition by the gp80 IL-6-receptor protein. |
| doi_str_mv | 10.1016/s0021-9258(18)82467-x |
| format | Article |
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chimeric human/murine IL-6-molecules, which were expressed in Escherichia coli and analyzed for biological activity and receptor
binding. This experimental strategy was based on the observation that human IL-6 acts on human and murine cells, whereas murine
IL-6 stimulates only murine cells. The regions to be exchanged were chosen according to the four antiparallel helix model
of the hematopoietic cytokine family. All 14 chimeras constructed showed biological activity on murine cells. From the differential
biological activities on human cells we deduced that three out of four domains of IL-6 are involved in species specificity,
whereas only two domains are necessary for specific recognition by the gp80 IL-6-receptor protein.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/s0021-9258(18)82467-x</identifier><identifier>PMID: 8325898</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Analysis of the immune response. Humoral and cellular immunity ; Animals ; Base Sequence ; Binding Sites ; Biological and medical sciences ; Cloning, Molecular ; DNA ; Escherichia coli ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; Humans ; Immunobiology ; Interleukin-6 - genetics ; Interleukin-6 - metabolism ; Lymphokines, interleukins ( function, expression) ; Mice ; Molecular Sequence Data ; Receptors, Immunologic - metabolism ; Receptors, Interleukin-6 ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Regulatory factors and their cellular receptors ; Structure-Activity Relationship ; Tumor Cells, Cultured</subject><ispartof>The Journal of biological chemistry, 1993-07, Vol.268 (20), p.15285-15290</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c390x-9de7f723a05dd0f2e9fc5078c3c039629a8859e7eb75d730e2fe1d82f3ab99973</citedby><cites>FETCH-LOGICAL-c390x-9de7f723a05dd0f2e9fc5078c3c039629a8859e7eb75d730e2fe1d82f3ab99973</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27922,27923</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4848010$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8325898$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>VAN DAM, M</creatorcontrib><creatorcontrib>MÜLLBERG, J</creatorcontrib><creatorcontrib>SCHOOLTINK, H</creatorcontrib><creatorcontrib>STOYAN, T</creatorcontrib><creatorcontrib>BRAKENHOFF, J. P. J</creatorcontrib><creatorcontrib>GRAEVE, L</creatorcontrib><creatorcontrib>HEINRICH, P. C</creatorcontrib><creatorcontrib>ROSE-JOHN, S</creatorcontrib><title>Structure-function analysis of interleukin-6 utilizing human/murine chimeric molecules. Involvement of two separate domains in receptor binding</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>As an approach to understanding the interaction of interleukin-6 (IL-6) and its 80-kDa receptor (gp80), we have constructed
chimeric human/murine IL-6-molecules, which were expressed in Escherichia coli and analyzed for biological activity and receptor
binding. This experimental strategy was based on the observation that human IL-6 acts on human and murine cells, whereas murine
IL-6 stimulates only murine cells. The regions to be exchanged were chosen according to the four antiparallel helix model
of the hematopoietic cytokine family. All 14 chimeras constructed showed biological activity on murine cells. From the differential
biological activities on human cells we deduced that three out of four domains of IL-6 are involved in species specificity,
whereas only two domains are necessary for specific recognition by the gp80 IL-6-receptor protein.</description><subject>Analysis of the immune response. Humoral and cellular immunity</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Cloning, Molecular</subject><subject>DNA</subject><subject>Escherichia coli</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>Humans</subject><subject>Immunobiology</subject><subject>Interleukin-6 - genetics</subject><subject>Interleukin-6 - metabolism</subject><subject>Lymphokines, interleukins ( function, expression)</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Receptors, Immunologic - metabolism</subject><subject>Receptors, Interleukin-6</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Regulatory factors and their cellular receptors</subject><subject>Structure-Activity Relationship</subject><subject>Tumor Cells, Cultured</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkctuFDEQRS0ECkPgEyJ5gRAsOvFj3G0vURQgUiQWASk7y-0uZwx-DHY7D36CX6aHjIbalFR16lbpFkInlJxSQvuzSgijnWJCvqfyg2TrfugenqEVJZJ3XNCb52h1QF6iV7X-IEusFT1CR5IvRSVX6M_1XJqdW4HOtWRnnxM2yYTH6ivODvs0QwnQfvrU9bjNPvjfPt3iTYsmncVWfAJsNz5C8RbHHMC2APUUX6a7HO4gQpp3OvN9xhW2ppgZ8JSj8aku4riAhe2cCx59mhbh1-iFM6HCm30-Rt8_XXw7_9Jdff18ef7xqrNckYdOTTC4gXFDxDQRx0A5K8ggLbeEq54pI6VQMMA4iGngBJgDOknmuBmVUgM_Ru-edLcl_2pQZx19tRCCSZBb1YOQXCreL6B4Am3JtRZwelt8NOVRU6J3j9DXO5f1zmVNpf73CH2zzJ3sF7QxwnSY2ju_9N_u-6ZaE1wxyfp6wNZyLQkl_7GNv93c-wJ69NluIGrWS82WEwSTgv8F39-g7Q</recordid><startdate>19930715</startdate><enddate>19930715</enddate><creator>VAN DAM, M</creator><creator>MÜLLBERG, J</creator><creator>SCHOOLTINK, H</creator><creator>STOYAN, T</creator><creator>BRAKENHOFF, J. P. J</creator><creator>GRAEVE, L</creator><creator>HEINRICH, P. C</creator><creator>ROSE-JOHN, S</creator><general>American Society for Biochemistry and Molecular Biology</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></search><sort><creationdate>19930715</creationdate><title>Structure-function analysis of interleukin-6 utilizing human/murine chimeric molecules. Involvement of two separate domains in receptor binding</title><author>VAN DAM, M ; MÜLLBERG, J ; SCHOOLTINK, H ; STOYAN, T ; BRAKENHOFF, J. P. J ; GRAEVE, L ; HEINRICH, P. C ; ROSE-JOHN, S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c390x-9de7f723a05dd0f2e9fc5078c3c039629a8859e7eb75d730e2fe1d82f3ab99973</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Analysis of the immune response. Humoral and cellular immunity</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Cloning, Molecular</topic><topic>DNA</topic><topic>Escherichia coli</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>Humans</topic><topic>Immunobiology</topic><topic>Interleukin-6 - genetics</topic><topic>Interleukin-6 - metabolism</topic><topic>Lymphokines, interleukins ( function, expression)</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Receptors, Immunologic - metabolism</topic><topic>Receptors, Interleukin-6</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Regulatory factors and their cellular receptors</topic><topic>Structure-Activity Relationship</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>VAN DAM, M</creatorcontrib><creatorcontrib>MÜLLBERG, J</creatorcontrib><creatorcontrib>SCHOOLTINK, H</creatorcontrib><creatorcontrib>STOYAN, T</creatorcontrib><creatorcontrib>BRAKENHOFF, J. P. 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Involvement of two separate domains in receptor binding</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1993-07-15</date><risdate>1993</risdate><volume>268</volume><issue>20</issue><spage>15285</spage><epage>15290</epage><pages>15285-15290</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>As an approach to understanding the interaction of interleukin-6 (IL-6) and its 80-kDa receptor (gp80), we have constructed
chimeric human/murine IL-6-molecules, which were expressed in Escherichia coli and analyzed for biological activity and receptor
binding. This experimental strategy was based on the observation that human IL-6 acts on human and murine cells, whereas murine
IL-6 stimulates only murine cells. The regions to be exchanged were chosen according to the four antiparallel helix model
of the hematopoietic cytokine family. All 14 chimeras constructed showed biological activity on murine cells. From the differential
biological activities on human cells we deduced that three out of four domains of IL-6 are involved in species specificity,
whereas only two domains are necessary for specific recognition by the gp80 IL-6-receptor protein.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8325898</pmid><doi>10.1016/s0021-9258(18)82467-x</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1993-07, Vol.268 (20), p.15285-15290 |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Analysis of the immune response. Humoral and cellular immunity Animals Base Sequence Binding Sites Biological and medical sciences Cloning, Molecular DNA Escherichia coli Fundamental and applied biological sciences. Psychology Fundamental immunology Humans Immunobiology Interleukin-6 - genetics Interleukin-6 - metabolism Lymphokines, interleukins ( function, expression) Mice Molecular Sequence Data Receptors, Immunologic - metabolism Receptors, Interleukin-6 Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Regulatory factors and their cellular receptors Structure-Activity Relationship Tumor Cells, Cultured |
| title | Structure-function analysis of interleukin-6 utilizing human/murine chimeric molecules. Involvement of two separate domains in receptor binding |
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