Functional properties of antibody insulin-like growth factor fusion proteins
Genetic engineering and expression techniques have been used to produce antibody growth factor fusion proteins. Insulin-like growth factors (IGFs) 1 and 2 have been fused to mouse-human chimeric IgG3 at the end of CH1, immediately after the hinge, and at the end of CH3. Fusion heavy chains of the ex...
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| Veröffentlicht in: | The Journal of biological chemistry 1994-02, Vol.269 (7), p.4979-4985 |
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| container_title | The Journal of biological chemistry |
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| creator | SEUNG-UON SHIN FRIDEN, P MORAN, M MORRISON, S. L |
| description | Genetic engineering and expression techniques have been used to produce antibody growth factor fusion proteins. Insulin-like
growth factors (IGFs) 1 and 2 have been fused to mouse-human chimeric IgG3 at the end of CH1, immediately after the hinge,
and at the end of CH3. Fusion heavy chains of the expected molecular weight were expressed, assembled with a co-expressed
light chain, and secreted. The resulting molecules continued to bind antigen; they also bound the growth factor receptors,
albeit with decreased affinity. The molecule with IGF1 attached after CH3 (CH3-IGF1) had reduced ability to carry out complement-mediated
cytolysis. In contrast the molecule with IGF2 attached after CH3 (CH3-IGF2) showed an approximately 50-fold increase in its
ability to effect complement-mediated cytolysis and so should be an effective cytolytic agent. Both CH3-IGF1 and CH3-IGF2
bound Fc gamma RI with affinity similar to that of IgG3. The growth factor fusion proteins showed small but significant uptake
into the brain parenchyma. |
| doi_str_mv | 10.1016/S0021-9258(17)37642-1 |
| format | Article |
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growth factors (IGFs) 1 and 2 have been fused to mouse-human chimeric IgG3 at the end of CH1, immediately after the hinge,
and at the end of CH3. Fusion heavy chains of the expected molecular weight were expressed, assembled with a co-expressed
light chain, and secreted. The resulting molecules continued to bind antigen; they also bound the growth factor receptors,
albeit with decreased affinity. The molecule with IGF1 attached after CH3 (CH3-IGF1) had reduced ability to carry out complement-mediated
cytolysis. In contrast the molecule with IGF2 attached after CH3 (CH3-IGF2) showed an approximately 50-fold increase in its
ability to effect complement-mediated cytolysis and so should be an effective cytolytic agent. Both CH3-IGF1 and CH3-IGF2
bound Fc gamma RI with affinity similar to that of IgG3. The growth factor fusion proteins showed small but significant uptake
into the brain parenchyma.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(17)37642-1</identifier><identifier>PMID: 8106473</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Animals ; Binding, Competitive ; Biological and medical sciences ; Biotechnology ; Cell Line ; Complement C1q - metabolism ; Fundamental and applied biological sciences. Psychology ; Genes, Immunoglobulin ; Health. Pharmaceutical industry ; Humans ; Immunoglobulin Constant Regions - biosynthesis ; Immunoglobulin Constant Regions - metabolism ; Immunoglobulin G - biosynthesis ; Immunoglobulin G - metabolism ; Industrial applications and implications. Economical aspects ; Insulin-Like Growth Factor I - biosynthesis ; Insulin-Like Growth Factor I - metabolism ; Insulin-Like Growth Factor II - biosynthesis ; Insulin-Like Growth Factor II - metabolism ; Kinetics ; Lymphocytes - metabolism ; Other active biomolecules ; Production of active biomolecules ; Rats ; Receptor, IGF Type 1 - metabolism ; Receptor, IGF Type 2 - metabolism ; Recombinant Fusion Proteins - biosynthesis ; Recombinant Fusion Proteins - metabolism</subject><ispartof>The Journal of biological chemistry, 1994-02, Vol.269 (7), p.4979-4985</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c438t-eae332976ed4926c2ce5580c9c19c629bea11e8c31e76bc749a3e71cbdcc949f3</citedby><cites>FETCH-LOGICAL-c438t-eae332976ed4926c2ce5580c9c19c629bea11e8c31e76bc749a3e71cbdcc949f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4042245$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8106473$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>SEUNG-UON SHIN</creatorcontrib><creatorcontrib>FRIDEN, P</creatorcontrib><creatorcontrib>MORAN, M</creatorcontrib><creatorcontrib>MORRISON, S. L</creatorcontrib><title>Functional properties of antibody insulin-like growth factor fusion proteins</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Genetic engineering and expression techniques have been used to produce antibody growth factor fusion proteins. Insulin-like
growth factors (IGFs) 1 and 2 have been fused to mouse-human chimeric IgG3 at the end of CH1, immediately after the hinge,
and at the end of CH3. Fusion heavy chains of the expected molecular weight were expressed, assembled with a co-expressed
light chain, and secreted. The resulting molecules continued to bind antigen; they also bound the growth factor receptors,
albeit with decreased affinity. The molecule with IGF1 attached after CH3 (CH3-IGF1) had reduced ability to carry out complement-mediated
cytolysis. In contrast the molecule with IGF2 attached after CH3 (CH3-IGF2) showed an approximately 50-fold increase in its
ability to effect complement-mediated cytolysis and so should be an effective cytolytic agent. Both CH3-IGF1 and CH3-IGF2
bound Fc gamma RI with affinity similar to that of IgG3. The growth factor fusion proteins showed small but significant uptake
into the brain parenchyma.</description><subject>Animals</subject><subject>Binding, Competitive</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Cell Line</subject><subject>Complement C1q - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes, Immunoglobulin</subject><subject>Health. Pharmaceutical industry</subject><subject>Humans</subject><subject>Immunoglobulin Constant Regions - biosynthesis</subject><subject>Immunoglobulin Constant Regions - metabolism</subject><subject>Immunoglobulin G - biosynthesis</subject><subject>Immunoglobulin G - metabolism</subject><subject>Industrial applications and implications. Economical aspects</subject><subject>Insulin-Like Growth Factor I - biosynthesis</subject><subject>Insulin-Like Growth Factor I - metabolism</subject><subject>Insulin-Like Growth Factor II - biosynthesis</subject><subject>Insulin-Like Growth Factor II - metabolism</subject><subject>Kinetics</subject><subject>Lymphocytes - metabolism</subject><subject>Other active biomolecules</subject><subject>Production of active biomolecules</subject><subject>Rats</subject><subject>Receptor, IGF Type 1 - metabolism</subject><subject>Receptor, IGF Type 2 - metabolism</subject><subject>Recombinant Fusion Proteins - biosynthesis</subject><subject>Recombinant Fusion Proteins - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1r3DAQhkVJSDdJf0LAhFDSgxuNJEvWMYSmDSzkkBZ6E_LsOKvWa20km7D_vt4P9tq5zOF93hl4GLsC_hU46LsXzgWUVlT1LZgv0mglSvjAZsBrWcoKfp-w2RH5yM5z_sOnURbO2FkNXCsjZ2z-OPY4hNj7rlinuKY0BMpFbAvfD6GJi00R-jx2oS-78JeK1xTfh2XRehxiKtoxT9VtcaAJu2Snre8yfTrsC_br8dvPhx_l_Pn708P9vEQl66EkT1IKazQtlBUaBVJV1RwtgkUtbEMegGqUQEY3aJT1kgxgs0C0yrbygn3e350ev42UB7cKGanrfE9xzM5oWRml9H9B0JXh2pgJrPYgpphzotatU1j5tHHA3Va32-l2W5cOjNvpdjD1rg4PxmZFi2Pr4HfKbw65z-i7NvkeQz5iiishVDVh13tsGV6X7yGRa0LEJa2c0NYZp6yx8h_Fe5RT</recordid><startdate>19940218</startdate><enddate>19940218</enddate><creator>SEUNG-UON SHIN</creator><creator>FRIDEN, P</creator><creator>MORAN, M</creator><creator>MORRISON, S. 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L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c438t-eae332976ed4926c2ce5580c9c19c629bea11e8c31e76bc749a3e71cbdcc949f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Animals</topic><topic>Binding, Competitive</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Cell Line</topic><topic>Complement C1q - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes, Immunoglobulin</topic><topic>Health. Pharmaceutical industry</topic><topic>Humans</topic><topic>Immunoglobulin Constant Regions - biosynthesis</topic><topic>Immunoglobulin Constant Regions - metabolism</topic><topic>Immunoglobulin G - biosynthesis</topic><topic>Immunoglobulin G - metabolism</topic><topic>Industrial applications and implications. Economical aspects</topic><topic>Insulin-Like Growth Factor I - biosynthesis</topic><topic>Insulin-Like Growth Factor I - metabolism</topic><topic>Insulin-Like Growth Factor II - biosynthesis</topic><topic>Insulin-Like Growth Factor II - metabolism</topic><topic>Kinetics</topic><topic>Lymphocytes - metabolism</topic><topic>Other active biomolecules</topic><topic>Production of active biomolecules</topic><topic>Rats</topic><topic>Receptor, IGF Type 1 - metabolism</topic><topic>Receptor, IGF Type 2 - metabolism</topic><topic>Recombinant Fusion Proteins - biosynthesis</topic><topic>Recombinant Fusion Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>SEUNG-UON SHIN</creatorcontrib><creatorcontrib>FRIDEN, P</creatorcontrib><creatorcontrib>MORAN, M</creatorcontrib><creatorcontrib>MORRISON, S. 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L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functional properties of antibody insulin-like growth factor fusion proteins</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1994-02-18</date><risdate>1994</risdate><volume>269</volume><issue>7</issue><spage>4979</spage><epage>4985</epage><pages>4979-4985</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Genetic engineering and expression techniques have been used to produce antibody growth factor fusion proteins. Insulin-like
growth factors (IGFs) 1 and 2 have been fused to mouse-human chimeric IgG3 at the end of CH1, immediately after the hinge,
and at the end of CH3. Fusion heavy chains of the expected molecular weight were expressed, assembled with a co-expressed
light chain, and secreted. The resulting molecules continued to bind antigen; they also bound the growth factor receptors,
albeit with decreased affinity. The molecule with IGF1 attached after CH3 (CH3-IGF1) had reduced ability to carry out complement-mediated
cytolysis. In contrast the molecule with IGF2 attached after CH3 (CH3-IGF2) showed an approximately 50-fold increase in its
ability to effect complement-mediated cytolysis and so should be an effective cytolytic agent. Both CH3-IGF1 and CH3-IGF2
bound Fc gamma RI with affinity similar to that of IgG3. The growth factor fusion proteins showed small but significant uptake
into the brain parenchyma.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8106473</pmid><doi>10.1016/S0021-9258(17)37642-1</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1994-02, Vol.269 (7), p.4979-4985 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76357446 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Freely accessible e-journals; Alma/SFX Local Collection |
| subjects | Animals Binding, Competitive Biological and medical sciences Biotechnology Cell Line Complement C1q - metabolism Fundamental and applied biological sciences. Psychology Genes, Immunoglobulin Health. Pharmaceutical industry Humans Immunoglobulin Constant Regions - biosynthesis Immunoglobulin Constant Regions - metabolism Immunoglobulin G - biosynthesis Immunoglobulin G - metabolism Industrial applications and implications. Economical aspects Insulin-Like Growth Factor I - biosynthesis Insulin-Like Growth Factor I - metabolism Insulin-Like Growth Factor II - biosynthesis Insulin-Like Growth Factor II - metabolism Kinetics Lymphocytes - metabolism Other active biomolecules Production of active biomolecules Rats Receptor, IGF Type 1 - metabolism Receptor, IGF Type 2 - metabolism Recombinant Fusion Proteins - biosynthesis Recombinant Fusion Proteins - metabolism |
| title | Functional properties of antibody insulin-like growth factor fusion proteins |
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