CH3 domain of IgG as binding site to Fc receptor on mouse lymphocytes
MEMBRANE receptors recognising the Fc portion of immunoglobulin molecules (Fc receptors) are found in many cells of the immune system 1–4 . Fc receptors on lymphocytes are readily detected by a rosette test 3,5,6 and this reaction is inhibited by pretreatment of the lymphocytes with IgG (ref. 3). Ig...
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Veröffentlicht in: | Nature (London) 1975-02, Vol.253 (5493), p.656-656 |
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creator | RAMASAMY, RANJAN SECHER, DAVID S. ADETUGBO, KAYODE |
description | MEMBRANE receptors recognising the Fc portion of immunoglobulin molecules (Fc receptors) are found in many cells of the immune system
1–4
. Fc receptors on lymphocytes are readily detected by a rosette test
3,5,6
and this reaction is inhibited by pretreatment of the lymphocytes with IgG (ref. 3). IgG proteins lacking almost the entire C
H
1 and C
H
3 homology regions have been obtained from mutant cell lines of MOPC 21, a plasmacytoma secreting IgG1 (refs 7 and 8) and the extent of the deletions determined (Fig. 1). To identify that part of the IgG molecule which interacts with the Fc receptor, we have tested the ability of these IgG proteins to inhibit Fc rosette formation on murine lymph node cells. We show (Table 1) that an intact C
H
3 region is essential for the binding of IgG to Fc receptors on lymph node cells. |
doi_str_mv | 10.1038/253656a0 |
format | Article |
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1–4
. Fc receptors on lymphocytes are readily detected by a rosette test
3,5,6
and this reaction is inhibited by pretreatment of the lymphocytes with IgG (ref. 3). IgG proteins lacking almost the entire C
H
1 and C
H
3 homology regions have been obtained from mutant cell lines of MOPC 21, a plasmacytoma secreting IgG1 (refs 7 and 8) and the extent of the deletions determined (Fig. 1). To identify that part of the IgG molecule which interacts with the Fc receptor, we have tested the ability of these IgG proteins to inhibit Fc rosette formation on murine lymph node cells. We show (Table 1) that an intact C
H
3 region is essential for the binding of IgG to Fc receptors on lymph node cells.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/253656a0</identifier><identifier>PMID: 1089902</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Animals ; Binding Sites, Antibody ; Cell Line ; Hemolytic Plaque Technique ; Humanities and Social Sciences ; Immunoglobulin Fc Fragments ; Immunoglobulin G ; letter ; Lymphocytes - immunology ; Mice ; multidisciplinary ; Plasmacytoma ; Science</subject><ispartof>Nature (London), 1975-02, Vol.253 (5493), p.656-656</ispartof><rights>Springer Nature Limited 1975</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c346t-72d76b231f7c5f1bea57df10949f7a6cb5bc4125e45d69a0116f2d9fb025ea4f3</citedby><cites>FETCH-LOGICAL-c346t-72d76b231f7c5f1bea57df10949f7a6cb5bc4125e45d69a0116f2d9fb025ea4f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/253656a0$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/253656a0$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1089902$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>RAMASAMY, RANJAN</creatorcontrib><creatorcontrib>SECHER, DAVID S.</creatorcontrib><creatorcontrib>ADETUGBO, KAYODE</creatorcontrib><title>CH3 domain of IgG as binding site to Fc receptor on mouse lymphocytes</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>MEMBRANE receptors recognising the Fc portion of immunoglobulin molecules (Fc receptors) are found in many cells of the immune system
1–4
. Fc receptors on lymphocytes are readily detected by a rosette test
3,5,6
and this reaction is inhibited by pretreatment of the lymphocytes with IgG (ref. 3). IgG proteins lacking almost the entire C
H
1 and C
H
3 homology regions have been obtained from mutant cell lines of MOPC 21, a plasmacytoma secreting IgG1 (refs 7 and 8) and the extent of the deletions determined (Fig. 1). To identify that part of the IgG molecule which interacts with the Fc receptor, we have tested the ability of these IgG proteins to inhibit Fc rosette formation on murine lymph node cells. We show (Table 1) that an intact C
H
3 region is essential for the binding of IgG to Fc receptors on lymph node cells.</description><subject>Animals</subject><subject>Binding Sites, Antibody</subject><subject>Cell Line</subject><subject>Hemolytic Plaque Technique</subject><subject>Humanities and Social Sciences</subject><subject>Immunoglobulin Fc Fragments</subject><subject>Immunoglobulin G</subject><subject>letter</subject><subject>Lymphocytes - immunology</subject><subject>Mice</subject><subject>multidisciplinary</subject><subject>Plasmacytoma</subject><subject>Science</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1975</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNplkE1LxDAQhoMo67oK_gEhJ9FDdZLmoznKsl-w4EXPJU2TtUvb1KQ97L-3uisIngbmfXiZeRC6JfBEIM2eKU8FFxrO0JQwKRImMnmOpgA0SyBLxSW6inEPAJxINkETAplSQKdoMV-nuPSNrlrsHd7sVlhHXFRtWbU7HKve4t7jpcHBGtv1PmDf4sYP0eL60HQf3hx6G6_RhdN1tDenOUPvy8XbfJ1sX1eb-cs2MSkTfSJpKUVBU-Kk4Y4UVnNZOgKKKSe1MAUvDCOUW8ZLoTQQIhwtlStg3Gnm0hm6P_Z2wX8ONvZ5U0Vj61q3drwpz6ikiio5gg9H0AQfY7Au70LV6HDICeTfxvJfYyN6d-ocisaWf8AfRWP-eMzjmLQ7G_K9H0I7vvm_6wsstHF4</recordid><startdate>19750220</startdate><enddate>19750220</enddate><creator>RAMASAMY, RANJAN</creator><creator>SECHER, DAVID S.</creator><creator>ADETUGBO, KAYODE</creator><general>Nature Publishing Group UK</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>19750220</creationdate><title>CH3 domain of IgG as binding site to Fc receptor on mouse lymphocytes</title><author>RAMASAMY, RANJAN ; SECHER, DAVID S. ; ADETUGBO, KAYODE</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c346t-72d76b231f7c5f1bea57df10949f7a6cb5bc4125e45d69a0116f2d9fb025ea4f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1975</creationdate><topic>Animals</topic><topic>Binding Sites, Antibody</topic><topic>Cell Line</topic><topic>Hemolytic Plaque Technique</topic><topic>Humanities and Social Sciences</topic><topic>Immunoglobulin Fc Fragments</topic><topic>Immunoglobulin G</topic><topic>letter</topic><topic>Lymphocytes - immunology</topic><topic>Mice</topic><topic>multidisciplinary</topic><topic>Plasmacytoma</topic><topic>Science</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>RAMASAMY, RANJAN</creatorcontrib><creatorcontrib>SECHER, DAVID S.</creatorcontrib><creatorcontrib>ADETUGBO, KAYODE</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>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>RAMASAMY, RANJAN</au><au>SECHER, DAVID S.</au><au>ADETUGBO, KAYODE</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>CH3 domain of IgG as binding site to Fc receptor on mouse lymphocytes</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>1975-02-20</date><risdate>1975</risdate><volume>253</volume><issue>5493</issue><spage>656</spage><epage>656</epage><pages>656-656</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><abstract>MEMBRANE receptors recognising the Fc portion of immunoglobulin molecules (Fc receptors) are found in many cells of the immune system
1–4
. Fc receptors on lymphocytes are readily detected by a rosette test
3,5,6
and this reaction is inhibited by pretreatment of the lymphocytes with IgG (ref. 3). IgG proteins lacking almost the entire C
H
1 and C
H
3 homology regions have been obtained from mutant cell lines of MOPC 21, a plasmacytoma secreting IgG1 (refs 7 and 8) and the extent of the deletions determined (Fig. 1). To identify that part of the IgG molecule which interacts with the Fc receptor, we have tested the ability of these IgG proteins to inhibit Fc rosette formation on murine lymph node cells. We show (Table 1) that an intact C
H
3 region is essential for the binding of IgG to Fc receptors on lymph node cells.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>1089902</pmid><doi>10.1038/253656a0</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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language | eng |
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source | MEDLINE; Springer Nature - Complete Springer Journals; Nature Journals Online |
subjects | Animals Binding Sites, Antibody Cell Line Hemolytic Plaque Technique Humanities and Social Sciences Immunoglobulin Fc Fragments Immunoglobulin G letter Lymphocytes - immunology Mice multidisciplinary Plasmacytoma Science |
title | CH3 domain of IgG as binding site to Fc receptor on mouse lymphocytes |
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