Aggregated Human Immunoglobulins Bind to Modified Proteins
Human immunoglobulins treated at 55°C in vitro are able to interact with maleylated bovine serum albumin (mBSA), but not with unmodified BSA. Gel filtration experiments demonstrated that the mBSA binding is associated with a high molecular weight complex of aggregated IgG. This aggregated IgG with b...
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| Veröffentlicht in: | Scandinavian journal of immunology 1993-05, Vol.37 (5), p.593-601 |
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| container_title | Scandinavian journal of immunology |
| container_volume | 37 |
| creator | LÓPEZ‐BOTE, J. P. LANGA, C. LASTRES, P. RIUS, C. MARQUET, A. RAMOS‐RUIZ, R. BERNABÉU, C. |
| description | Human immunoglobulins treated at 55°C in vitro are able to interact with maleylated bovine serum albumin (mBSA), but not with unmodified BSA. Gel filtration experiments demonstrated that the mBSA binding is associated with a high molecular weight complex of aggregated IgG. This aggregated IgG with binding capacity for mBSA could also be generated in vitro by treatment of human IgG at 37°C or 40°C and by incubation with human neutrophils. Furthermore, IgG aggregates with binding activity for mBSA could be detected in untreated synovial fluids from rheumatoid arthritis patients, indicating that these complexes occur in vivo. The phenomenon of binding to aggregated IgG was extended to other modified proteins such as maleylated human serum albumin (mHSA), acetyl low density lipoprotein (Ac‐LDL) and BSA reacted with oxidized linolenic acid. Soluble forms of these modified proteins were able to compete for the interaction between aggregated IgG and surface‐bound mBSA. We also found that aggregated IgG enhanced the Ac‐LDL‐dependent foam cell formation. These findings suggest a role for aggregated IgG in the metabolism of oxidized proteins. |
| doi_str_mv | 10.1111/j.1365-3083.1993.tb02577.x |
| format | Article |
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P. ; LANGA, C. ; LASTRES, P. ; RIUS, C. ; MARQUET, A. ; RAMOS‐RUIZ, R. ; BERNABÉU, C.</creator><creatorcontrib>LÓPEZ‐BOTE, J. P. ; LANGA, C. ; LASTRES, P. ; RIUS, C. ; MARQUET, A. ; RAMOS‐RUIZ, R. ; BERNABÉU, C.</creatorcontrib><description>Human immunoglobulins treated at 55°C in vitro are able to interact with maleylated bovine serum albumin (mBSA), but not with unmodified BSA. Gel filtration experiments demonstrated that the mBSA binding is associated with a high molecular weight complex of aggregated IgG. This aggregated IgG with binding capacity for mBSA could also be generated in vitro by treatment of human IgG at 37°C or 40°C and by incubation with human neutrophils. Furthermore, IgG aggregates with binding activity for mBSA could be detected in untreated synovial fluids from rheumatoid arthritis patients, indicating that these complexes occur in vivo. The phenomenon of binding to aggregated IgG was extended to other modified proteins such as maleylated human serum albumin (mHSA), acetyl low density lipoprotein (Ac‐LDL) and BSA reacted with oxidized linolenic acid. Soluble forms of these modified proteins were able to compete for the interaction between aggregated IgG and surface‐bound mBSA. We also found that aggregated IgG enhanced the Ac‐LDL‐dependent foam cell formation. These findings suggest a role for aggregated IgG in the metabolism of oxidized proteins.</description><identifier>ISSN: 0300-9475</identifier><identifier>EISSN: 1365-3083</identifier><identifier>DOI: 10.1111/j.1365-3083.1993.tb02577.x</identifier><identifier>PMID: 8484105</identifier><identifier>CODEN: SJIMAX</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Animals ; Antigen-antibody reactions, antigen-antibody complexes, antibody-complement and others. Study of affinity. Antigen presentation ; Arthritis, Rheumatoid - immunology ; Biological and medical sciences ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; Granulocytes - immunology ; Hot Temperature ; Humans ; Immune Sera - immunology ; Immunoglobulin Fab Fragments - chemistry ; Immunoglobulin Fab Fragments - metabolism ; Immunoglobulin G - chemistry ; Immunoglobulin G - metabolism ; Lipoproteins, LDL - chemistry ; Lipoproteins, LDL - metabolism ; Macrophages - metabolism ; Molecular immunology ; Oxidation-Reduction ; Rats ; Serum Albumin - chemistry ; Serum Albumin - metabolism ; Serum Albumin, Bovine - chemistry ; Serum Albumin, Bovine - metabolism ; Synovial Fluid - immunology</subject><ispartof>Scandinavian journal of immunology, 1993-05, Vol.37 (5), p.593-601</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4293-f90b77aed44f9ebd4b4211d6bc3ec9a1210c448979571326cb23d5cc4569f8ca3</citedby><cites>FETCH-LOGICAL-c4293-f90b77aed44f9ebd4b4211d6bc3ec9a1210c448979571326cb23d5cc4569f8ca3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1365-3083.1993.tb02577.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1365-3083.1993.tb02577.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4780469$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8484105$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>LÓPEZ‐BOTE, J. P.</creatorcontrib><creatorcontrib>LANGA, C.</creatorcontrib><creatorcontrib>LASTRES, P.</creatorcontrib><creatorcontrib>RIUS, C.</creatorcontrib><creatorcontrib>MARQUET, A.</creatorcontrib><creatorcontrib>RAMOS‐RUIZ, R.</creatorcontrib><creatorcontrib>BERNABÉU, C.</creatorcontrib><title>Aggregated Human Immunoglobulins Bind to Modified Proteins</title><title>Scandinavian journal of immunology</title><addtitle>Scand J Immunol</addtitle><description>Human immunoglobulins treated at 55°C in vitro are able to interact with maleylated bovine serum albumin (mBSA), but not with unmodified BSA. Gel filtration experiments demonstrated that the mBSA binding is associated with a high molecular weight complex of aggregated IgG. This aggregated IgG with binding capacity for mBSA could also be generated in vitro by treatment of human IgG at 37°C or 40°C and by incubation with human neutrophils. Furthermore, IgG aggregates with binding activity for mBSA could be detected in untreated synovial fluids from rheumatoid arthritis patients, indicating that these complexes occur in vivo. The phenomenon of binding to aggregated IgG was extended to other modified proteins such as maleylated human serum albumin (mHSA), acetyl low density lipoprotein (Ac‐LDL) and BSA reacted with oxidized linolenic acid. Soluble forms of these modified proteins were able to compete for the interaction between aggregated IgG and surface‐bound mBSA. We also found that aggregated IgG enhanced the Ac‐LDL‐dependent foam cell formation. These findings suggest a role for aggregated IgG in the metabolism of oxidized proteins.</description><subject>Animals</subject><subject>Antigen-antibody reactions, antigen-antibody complexes, antibody-complement and others. Study of affinity. Antigen presentation</subject><subject>Arthritis, Rheumatoid - immunology</subject><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>Granulocytes - immunology</subject><subject>Hot Temperature</subject><subject>Humans</subject><subject>Immune Sera - immunology</subject><subject>Immunoglobulin Fab Fragments - chemistry</subject><subject>Immunoglobulin Fab Fragments - metabolism</subject><subject>Immunoglobulin G - chemistry</subject><subject>Immunoglobulin G - metabolism</subject><subject>Lipoproteins, LDL - chemistry</subject><subject>Lipoproteins, LDL - metabolism</subject><subject>Macrophages - metabolism</subject><subject>Molecular immunology</subject><subject>Oxidation-Reduction</subject><subject>Rats</subject><subject>Serum Albumin - chemistry</subject><subject>Serum Albumin - metabolism</subject><subject>Serum Albumin, Bovine - chemistry</subject><subject>Serum Albumin, Bovine - metabolism</subject><subject>Synovial Fluid - immunology</subject><issn>0300-9475</issn><issn>1365-3083</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkF1LwzAUhoMoc05_glBEvGtNmqRpdiHM4cdkoqBehzRNR0fbzKTF7d-bsrJbMTfn4n3ek8MDwBWCEfLvdh0hnNAQwxRHiHMctRmMKWPR9giMD9ExGEMMYcgJo6fgzLk1hAjHDI_AKCUpQZCOwXS2Wlm9kq3Og-eulk2wqOuuMavKZF1VNi64L5s8aE3wavKyKD32bk2rfXIOTgpZOX0xzAn4enz4nD-Hy7enxXy2DBWJOQ4LDjPGpM4JKbjOcpKRGKE8yRTWiksUI6gISTnjlPnzEpXFOKdKEZrwIlUST8DNfu_Gmu9Ou1bUpVO6qmSjTecE870YEvgniBLC4ySlHpzuQWWNc1YXYmPLWtqdQFD0hsVa9BpFr1H0hsVgWGx9-XL4pctqnR-qg1KfXw-5dEpWhZWNKt0BIyyFJOEeu9tjP2Wld_84QHy8LCjH-BfMt5cO</recordid><startdate>199305</startdate><enddate>199305</enddate><creator>LÓPEZ‐BOTE, J. P.</creator><creator>LANGA, C.</creator><creator>LASTRES, P.</creator><creator>RIUS, C.</creator><creator>MARQUET, A.</creator><creator>RAMOS‐RUIZ, R.</creator><creator>BERNABÉU, C.</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</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>7T5</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>199305</creationdate><title>Aggregated Human Immunoglobulins Bind to Modified Proteins</title><author>LÓPEZ‐BOTE, J. P. ; LANGA, C. ; LASTRES, P. ; RIUS, C. ; MARQUET, A. ; RAMOS‐RUIZ, R. ; BERNABÉU, C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4293-f90b77aed44f9ebd4b4211d6bc3ec9a1210c448979571326cb23d5cc4569f8ca3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Animals</topic><topic>Antigen-antibody reactions, antigen-antibody complexes, antibody-complement and others. Study of affinity. Antigen presentation</topic><topic>Arthritis, Rheumatoid - immunology</topic><topic>Biological and medical sciences</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>Granulocytes - immunology</topic><topic>Hot Temperature</topic><topic>Humans</topic><topic>Immune Sera - immunology</topic><topic>Immunoglobulin Fab Fragments - chemistry</topic><topic>Immunoglobulin Fab Fragments - metabolism</topic><topic>Immunoglobulin G - chemistry</topic><topic>Immunoglobulin G - metabolism</topic><topic>Lipoproteins, LDL - chemistry</topic><topic>Lipoproteins, LDL - metabolism</topic><topic>Macrophages - metabolism</topic><topic>Molecular immunology</topic><topic>Oxidation-Reduction</topic><topic>Rats</topic><topic>Serum Albumin - chemistry</topic><topic>Serum Albumin - metabolism</topic><topic>Serum Albumin, Bovine - chemistry</topic><topic>Serum Albumin, Bovine - metabolism</topic><topic>Synovial Fluid - immunology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>LÓPEZ‐BOTE, J. P.</creatorcontrib><creatorcontrib>LANGA, C.</creatorcontrib><creatorcontrib>LASTRES, P.</creatorcontrib><creatorcontrib>RIUS, C.</creatorcontrib><creatorcontrib>MARQUET, A.</creatorcontrib><creatorcontrib>RAMOS‐RUIZ, R.</creatorcontrib><creatorcontrib>BERNABÉU, C.</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>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Scandinavian journal of immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>LÓPEZ‐BOTE, J. P.</au><au>LANGA, C.</au><au>LASTRES, P.</au><au>RIUS, C.</au><au>MARQUET, A.</au><au>RAMOS‐RUIZ, R.</au><au>BERNABÉU, C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Aggregated Human Immunoglobulins Bind to Modified Proteins</atitle><jtitle>Scandinavian journal of immunology</jtitle><addtitle>Scand J Immunol</addtitle><date>1993-05</date><risdate>1993</risdate><volume>37</volume><issue>5</issue><spage>593</spage><epage>601</epage><pages>593-601</pages><issn>0300-9475</issn><eissn>1365-3083</eissn><coden>SJIMAX</coden><abstract>Human immunoglobulins treated at 55°C in vitro are able to interact with maleylated bovine serum albumin (mBSA), but not with unmodified BSA. Gel filtration experiments demonstrated that the mBSA binding is associated with a high molecular weight complex of aggregated IgG. This aggregated IgG with binding capacity for mBSA could also be generated in vitro by treatment of human IgG at 37°C or 40°C and by incubation with human neutrophils. Furthermore, IgG aggregates with binding activity for mBSA could be detected in untreated synovial fluids from rheumatoid arthritis patients, indicating that these complexes occur in vivo. The phenomenon of binding to aggregated IgG was extended to other modified proteins such as maleylated human serum albumin (mHSA), acetyl low density lipoprotein (Ac‐LDL) and BSA reacted with oxidized linolenic acid. Soluble forms of these modified proteins were able to compete for the interaction between aggregated IgG and surface‐bound mBSA. We also found that aggregated IgG enhanced the Ac‐LDL‐dependent foam cell formation. These findings suggest a role for aggregated IgG in the metabolism of oxidized proteins.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>8484105</pmid><doi>10.1111/j.1365-3083.1993.tb02577.x</doi><tpages>9</tpages></addata></record> |
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| ispartof | Scandinavian journal of immunology, 1993-05, Vol.37 (5), p.593-601 |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Animals Antigen-antibody reactions, antigen-antibody complexes, antibody-complement and others. Study of affinity. Antigen presentation Arthritis, Rheumatoid - immunology Biological and medical sciences Fundamental and applied biological sciences. Psychology Fundamental immunology Granulocytes - immunology Hot Temperature Humans Immune Sera - immunology Immunoglobulin Fab Fragments - chemistry Immunoglobulin Fab Fragments - metabolism Immunoglobulin G - chemistry Immunoglobulin G - metabolism Lipoproteins, LDL - chemistry Lipoproteins, LDL - metabolism Macrophages - metabolism Molecular immunology Oxidation-Reduction Rats Serum Albumin - chemistry Serum Albumin - metabolism Serum Albumin, Bovine - chemistry Serum Albumin, Bovine - metabolism Synovial Fluid - immunology |
| title | Aggregated Human Immunoglobulins Bind to Modified Proteins |
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