Activation of cryptic IgG reactive with BAFF, amyloid beta peptide and GM-CSF during the industrial fractionation of human plasma into therapeutic intravenous immunoglobulins
Abstract The mechanisms of therapeutic action of IVIg are still unclear in most autoimmune and inflammatory diseases. IVIg have been shown to bind to a variety of human proteins including BAFF, amyloid beta peptide and GM-CSF. It has been suggested that this autoreactivity could contribute to the th...
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| Veröffentlicht in: | Clinical immunology (Orlando, Fla.) Fla.), 2009-10, Vol.133 (1), p.52-60 |
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| creator | St-Amour, Isabelle Laroche, André Bazin, Renée Lemieux, Réal |
| description | Abstract The mechanisms of therapeutic action of IVIg are still unclear in most autoimmune and inflammatory diseases. IVIg have been shown to bind to a variety of human proteins including BAFF, amyloid beta peptide and GM-CSF. It has been suggested that this autoreactivity could contribute to the therapeutic immunomodulatory effects of IVIg. In this work, we showed that native IgG purified from plasma under non-denaturing conditions were much less autoreactive than IVIg. However the native IgG autoreactivity with BAFF, amyloid beta peptide and GM-CSF was significantly increased by short incubation under the slightly denaturing conditions used during industrial plasma fractionation. We conclude that the relatively mild conditions used in industrial plasma fractionation are sufficiently denaturing to activate a significant amount of cryptic autoreactive plasma IgG which could be involved not only in the therapeutic immunomodulatory effects of IVIg but also in the adverse “allergic” reactions often observed in IVIg-infused patients. |
| doi_str_mv | 10.1016/j.clim.2009.06.005 |
| format | Article |
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IVIg have been shown to bind to a variety of human proteins including BAFF, amyloid beta peptide and GM-CSF. It has been suggested that this autoreactivity could contribute to the therapeutic immunomodulatory effects of IVIg. In this work, we showed that native IgG purified from plasma under non-denaturing conditions were much less autoreactive than IVIg. However the native IgG autoreactivity with BAFF, amyloid beta peptide and GM-CSF was significantly increased by short incubation under the slightly denaturing conditions used during industrial plasma fractionation. We conclude that the relatively mild conditions used in industrial plasma fractionation are sufficiently denaturing to activate a significant amount of cryptic autoreactive plasma IgG which could be involved not only in the therapeutic immunomodulatory effects of IVIg but also in the adverse “allergic” reactions often observed in IVIg-infused patients.</description><identifier>ISSN: 1521-6616</identifier><identifier>EISSN: 1521-7035</identifier><identifier>DOI: 10.1016/j.clim.2009.06.005</identifier><identifier>PMID: 19604724</identifier><identifier>CODEN: CLIIFY</identifier><language>eng</language><publisher>Amsterdam: Elsevier Inc</publisher><subject>Allergy and Immunology ; Amyloid beta-Peptides - immunology ; Autoreactivity ; B-Cell Activating Factor - immunology ; Biological and medical sciences ; Cryptic autoantibodies ; Ethanol - pharmacology ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; Granulocyte-Macrophage Colony-Stimulating Factor - immunology ; Humans ; Hydrogen-Ion Concentration ; Immunoglobulin G - chemistry ; Immunoglobulin G - immunology ; Immunoglobulin G - isolation & purification ; Immunoglobulins, Intravenous - chemistry ; Immunoglobulins, Intravenous - immunology ; Intravenous immunoglobulins ; Mild denaturation ; Protein Denaturation ; Serum - chemistry ; Serum - immunology</subject><ispartof>Clinical immunology (Orlando, Fla.), 2009-10, Vol.133 (1), p.52-60</ispartof><rights>Elsevier Inc.</rights><rights>2009 Elsevier Inc.</rights><rights>2009 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c470t-747fcf225bdfa43a9b17555fad6c58146775ca3439db228e3bb80b643c38d0533</citedby><cites>FETCH-LOGICAL-c470t-747fcf225bdfa43a9b17555fad6c58146775ca3439db228e3bb80b643c38d0533</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.clim.2009.06.005$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,778,782,3539,27911,27912,45982</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21979854$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19604724$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>St-Amour, Isabelle</creatorcontrib><creatorcontrib>Laroche, André</creatorcontrib><creatorcontrib>Bazin, Renée</creatorcontrib><creatorcontrib>Lemieux, Réal</creatorcontrib><title>Activation of cryptic IgG reactive with BAFF, amyloid beta peptide and GM-CSF during the industrial fractionation of human plasma into therapeutic intravenous immunoglobulins</title><title>Clinical immunology (Orlando, Fla.)</title><addtitle>Clin Immunol</addtitle><description>Abstract The mechanisms of therapeutic action of IVIg are still unclear in most autoimmune and inflammatory diseases. IVIg have been shown to bind to a variety of human proteins including BAFF, amyloid beta peptide and GM-CSF. It has been suggested that this autoreactivity could contribute to the therapeutic immunomodulatory effects of IVIg. In this work, we showed that native IgG purified from plasma under non-denaturing conditions were much less autoreactive than IVIg. However the native IgG autoreactivity with BAFF, amyloid beta peptide and GM-CSF was significantly increased by short incubation under the slightly denaturing conditions used during industrial plasma fractionation. We conclude that the relatively mild conditions used in industrial plasma fractionation are sufficiently denaturing to activate a significant amount of cryptic autoreactive plasma IgG which could be involved not only in the therapeutic immunomodulatory effects of IVIg but also in the adverse “allergic” reactions often observed in IVIg-infused patients.</description><subject>Allergy and Immunology</subject><subject>Amyloid beta-Peptides - immunology</subject><subject>Autoreactivity</subject><subject>B-Cell Activating Factor - immunology</subject><subject>Biological and medical sciences</subject><subject>Cryptic autoantibodies</subject><subject>Ethanol - pharmacology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>Granulocyte-Macrophage Colony-Stimulating Factor - immunology</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>Immunoglobulin G - chemistry</subject><subject>Immunoglobulin G - immunology</subject><subject>Immunoglobulin G - isolation & purification</subject><subject>Immunoglobulins, Intravenous - chemistry</subject><subject>Immunoglobulins, Intravenous - immunology</subject><subject>Intravenous immunoglobulins</subject><subject>Mild denaturation</subject><subject>Protein Denaturation</subject><subject>Serum - chemistry</subject><subject>Serum - immunology</subject><issn>1521-6616</issn><issn>1521-7035</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFks2O0zAUhSMEYn7gBVggb2A1LbYT242EkEpFy0iDWAysLce-aV0SO2M7RX0pnhFHrQaJBaxs2d-55-qeWxSvCJ4TTPi7_Vx3tp9TjOs55nOM2ZPikjBKZgKX7On5zjnhF8VVjHucCUr58-KC1BxXglaXxa-lTvagkvUO-RbpcByS1eh2u0EB1PQH6KdNO_RxuV7fINUfO28NaiApNEBmDSDlDNp8ma3u18iMwbotSjtA1pkxpmBVh9owVfLu0WY39sqhoVOxVxlMflIENcA4meeHoA7g_BiR7fvR-W3nm7GzLr4onrWqi_DyfF4X39efvq0-z-6-bm5Xy7uZrgROM1GJVreUssa0qipV3RDBGGuV4ZotSMWFYFqVVVmbhtIFlE2zwA2vSl0uDGZleV28PdUdgn8YISbZ26ih65SD3JbkgjNci_-DlJA6D11kkJ5AHXyMAVo5BNurcJQEyylOuZdTnHKKU2Iuc1hZ9PpcfWx6MH8k5_wy8OYMqKhVlwfttI2PHCW1qBds4t6fOMhDO1gIMmoLToOxAXSSxtt_9_HhL3lGnM2OP-AIce_H4HIckshIJZb30-JNe4drjAUmZfkb-pnVqA</recordid><startdate>20091001</startdate><enddate>20091001</enddate><creator>St-Amour, Isabelle</creator><creator>Laroche, André</creator><creator>Bazin, Renée</creator><creator>Lemieux, Réal</creator><general>Elsevier Inc</general><general>Elsevier</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>7TK</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20091001</creationdate><title>Activation of cryptic IgG reactive with BAFF, amyloid beta peptide and GM-CSF during the industrial fractionation of human plasma into therapeutic intravenous immunoglobulins</title><author>St-Amour, Isabelle ; Laroche, André ; Bazin, Renée ; Lemieux, Réal</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c470t-747fcf225bdfa43a9b17555fad6c58146775ca3439db228e3bb80b643c38d0533</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Allergy and Immunology</topic><topic>Amyloid beta-Peptides - immunology</topic><topic>Autoreactivity</topic><topic>B-Cell Activating Factor - immunology</topic><topic>Biological and medical sciences</topic><topic>Cryptic autoantibodies</topic><topic>Ethanol - pharmacology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>Granulocyte-Macrophage Colony-Stimulating Factor - immunology</topic><topic>Humans</topic><topic>Hydrogen-Ion Concentration</topic><topic>Immunoglobulin G - chemistry</topic><topic>Immunoglobulin G - immunology</topic><topic>Immunoglobulin G - isolation & purification</topic><topic>Immunoglobulins, Intravenous - chemistry</topic><topic>Immunoglobulins, Intravenous - immunology</topic><topic>Intravenous immunoglobulins</topic><topic>Mild denaturation</topic><topic>Protein Denaturation</topic><topic>Serum - chemistry</topic><topic>Serum - immunology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>St-Amour, Isabelle</creatorcontrib><creatorcontrib>Laroche, André</creatorcontrib><creatorcontrib>Bazin, Renée</creatorcontrib><creatorcontrib>Lemieux, Réal</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>Neurosciences Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Clinical immunology (Orlando, Fla.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>St-Amour, Isabelle</au><au>Laroche, André</au><au>Bazin, Renée</au><au>Lemieux, Réal</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Activation of cryptic IgG reactive with BAFF, amyloid beta peptide and GM-CSF during the industrial fractionation of human plasma into therapeutic intravenous immunoglobulins</atitle><jtitle>Clinical immunology (Orlando, Fla.)</jtitle><addtitle>Clin Immunol</addtitle><date>2009-10-01</date><risdate>2009</risdate><volume>133</volume><issue>1</issue><spage>52</spage><epage>60</epage><pages>52-60</pages><issn>1521-6616</issn><eissn>1521-7035</eissn><coden>CLIIFY</coden><abstract>Abstract The mechanisms of therapeutic action of IVIg are still unclear in most autoimmune and inflammatory diseases. IVIg have been shown to bind to a variety of human proteins including BAFF, amyloid beta peptide and GM-CSF. It has been suggested that this autoreactivity could contribute to the therapeutic immunomodulatory effects of IVIg. In this work, we showed that native IgG purified from plasma under non-denaturing conditions were much less autoreactive than IVIg. However the native IgG autoreactivity with BAFF, amyloid beta peptide and GM-CSF was significantly increased by short incubation under the slightly denaturing conditions used during industrial plasma fractionation. We conclude that the relatively mild conditions used in industrial plasma fractionation are sufficiently denaturing to activate a significant amount of cryptic autoreactive plasma IgG which could be involved not only in the therapeutic immunomodulatory effects of IVIg but also in the adverse “allergic” reactions often observed in IVIg-infused patients.</abstract><cop>Amsterdam</cop><pub>Elsevier Inc</pub><pmid>19604724</pmid><doi>10.1016/j.clim.2009.06.005</doi><tpages>9</tpages></addata></record> |
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| subjects | Allergy and Immunology Amyloid beta-Peptides - immunology Autoreactivity B-Cell Activating Factor - immunology Biological and medical sciences Cryptic autoantibodies Ethanol - pharmacology Fundamental and applied biological sciences. Psychology Fundamental immunology Granulocyte-Macrophage Colony-Stimulating Factor - immunology Humans Hydrogen-Ion Concentration Immunoglobulin G - chemistry Immunoglobulin G - immunology Immunoglobulin G - isolation & purification Immunoglobulins, Intravenous - chemistry Immunoglobulins, Intravenous - immunology Intravenous immunoglobulins Mild denaturation Protein Denaturation Serum - chemistry Serum - immunology |
| title | Activation of cryptic IgG reactive with BAFF, amyloid beta peptide and GM-CSF during the industrial fractionation of human plasma into therapeutic intravenous immunoglobulins |
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