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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2011-7-6
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pubmed:abstractText |
Intravenous immunoglobulin G (IVIg) is widely used against a range of clinical symptoms. For its use in immune modulating therapies such as treatment of immune thrombocytopenic purpura high doses of IVIg are required. It has been suggested that only a fraction of IVIg causes this anti immune modulating effect. Recent studies indicated that this fraction is the Fc-sialylated IgG fraction. The aim of our study was to determine the efficacy of IVIg enriched for sialylated IgG (IVIg-SA?) in a murine model of passive immune thrombocytopenia (PIT). We enriched IVIg for sialylated IgG by Sambucus nigra agglutinin (SNA) lectin fractionation and determined the degree of sialylation. Analysis of IVIg-SA? using a lectin-based ELISA revealed that we enriched predominantly for Fab-sialylated IgG, whereas we did not find an increase in Fc-sialylated IgG. Mass spectrometric analysis confirmed that Fc sialylation did not change after SNA lectin fractionation. The efficacy of sialylated IgG was measured by administering IVIg or IVIg-SA? 24 hours prior to an injection of a rat anti-mouse platelet mAb. We found an 85% decrease in platelet count after injection of an anti-platelet mAb, which was reduced to a 70% decrease by injecting IVIg (p<0.01). In contrast, IVIg-SA? had no effect on the platelet count. Serum levels of IVIg and IVIg-SA? were similar, ruling out enhanced IgG clearance as a possible explanation. Our results indicate that SNA lectin fractionation is not a suitable method to enrich IVIg for Fc-sialylated IgG. The use of IVIg enriched for Fab-sialylated IgG abolishes the efficacy of IVIg in the murine PIT model.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/21731683-11133020,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21731683-11161202,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21731683-11493456,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21731683-11547745,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21731683-11736954,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21731683-12617104,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21731683-1387255,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21731683-15866704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21731683-16377538,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21731683-16682800,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21731683-16888140,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/21731683-18926775,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21731683-19036920,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21731683-1934588,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21731683-19688751,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21731683-19821958,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/21731683-20444501,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21731683-20516366,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21731683-20699442,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/21731683-6112565,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21731683-7840433
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1932-6203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
e21246
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pubmed:meshHeading |
pubmed-meshheading:21731683-Animals,
pubmed-meshheading:21731683-Chemical Fractionation,
pubmed-meshheading:21731683-Chromatography, Affinity,
pubmed-meshheading:21731683-Disease Models, Animal,
pubmed-meshheading:21731683-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:21731683-Glycosylation,
pubmed-meshheading:21731683-Humans,
pubmed-meshheading:21731683-Immunoglobulin G,
pubmed-meshheading:21731683-Immunoglobulins, Intravenous,
pubmed-meshheading:21731683-Immunomodulation,
pubmed-meshheading:21731683-Mass Spectrometry,
pubmed-meshheading:21731683-Mice,
pubmed-meshheading:21731683-N-Acetylneuraminic Acid,
pubmed-meshheading:21731683-Plant Lectins,
pubmed-meshheading:21731683-Platelet Count,
pubmed-meshheading:21731683-Purpura, Thrombocytopenic, Idiopathic,
pubmed-meshheading:21731683-Rats,
pubmed-meshheading:21731683-Ribosome Inactivating Proteins
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pubmed:year |
2011
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pubmed:articleTitle |
Enrichment of sialylated IgG by lectin fractionation does not enhance the efficacy of immunoglobulin G in a murine model of immune thrombocytopenia.
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pubmed:affiliation |
Sanquin Research and Landsteiner Laboratory, Academic Medical Centre, University of Amsterdam, Amsterdam, The Netherlands.
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pubmed:publicationType |
Journal Article
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