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Recent Advances in Clinical Glycoproteomics of Immunoglobulins (Igs)

Antibody glycosylation analysis has seen methodological progress resulting in new findings with regard to antibody glycan structure and function in recent years. For example, antigen-specific IgG glycosylation analysis is now applicable for clinical samples because of the increased sensitivity of me...

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Autores principales: Plomp, Rosina, Bondt, Albert, de Haan, Noortje, Rombouts, Yoann, Wuhrer, Manfred
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Biochemistry and Molecular Biology 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4937499/
https://www.ncbi.nlm.nih.gov/pubmed/27009965
http://dx.doi.org/10.1074/mcp.O116.058503
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author Plomp, Rosina
Bondt, Albert
de Haan, Noortje
Rombouts, Yoann
Wuhrer, Manfred
author_facet Plomp, Rosina
Bondt, Albert
de Haan, Noortje
Rombouts, Yoann
Wuhrer, Manfred
author_sort Plomp, Rosina
collection PubMed
description Antibody glycosylation analysis has seen methodological progress resulting in new findings with regard to antibody glycan structure and function in recent years. For example, antigen-specific IgG glycosylation analysis is now applicable for clinical samples because of the increased sensitivity of measurements, and this has led to new insights in the relationship between IgG glycosylation and various diseases. Furthermore, many new methods have been developed for the purification and analysis of IgG Fc glycopeptides, notably multiple reaction monitoring for high-throughput quantitative glycosylation analysis. In addition, new protocols for IgG Fab glycosylation analysis were established revealing autoimmune disease-associated changes. Functional analysis has shown that glycosylation of IgA and IgE is involved in transport across the intestinal epithelium and receptor binding, respectively.
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spelling pubmed-49374992016-07-19 Recent Advances in Clinical Glycoproteomics of Immunoglobulins (Igs) Plomp, Rosina Bondt, Albert de Haan, Noortje Rombouts, Yoann Wuhrer, Manfred Mol Cell Proteomics Minireview Antibody glycosylation analysis has seen methodological progress resulting in new findings with regard to antibody glycan structure and function in recent years. For example, antigen-specific IgG glycosylation analysis is now applicable for clinical samples because of the increased sensitivity of measurements, and this has led to new insights in the relationship between IgG glycosylation and various diseases. Furthermore, many new methods have been developed for the purification and analysis of IgG Fc glycopeptides, notably multiple reaction monitoring for high-throughput quantitative glycosylation analysis. In addition, new protocols for IgG Fab glycosylation analysis were established revealing autoimmune disease-associated changes. Functional analysis has shown that glycosylation of IgA and IgE is involved in transport across the intestinal epithelium and receptor binding, respectively. The American Society for Biochemistry and Molecular Biology 2016-07 2016-03-23 /pmc/articles/PMC4937499/ /pubmed/27009965 http://dx.doi.org/10.1074/mcp.O116.058503 Text en © 2016 by The American Society for Biochemistry and Molecular Biology, Inc. Author's Choice—Final version free via Creative Commons CC-BY license (http://creativecommons.org/licenses/by/4.0) .
spellingShingle Minireview
Plomp, Rosina
Bondt, Albert
de Haan, Noortje
Rombouts, Yoann
Wuhrer, Manfred
Recent Advances in Clinical Glycoproteomics of Immunoglobulins (Igs)
title Recent Advances in Clinical Glycoproteomics of Immunoglobulins (Igs)
title_full Recent Advances in Clinical Glycoproteomics of Immunoglobulins (Igs)
title_fullStr Recent Advances in Clinical Glycoproteomics of Immunoglobulins (Igs)
title_full_unstemmed Recent Advances in Clinical Glycoproteomics of Immunoglobulins (Igs)
title_short Recent Advances in Clinical Glycoproteomics of Immunoglobulins (Igs)
title_sort recent advances in clinical glycoproteomics of immunoglobulins (igs)
topic Minireview
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4937499/
https://www.ncbi.nlm.nih.gov/pubmed/27009965
http://dx.doi.org/10.1074/mcp.O116.058503
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