Analysis of site and structure specific core fucosylation in liver cirrhosis using exoglycosidase-assisted data-independent LC-MS/MS

Abstract Carbohydrates form one of the major groups of biological macromolecules in living organisms. Many biological processes including protein folding, stability, immune response, and receptor activation are regulated by glycosylation. Fucosylation of proteins regulates such processes and is asso...

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Autores principales:	Miloslav Sanda, Jaeil Ahn, Petr Kozlik, Radoslav Goldman
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/36a4944f127b46fbb80e2e4198cbad33
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spelling	oai:doaj.org-article:36a4944f127b46fbb80e2e4198cbad332021-12-05T12:12:15ZAnalysis of site and structure specific core fucosylation in liver cirrhosis using exoglycosidase-assisted data-independent LC-MS/MS10.1038/s41598-021-02838-32045-2322https://doaj.org/article/36a4944f127b46fbb80e2e4198cbad332021-12-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-02838-3https://doaj.org/toc/2045-2322Abstract Carbohydrates form one of the major groups of biological macromolecules in living organisms. Many biological processes including protein folding, stability, immune response, and receptor activation are regulated by glycosylation. Fucosylation of proteins regulates such processes and is associated with various diseases including autoimmunity and cancer. Mass spectrometry efficiently identifies structures of fucosylated glycans or sites of core fucosylated N-glycopeptides but quantification of the glycopeptides remains less explored. We performed experiments that facilitate quantitative analysis of the core fucosylation of proteins with partial structural resolution of the glycans and we present results of the mass spectrometric SWATH-type DIA analysis of relative abundances of the core fucosylated glycoforms of 45 glycopeptides to their nonfucosylated glycoforms derived from 18 serum proteins in liver disease of different etiologies. Our results show that a combination of soft fragmentation with exoglycosidases is efficient at the assignment and quantification of the core fucosylated N-glycoforms at specific sites of protein attachment. In addition, our results show that disease-associated changes in core fucosylation are peptide-dependent and further differ by branching of the core fucosylated glycans. Further studies are needed to verify whether tri- and tetra-antennary core fucosylated glycopeptides could be used as markers of liver disease progression.Miloslav SandaJaeil AhnPetr KozlikRadoslav GoldmanNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Miloslav Sanda Jaeil Ahn Petr Kozlik Radoslav Goldman Analysis of site and structure specific core fucosylation in liver cirrhosis using exoglycosidase-assisted data-independent LC-MS/MS
description	Abstract Carbohydrates form one of the major groups of biological macromolecules in living organisms. Many biological processes including protein folding, stability, immune response, and receptor activation are regulated by glycosylation. Fucosylation of proteins regulates such processes and is associated with various diseases including autoimmunity and cancer. Mass spectrometry efficiently identifies structures of fucosylated glycans or sites of core fucosylated N-glycopeptides but quantification of the glycopeptides remains less explored. We performed experiments that facilitate quantitative analysis of the core fucosylation of proteins with partial structural resolution of the glycans and we present results of the mass spectrometric SWATH-type DIA analysis of relative abundances of the core fucosylated glycoforms of 45 glycopeptides to their nonfucosylated glycoforms derived from 18 serum proteins in liver disease of different etiologies. Our results show that a combination of soft fragmentation with exoglycosidases is efficient at the assignment and quantification of the core fucosylated N-glycoforms at specific sites of protein attachment. In addition, our results show that disease-associated changes in core fucosylation are peptide-dependent and further differ by branching of the core fucosylated glycans. Further studies are needed to verify whether tri- and tetra-antennary core fucosylated glycopeptides could be used as markers of liver disease progression.
format	article
author	Miloslav Sanda Jaeil Ahn Petr Kozlik Radoslav Goldman
author_facet	Miloslav Sanda Jaeil Ahn Petr Kozlik Radoslav Goldman
author_sort	Miloslav Sanda
title	Analysis of site and structure specific core fucosylation in liver cirrhosis using exoglycosidase-assisted data-independent LC-MS/MS
title_short	Analysis of site and structure specific core fucosylation in liver cirrhosis using exoglycosidase-assisted data-independent LC-MS/MS
title_full	Analysis of site and structure specific core fucosylation in liver cirrhosis using exoglycosidase-assisted data-independent LC-MS/MS
title_fullStr	Analysis of site and structure specific core fucosylation in liver cirrhosis using exoglycosidase-assisted data-independent LC-MS/MS
title_full_unstemmed	Analysis of site and structure specific core fucosylation in liver cirrhosis using exoglycosidase-assisted data-independent LC-MS/MS
title_sort	analysis of site and structure specific core fucosylation in liver cirrhosis using exoglycosidase-assisted data-independent lc-ms/ms
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/36a4944f127b46fbb80e2e4198cbad33
work_keys_str_mv	AT miloslavsanda analysisofsiteandstructurespecificcorefucosylationinlivercirrhosisusingexoglycosidaseassisteddataindependentlcmsms AT jaeilahn analysisofsiteandstructurespecificcorefucosylationinlivercirrhosisusingexoglycosidaseassisteddataindependentlcmsms AT petrkozlik analysisofsiteandstructurespecificcorefucosylationinlivercirrhosisusingexoglycosidaseassisteddataindependentlcmsms AT radoslavgoldman analysisofsiteandstructurespecificcorefucosylationinlivercirrhosisusingexoglycosidaseassisteddataindependentlcmsms
_version_	1718372126122049536

Analysis of site and structure specific core fucosylation in liver cirrhosis using exoglycosidase-assisted data-independent LC-MS/MS

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