Alterations in the glycan profile of mouse transferrin: new insights in collagen-​induced arthritis

Transferrin purification from mice serum samples by immunoaffinity chromatography (IAC) was optimized in order to study the possible modifications occurred in its glycans in collagen-induced arthritis (CIA) samples. SDS-PAGE and nanoLC-MS/MS were used to monitor the IAC purification performance. Aft...

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Autores: Mancera Arteu, Montserrat; Giménez López, Estela; Sancho, Jaime; Sanz Nebot, María Victoria
Tipo de documento: Artículo
Estado:Accepted version
Fecha de publicación:2020
País:España
Institución:Universidad de Barcelona
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/184863
Acceso en línea:https://hdl.handle.net/2445/184863
Nivel de acceso:Acceso abierto
Palabra clave:Artritis
Glicoproteïnes
Marcadors bioquímics
Cromatografia d'afinitat
Arthritis
Glycoproteins
Biochemical markers
Affinity chromatography
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author Mancera Arteu, Montserrat
author2 Giménez López, Estela
Sancho, Jaime
Sanz Nebot, María Victoria
author2_role author
author
author
author_browse Giménez López, Estela
Mancera Arteu, Montserrat
Sancho, Jaime
Sanz Nebot, María Victoria
author_facet Mancera Arteu, Montserrat
Giménez López, Estela
Sancho, Jaime
Sanz Nebot, María Victoria
author_role author
collection Dipòsit Digital de la UB
description Transferrin purification from mice serum samples by immunoaffinity chromatography (IAC) was optimized in order to study the possible modifications occurred in its glycans in collagen-induced arthritis (CIA) samples. SDS-PAGE and nanoLC-MS/MS were used to monitor the IAC purification performance. Afterwards, a relative quantification of mouse transferrin (mTf) glycan isomers using [12C6]/[13C6]-aniline was used to unequivocally detect alterations in the glycan profile of CIA mice. In addition, multivariate data analysis was applied to identify the most meaningful glycan isomers for the discrimination between control and pathological samples. Partial least squares discriminant analysis (PLS-DA) revealed that five out of fifteen mTf glycan isomers could be potential biomarkers of CIA, most of them corresponding to highly sialylated structures (H6N5S3_2, H6N5S3_3 and H5N4S3_2). Moreover, some of these glycan isomers also seemed to be related with the progression of CIA, especially H6N5S2 and H6N5S3_2, as their overexpression increased with the clinical score of the pathology. Hence, the established methodology provides valuable information to find glycan-based biomarkers of CIA, but also leaves the door open to evaluate, in the future, glycosylation changes of many other inflammatory diseases, in which transferrin has been described to be altered.
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instname_str Universidad de Barcelona
network_acronym_str ES
network_name_str España
oai_identifier_str oai:diposit.ub.edu:2445/184863
publishDate 2020
publishDateSort 2020
publisher American Chemical Society
publisherStr American Chemical Society
reponame_str Dipòsit Digital de la UB
spelling Alterations in the glycan profile of mouse transferrin: new insights in collagen-​induced arthritis Mancera Arteu, Montserrat Giménez López, Estela Sancho, Jaime Sanz Nebot, María Victoria Artritis Glicoproteïnes Marcadors bioquímics Cromatografia d'afinitat Arthritis Glycoproteins Biochemical markers Affinity chromatography Transferrin purification from mice serum samples by immunoaffinity chromatography (IAC) was optimized in order to study the possible modifications occurred in its glycans in collagen-induced arthritis (CIA) samples. SDS-PAGE and nanoLC-MS/MS were used to monitor the IAC purification performance. Afterwards, a relative quantification of mouse transferrin (mTf) glycan isomers using [12C6]/[13C6]-aniline was used to unequivocally detect alterations in the glycan profile of CIA mice. In addition, multivariate data analysis was applied to identify the most meaningful glycan isomers for the discrimination between control and pathological samples. Partial least squares discriminant analysis (PLS-DA) revealed that five out of fifteen mTf glycan isomers could be potential biomarkers of CIA, most of them corresponding to highly sialylated structures (H6N5S3_2, H6N5S3_3 and H5N4S3_2). Moreover, some of these glycan isomers also seemed to be related with the progression of CIA, especially H6N5S2 and H6N5S3_2, as their overexpression increased with the clinical score of the pathology. Hence, the established methodology provides valuable information to find glycan-based biomarkers of CIA, but also leaves the door open to evaluate, in the future, glycosylation changes of many other inflammatory diseases, in which transferrin has been described to be altered. American Chemical Society https://hdl.handle.net/2445/184863
spellingShingle Alterations in the glycan profile of mouse transferrin: new insights in collagen-​induced arthritis
Mancera Arteu, Montserrat
Artritis
Glicoproteïnes
Marcadors bioquímics
Cromatografia d'afinitat
Arthritis
Glycoproteins
Biochemical markers
Affinity chromatography
status_str acceptedVersion
title Alterations in the glycan profile of mouse transferrin: new insights in collagen-​induced arthritis
title_full Alterations in the glycan profile of mouse transferrin: new insights in collagen-​induced arthritis
title_fullStr Alterations in the glycan profile of mouse transferrin: new insights in collagen-​induced arthritis
title_full_unstemmed Alterations in the glycan profile of mouse transferrin: new insights in collagen-​induced arthritis
title_short Alterations in the glycan profile of mouse transferrin: new insights in collagen-​induced arthritis
title_sort Alterations in the glycan profile of mouse transferrin: new insights in collagen-​induced arthritis
topic Artritis
Glicoproteïnes
Marcadors bioquímics
Cromatografia d'afinitat
Arthritis
Glycoproteins
Biochemical markers
Affinity chromatography
topic_facet Artritis
Glicoproteïnes
Marcadors bioquímics
Cromatografia d'afinitat
Arthritis
Glycoproteins
Biochemical markers
Affinity chromatography
url https://hdl.handle.net/2445/184863