Increased α1-3 fucosylation of α-1-acid glycoprotein (AGP) in pancreatic cancer.

Pancreatic cancer (PDAC) lacks reliable diagnostic biomarkers and the search for new biomarkers represents an important challenge. Previous results looking at a small cohort of patients showed an increase in α-1-acid glycoprotein (AGP) fucosylation in advanced PDAC using N-glycan sequencing. Here, w...

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Detalles Bibliográficos
Autores: Balmaña, Meritxell, Giménez, Estela, Puerta, Angel, Llop Escorihuela, Esther, Figueras, Joan, Fort, Esther, Sanz-Nebot, Victoria, Bolos Pi, Ma. Carmen de, Rizzi, Andreas, Barrabés, Sílvia, Frutos, Mercedes de, Peracaula, Rosa
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2016
País:España
Institución:Universitat Pompeu Fabra
Repositorio:Repositorio Digital de la UPF
OAI Identifier:oai:repositori.upf.edu:10230/25722
Acceso en línea:http://hdl.handle.net/10230/25722
http://dx.doi.org/10.1016/j.jprot.2015.11.006
Access Level:acceso abierto
Palabra clave:Pàncrees -- Càncer
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spelling Increased α1-3 fucosylation of α-1-acid glycoprotein (AGP) in pancreatic cancer.Balmaña, MeritxellGiménez, EstelaPuerta, AngelLlop Escorihuela, EstherFigueras, JoanFort, EstherSanz-Nebot, VictoriaBolos Pi, Ma. Carmen deRizzi, AndreasBarrabés, SílviaFrutos, Mercedes dePeracaula, RosaPàncrees -- CàncerPancreatic cancer (PDAC) lacks reliable diagnostic biomarkers and the search for new biomarkers represents an important challenge. Previous results looking at a small cohort of patients showed an increase in α-1-acid glycoprotein (AGP) fucosylation in advanced PDAC using N-glycan sequencing. Here, we have analysed AGP glycoforms in a larger cohort using several analytical techniques including mass spectrometry (MS), capillary zone electrophoresis (CZE) and enzyme-linked lectin assays (ELLAs) for determining AGP glycoforms which could be PDAC associated. AGP from 31 serum samples, including healthy controls (HC), chronic pancreatitis (ChrP) and PDAC patients, was purified by immunoaffinity chromatography. Stable isotope labelling of AGP released N-glycans and their analysis by zwitterionic hydrophilic interaction capillary liquid chromatography electrospray MS (μZIC-HILIC-ESI-MS) showed an increase in AGP fucosylated glycoforms in PDAC compared to ChrP and HC. By CZE-UV analysis, relative concentrations of some of the AGP isoforms were found significantly different compared to those in PDAC and HC. Finally, ELLAs using Aleuria aurantia lectin displayed a significant increase in AGP fucosylation, before and after AGP neuraminidase treatment, in advanced PDAC compared to ChrP and HC, respectively. Altogether, these results indicate that α1-3 fucosylated glycoforms of AGP are increased in PDAC and could be potentially regarded as a PDAC biomarker.M.B. acknowledges the University of Girona for a pre-doctoral fellowship. This work was supported by the Government of Catalonia (grant 2014 SGR 229), the Spanish Ministry of Science and Innovation (grant BIO 2010-16922, awarded to R. P) and the Spanish Ministry of Economy and Competitiveness (grant CTQ2013-43236, awarded to M.F. and grant CTQ2011-27130, awarded to V. S-N).Elsevier201620172016info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersionapplication/pdfapplication/pdfhttp://hdl.handle.net/10230/25722http://dx.doi.org/10.1016/j.jprot.2015.11.006reponame:Repositorio Digital de la UPFinstname:Universitat Pompeu FabraInglésJournal of Proteomics. 2016 Jan 30;132:144-54info:eu-repo/grantAgreement/ES/3PN/BIO2010-16922© 2015 Elsevier. Elsevier has partnered with Copyright Clearance Center's RightsLink service to offer a variety of options for reusing Elsevier contentinfo:eu-repo/semantics/openAccessoai:repositori.upf.edu:10230/257222026-06-12T07:21:37Z
dc.title.none.fl_str_mv Increased α1-3 fucosylation of α-1-acid glycoprotein (AGP) in pancreatic cancer.
title Increased α1-3 fucosylation of α-1-acid glycoprotein (AGP) in pancreatic cancer.
spellingShingle Increased α1-3 fucosylation of α-1-acid glycoprotein (AGP) in pancreatic cancer.
Balmaña, Meritxell
Pàncrees -- Càncer
title_short Increased α1-3 fucosylation of α-1-acid glycoprotein (AGP) in pancreatic cancer.
title_full Increased α1-3 fucosylation of α-1-acid glycoprotein (AGP) in pancreatic cancer.
title_fullStr Increased α1-3 fucosylation of α-1-acid glycoprotein (AGP) in pancreatic cancer.
title_full_unstemmed Increased α1-3 fucosylation of α-1-acid glycoprotein (AGP) in pancreatic cancer.
title_sort Increased α1-3 fucosylation of α-1-acid glycoprotein (AGP) in pancreatic cancer.
dc.creator.none.fl_str_mv Balmaña, Meritxell
Giménez, Estela
Puerta, Angel
Llop Escorihuela, Esther
Figueras, Joan
Fort, Esther
Sanz-Nebot, Victoria
Bolos Pi, Ma. Carmen de
Rizzi, Andreas
Barrabés, Sílvia
Frutos, Mercedes de
Peracaula, Rosa
author Balmaña, Meritxell
author_facet Balmaña, Meritxell
Giménez, Estela
Puerta, Angel
Llop Escorihuela, Esther
Figueras, Joan
Fort, Esther
Sanz-Nebot, Victoria
Bolos Pi, Ma. Carmen de
Rizzi, Andreas
Barrabés, Sílvia
Frutos, Mercedes de
Peracaula, Rosa
author_role author
author2 Giménez, Estela
Puerta, Angel
Llop Escorihuela, Esther
Figueras, Joan
Fort, Esther
Sanz-Nebot, Victoria
Bolos Pi, Ma. Carmen de
Rizzi, Andreas
Barrabés, Sílvia
Frutos, Mercedes de
Peracaula, Rosa
author2_role author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Pàncrees -- Càncer
topic Pàncrees -- Càncer
description Pancreatic cancer (PDAC) lacks reliable diagnostic biomarkers and the search for new biomarkers represents an important challenge. Previous results looking at a small cohort of patients showed an increase in α-1-acid glycoprotein (AGP) fucosylation in advanced PDAC using N-glycan sequencing. Here, we have analysed AGP glycoforms in a larger cohort using several analytical techniques including mass spectrometry (MS), capillary zone electrophoresis (CZE) and enzyme-linked lectin assays (ELLAs) for determining AGP glycoforms which could be PDAC associated. AGP from 31 serum samples, including healthy controls (HC), chronic pancreatitis (ChrP) and PDAC patients, was purified by immunoaffinity chromatography. Stable isotope labelling of AGP released N-glycans and their analysis by zwitterionic hydrophilic interaction capillary liquid chromatography electrospray MS (μZIC-HILIC-ESI-MS) showed an increase in AGP fucosylated glycoforms in PDAC compared to ChrP and HC. By CZE-UV analysis, relative concentrations of some of the AGP isoforms were found significantly different compared to those in PDAC and HC. Finally, ELLAs using Aleuria aurantia lectin displayed a significant increase in AGP fucosylation, before and after AGP neuraminidase treatment, in advanced PDAC compared to ChrP and HC, respectively. Altogether, these results indicate that α1-3 fucosylated glycoforms of AGP are increased in PDAC and could be potentially regarded as a PDAC biomarker.
publishDate 2016
dc.date.none.fl_str_mv 2016
2016
2017
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10230/25722
http://dx.doi.org/10.1016/j.jprot.2015.11.006
url http://hdl.handle.net/10230/25722
http://dx.doi.org/10.1016/j.jprot.2015.11.006
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Journal of Proteomics. 2016 Jan 30;132:144-54
info:eu-repo/grantAgreement/ES/3PN/BIO2010-16922
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Repositorio Digital de la UPF
instname:Universitat Pompeu Fabra
instname_str Universitat Pompeu Fabra
reponame_str Repositorio Digital de la UPF
collection Repositorio Digital de la UPF
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.81155

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