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

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

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

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dc.contributor.author Balmaña, Meritxellca
dc.contributor.author Giménez, Estelaca
dc.contributor.author Puerta, Angelca
dc.contributor.author Llop Escorihuela, Estherca
dc.contributor.author Figueras, Joanca
dc.contributor.author Fort, Estherca
dc.contributor.author Sanz-Nebot, Victoriaca
dc.contributor.author Bolos Pi, Ma. Carmen deca
dc.contributor.author Rizzi, Andreasca
dc.contributor.author Barrabés, Sílviaca
dc.contributor.author Frutos, Mercedes deca
dc.contributor.author Peracaula, Rosaca
dc.date.accessioned 2016-02-03T08:35:08Z
dc.date.available 2017-01-31T03:00:04Z
dc.date.issued 2016
dc.description.abstract 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.ca
dc.description.sponsorship 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).
dc.format.mimetype application/pdfca
dc.identifier.citation Balmaña M, Giménez E, Puerta A, Llop E, Figueras J, Fort E. et al. Increased α1-3 fucosylation of α-1-acid glycoprotein (AGP) in pancreatic cancer. J Proteomics. 2016 Jan 30;132:144-54. doi: 10.1016/j.jprot.2015.11.006.ca
dc.identifier.doi http://dx.doi.org/10.1016/j.jprot.2015.11.006
dc.identifier.issn 1874-3919
dc.identifier.uri http://hdl.handle.net/10230/25722
dc.language.iso engca
dc.publisher Elsevierca
dc.relation.ispartof Journal of Proteomics. 2016 Jan 30;132:144-54
dc.relation.projectID info:eu-repo/grantAgreement/ES/3PN/BIO2010-16922
dc.rights.accessRights info:eu-repo/semantics/openAccess
dc.subject.other Pàncrees -- Càncerca
dc.title Increased α1-3 fucosylation of α-1-acid glycoprotein (AGP) in pancreatic cancer.ca
dc.type info:eu-repo/semantics/articleca
dc.type.version info:eu-repo/semantics/acceptedVersionca

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