2026-04-17T05:55:09Zhttps://recercat.cat/oai/request

oai:recercat.cat:10256/124632024-06-18T13:35:30Zcom_2072_452955com_2072_2054col_2072_452958

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 Martorell, Esther Sanz Nebot, María Victoria Bolòs, Carme de Rizzi, Andreas Barrabés Vera, Sílvia Frutos, Mercedes de Peracaula Miró, Rosa Pàncrees -- Càncer Pancreas -- Cancer Marcadors tumorals Tumor markers 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 includingmass 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 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) 2024-06-18T13:35:30Z 2024-06-18T13:35:30Z 2024-06-18T13:35:30Z info:eu-repo/date/embargoEnd/2026-01-01 info:eu-repo/date/embargoEnd/2026-01-01 2016-01-30 info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://hdl.handle.net/10256/12463 info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jprot.2015.11.006 info:eu-repo/semantics/altIdentifier/issn/1874-3919 info:eu-repo/grantAgreement/MICINN//BIO2010-16922/ES/GLICOSILACION ALTERADA EN CANCER: GLICOPROTEINAS Y GLICOSILTRANSFERASAS EN SUERO Y EN TEJIDOS COMO MARCADORES TUMORALES/ Tots els drets reservats info:eu-repo/semantics/embargoedAccess Elsevier © Journal of Proteomics, 2016, vol. 132, p. 144-154 Articles publicats (D-B)