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Identification of α(1,6)fucosylated proteins differentially expressed in human colorectal cancer

SUMMARY: BACKGROUND: A universal hallmark of cancer cells is the change in their glycosylation phenotype. One of the most frequent alterations in the normal glycosylation pattern observed during carcinogenesis is the enhancement of α(1,6)linked fucose residues of glycoproteins, due to the up-regulat...

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Autores principales: Muinelo-Romay, Laura, Villar-Portela, Susana, Cuevas, Elisa, Gil-Martín, Emilio, Fernández-Briera, Almudena
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3297542/
https://www.ncbi.nlm.nih.gov/pubmed/22152070
http://dx.doi.org/10.1186/1471-2407-11-508
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author Muinelo-Romay, Laura
Villar-Portela, Susana
Cuevas, Elisa
Gil-Martín, Emilio
Fernández-Briera, Almudena
author_facet Muinelo-Romay, Laura
Villar-Portela, Susana
Cuevas, Elisa
Gil-Martín, Emilio
Fernández-Briera, Almudena
author_sort Muinelo-Romay, Laura
collection PubMed
description SUMMARY: BACKGROUND: A universal hallmark of cancer cells is the change in their glycosylation phenotype. One of the most frequent alterations in the normal glycosylation pattern observed during carcinogenesis is the enhancement of α(1,6)linked fucose residues of glycoproteins, due to the up-regulation of the α(1,6)fucosyltransferase activity. Our previous results demonstrated the specific alteration of this enzyme activity and expression in colorectal cancer, suggesting its implication in tumour development and progression. METHODS: In the current work we combined a LCA-affinity chromatography with SDS-PAGE and mass spectrometry in order to identify α(1,6)fucosylated proteins differentially expressed in colorectal cancer. This strategy allowed the identification of a group of α(1,6)fucosylated proteins candidates to be involved in CRC malignancy. RESULTS: The majority of the identified proteins take part in cell signaling and interaction processes as well as in modulation of the immunological response. Likewise, we confirmed the increased expression of GRP94 in colorectal cancer tissue and the significant down-regulation of the IgGFcBP expression in tumour cells. CONCLUSION: All these results validate the importance of core-fucosylated proteins profile analysis to understand the mechanisms which promote cancer onset and progression and to discover new tumour markers or therapeutic targets.
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spelling pubmed-32975422012-03-09 Identification of α(1,6)fucosylated proteins differentially expressed in human colorectal cancer Muinelo-Romay, Laura Villar-Portela, Susana Cuevas, Elisa Gil-Martín, Emilio Fernández-Briera, Almudena BMC Cancer Research Article SUMMARY: BACKGROUND: A universal hallmark of cancer cells is the change in their glycosylation phenotype. One of the most frequent alterations in the normal glycosylation pattern observed during carcinogenesis is the enhancement of α(1,6)linked fucose residues of glycoproteins, due to the up-regulation of the α(1,6)fucosyltransferase activity. Our previous results demonstrated the specific alteration of this enzyme activity and expression in colorectal cancer, suggesting its implication in tumour development and progression. METHODS: In the current work we combined a LCA-affinity chromatography with SDS-PAGE and mass spectrometry in order to identify α(1,6)fucosylated proteins differentially expressed in colorectal cancer. This strategy allowed the identification of a group of α(1,6)fucosylated proteins candidates to be involved in CRC malignancy. RESULTS: The majority of the identified proteins take part in cell signaling and interaction processes as well as in modulation of the immunological response. Likewise, we confirmed the increased expression of GRP94 in colorectal cancer tissue and the significant down-regulation of the IgGFcBP expression in tumour cells. CONCLUSION: All these results validate the importance of core-fucosylated proteins profile analysis to understand the mechanisms which promote cancer onset and progression and to discover new tumour markers or therapeutic targets. BioMed Central 2011-12-07 /pmc/articles/PMC3297542/ /pubmed/22152070 http://dx.doi.org/10.1186/1471-2407-11-508 Text en Copyright ©2011 Muinelo-Romay et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Muinelo-Romay, Laura
Villar-Portela, Susana
Cuevas, Elisa
Gil-Martín, Emilio
Fernández-Briera, Almudena
Identification of α(1,6)fucosylated proteins differentially expressed in human colorectal cancer
title Identification of α(1,6)fucosylated proteins differentially expressed in human colorectal cancer
title_full Identification of α(1,6)fucosylated proteins differentially expressed in human colorectal cancer
title_fullStr Identification of α(1,6)fucosylated proteins differentially expressed in human colorectal cancer
title_full_unstemmed Identification of α(1,6)fucosylated proteins differentially expressed in human colorectal cancer
title_short Identification of α(1,6)fucosylated proteins differentially expressed in human colorectal cancer
title_sort identification of α(1,6)fucosylated proteins differentially expressed in human colorectal cancer
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3297542/
https://www.ncbi.nlm.nih.gov/pubmed/22152070
http://dx.doi.org/10.1186/1471-2407-11-508
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