Cargando…
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...
Autores principales: | , , , , |
---|---|
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 |
_version_ | 1782225884663513088 |
---|---|
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. |
format | Online Article Text |
id | pubmed-3297542 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT muineloromaylaura identificationofa16fucosylatedproteinsdifferentiallyexpressedinhumancolorectalcancer AT villarportelasusana identificationofa16fucosylatedproteinsdifferentiallyexpressedinhumancolorectalcancer AT cuevaselisa identificationofa16fucosylatedproteinsdifferentiallyexpressedinhumancolorectalcancer AT gilmartinemilio identificationofa16fucosylatedproteinsdifferentiallyexpressedinhumancolorectalcancer AT fernandezbrieraalmudena identificationofa16fucosylatedproteinsdifferentiallyexpressedinhumancolorectalcancer |