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

ABSTRACT:

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)fu

SUBMITTER: Muinelo-Romay L 

PROVIDER: S-EPMC3297542 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature