Identification of α(1,6)fucosylated proteins differentially expressed in human colorectal cancer
- Equal contributors
1 Department of Biochemistry, Genetics and Immunology, Faculty of Biology, University of Vigo, Campus As Lagoas-Marcosende S/N, 36310, Vigo, Spain
2 Pathology Service, University Complex Hospital of Ourense, Ramón Puga 54, 32005, Ourense, Spain
Citation and License
BMC Cancer 2011, 11:508 doi:10.1186/1471-2407-11-508Published: 7 December 2011
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.
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.
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.
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.