ArticleBMC cancer2011
Identification of α(1,6)fucosylated proteins differentially expressed in human colorectal cancer.
Article in BMC cancer, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- High-Throughput Mass Spectrometry Analysis ofJournal of proteome research · 2024Article
- Inhibition of α(1,6)fucosyltransferase: Effects on Cell Proliferation, Migration, and Adhesion in an SW480/SW620 Syngeneic Colorectal Cancer Model.International journal of molecular sciences · 2022Article
- Identification of Fucosylated SERPINA1 as a Novel Plasma Marker for Pancreatic Cancer Using Lectin Affinity Capture Coupled with iTRAQ-Based Quantitative Glycoproteomics.International journal of molecular sciences · 2021Article
- Glycan array analysis of Pholiota squarrosa lectin and other fucose-oriented lectins.Glycobiology · 2021Article
- Recombinant Lectin from Tepary Bean (Biomolecules · 2020Article
- Large-scale identification of core-fucosylated glycopeptide sites in pancreatic cancer serum using mass spectrometry.Journal of proteome research · 2015Article
- Mass spectrometry-based analysis of glycoproteins and its clinical applications in cancer biomarker discovery.Clinical proteomics · 2014Article
- Targeting deeper the human serum fucome by a liquid-phase multicolumn platform in combination with combinatorial peptide ligand libraries.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2014Article
- Proteomic identification of fucosylated haptoglobin alpha isoforms in ascitic fluids and its localization in ovarian carcinoma tissues from Mexican patients.Journal of ovarian research · 2014Article
- High-sensitivity analytical approaches for the structural characterization of glycoproteins.Chemical reviews · 2013Review
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundA 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.
methodsIn 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.
resultsThe 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.
conclusionAll 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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