GDP-L-Fuc:N-acetyl--D-glucosaminide ␣1-6 fucosyltransferase (␣1-6FucT) catalyzes the transfer of a fucosyl residue from GDP-fucose to the asparagine-linked GlcNAc residue of complex N-glycans via ␣1-6 linkage. These oligosaccharide structures are essential for the attachment of polysialic acid to t
Expression and enzyme activity of α(1,6)fucosyltransferase in human colorectal cancer
✍ Scribed by Laura Muinelo-Romay; Cristina Vázquez-Martín; Susana Villar-Portela; Elisa Cuevas; Emilio Gil-Martín; Almudena Fernández-Briera
- Publisher
- John Wiley and Sons
- Year
- 2008
- Tongue
- French
- Weight
- 210 KB
- Volume
- 123
- Category
- Article
- ISSN
- 0020-7136
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✦ Synopsis
Abstract
Changes in enzyme activity and the expression levels of α(1,6)fucosyltransferase [α(1,6)FT] have been reported in certain types of malignant transformations. To develop a better understanding of the role of α(1,6)FT in human colorectal carcinoma (CRC), we analysed the enzyme activity in healthy and tumour tissues. α(1,6)FT activity was considerably higher in tumour tissue than in healthy tissue and was related to gender, lymph node metastasis, type of growth and tumour stage. We also observed a significant increase in the α(1,6)FT expression in tumour tissues as compared to healthy and transitional tissues, inflammatory lesions and adenomas. The immunohistochemical expression in tumour tissues was correlated with the degree of infiltration through the intestinal wall. Finally, a statistical correlation was found between enzyme activity and expression obtained by Western blot in colorectal tumours when compared in the same patient. All these findings demonstrate an alteration of α(1,6)FT activity and expression in CRC. © 2008 Wiley‐Liss, Inc.
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