Alterations of CMP-NeuAc:asialofetuin sialyltransferase activities in human colorectal adenocarcinoma.
It has been reported that surface glycoconjugates in tumour cells have more complex and more heavily sialylated sugar chains in glycoproteins. Here, we analysed CMP-NeuAc:asialofetuin sialyltransferase activities in total cell membranes from colorectal cancer tissue with respect to normal adjacent tissue, finding enhanced sialyltransferase activities. Determination of the kinetic parameters for the donor substrate, CMP-NeuAc, revealed that the apparent K(m) in tumour tissue was decreased as regards to the normal value. Furthermore, we failed to find any correlation between this activity and the characteristics of the samples such as the age or sex of the patient, or Dukes' stage of the tumour. In order to know which sialyltransferase activity was altered, we studied the incorporation of NeuAc into N- and O-linked chains from asialofetuin. The results allow us to conclude that it is on N-linked chains where the activity is enhanced. With respect to alpha(2,3)- and alpha(2,6)-NeuAc linkages, we observed that enhanced activity in tumour tissues affects both linkages equally.
Vázquez-Martín
C
C
Department of Biochemistry, Genetics and Immunology, Faculty of Sciences, University of Vigo, Vigo, Spain.
Gil-Martín
E
E
Fernández-Briera
A
A
D000230:Adenocarcinoma / Q000201:enzymology*; D000368:Aged; D000369:Aged, 80 and over; D016022:Case-Control Studies; D002850:Chromatography, Gel; D015179:Colorectal Neoplasms / Q000201:enzymology*; D005260:Female; D006020:Glycopeptides / Q000378:metabolism*; D006801:Humans; D008297:Male; D008875:Middle Aged; D011402:Pronase / Q000494:pharmacology; D012799:Sialyltransferases / Q000378:metabolism*; D000094663:beta-Galactoside alpha-2,3-Sialyltransferase
D006020:Glycopeptides; D012799:Sialyltransferases; D011402:Pronase; D000094663:beta-Galactoside alpha-2,3-Sialyltransferase; C000722087:ST3GAL1 protein, human