Sialyltransferases functions in cancers.
Abnormally elevated levels of sialylated tumor associated carbohydrate antigens are frequently described at the surface of cancer cells and/or secreted in biological fluids. It is now well established that this over-expression may result from deregulation in sialyltransferases enzymatic activity involved in their biosynthesis, but the precise molecular mechanisms remain unknown. Twenty different human sialyltransferases preside to the sialylation of glycoconjugates, either glycolipids or glycoproteins. This review summarizes the current knowledge on human sialyltransferases implicated in the altered expression of sialylated tumor associated antigens, the molecular basis of their regulated expression in cancer cells and the various tools developed by researchers and clinicians for their study in pathological samples.
Unite de Glycobiologie Structurale et Fonctionnelle, Universite Lille Nord de France, Lille1, CNRS UMR 8576, F-59655 Villeneuve d'Ascq, France. anne.harduin@univ-lille1.fr
Anne
A
Harduin-Lepers
Marie-Ange
MA
Krzewinski-Recchi
Florent
F
Colomb
Francois
F
Foulquier
Sophie
S
Groux-Degroote
Philippe
P
Delannoy
D002240:Carbohydrate Sequence; D015971:Gene Expression Regulation, Enzymologic; D006801:Humans; D008969:Molecular Sequence Data; D019158:N-Acetylneuraminic Acid / Q000378:metabolism; D009369:Neoplasms / Q000201:enzymology* / Q000378:metabolism; D012799:Sialyltransferases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D012799:Sialyltransferases; D019158:N-Acetylneuraminic Acid