Sialyltransferases in cancer.
It has long been known that cancer cells often express more heavily sialylated glycans on their surface and that this feature sometimes correlates with invasion. It is now well established that specific sialylated structures, such as the Thomsen-Friedenreich-related antigens, the sialyl Lewis antigens, the sialyl alpha2-6 lactosaminyl structure, the polysialic acid or some gangliosides, can mediate cellular interactions and are altered in cancer cells. This review summarizes the current knowledge on the cancer-associated alterations in sialyltransferase expression which are often at the basis of the deranged expression of sialylated structures.
Dall'Olio
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Dipartimento di Patologia Sperimentale, Università di Bologna, Via S. Giacomo 14, 40126 Bologna, Italy.
Chiricolo
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D000818:Animals; D015295:Antigens, Tumor-Associated, Carbohydrate / Q000737:chemistry / Q000378:metabolism; D002240:Carbohydrate Sequence; D005732:Gangliosides / Q000378:metabolism; D006801:Humans; D007983:Lewis Blood Group Antigens / Q000737:chemistry / Q000502:physiology; D008969:Molecular Sequence Data; D009369:Neoplasms / Q000201:enzymology* / Q000473:pathology; D012794:Sialic Acids / Q000378:metabolism; D012799:Sialyltransferases / Q000737:chemistry* / Q000502:physiology*
D015295:Antigens, Tumor-Associated, Carbohydrate; D005732:Gangliosides; D007983:Lewis Blood Group Antigens; D012794:Sialic Acids; C021319:polysialic acid; C016467:Thomsen-Friedenreich antigen; D012799:Sialyltransferases