Open AccessComparative Study of the Levels of Sialyltransferases Responsible for the Formation of Sugar Chains in Glycoproteins and Gangliosides in Rat Liver and Hepatomas
Author(s) -
Miyagi Taeko,
Koseki Masai,
Tsuiki Shigeru
Publication year - 1988
Publication title -
japanese journal of cancer research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.035
H-Index - 141
eISSN - 1349-7006
pISSN - 0910-5050
DOI - 10.1111/j.1349-7006.1988.tb02231.x
Subject(s) - sialyltransferase , mucin , glycoprotein , chemistry , biochemistry , lactosylceramide , sugar , medicine , endocrinology , biology , enzyme
Sialyltransferases responsible for the formation of sugar chains in glycoproteins were studied in rat hepatoma in comparison with rat liver. Hepatoma induced by feeding Wistar rats with 3′‐ methyl‐4‐dimethyIaminoazobenzene (MeDAB) was more active than Wistar liver in sialylating asialo‐orosomucoid, and this was due to an increased activity of GaI(β1→4)GlcNAc (α→6) sialyltransferase, the major sialyltransferase in these tissues, Gal(β1→3,4)GlcNAc (α→3) sialyltransferase and the sialyltransferases acting on asialo‐bovine submaxillary mucin were, however, decreased in the hepatoma. A similar pattern of sialyltransferase alterations was observed in regenerating liver and other tumors such as AH‐109A hepatoma and Sato lung cancer, both of which had been inoculated into Donryu rats. In contrast to these sialyltransferases, the activities of the sialyltransferases responsible for the formation of gangliosides were markedly different even between Wistar and Donryu livers. When compared with Wistar liver, MeDAB induced hepatoma was higher in lactosylceramide‐ and lower in GM 3 ‐sialyltransferase activity, but these two activities were both lower in AH‐109A compared with Donryu liver.