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© 1993 Oxford University Press

research-article

UDP-GalNAc:Fuc{alpha}1–2Gal{alpha}1–3GalNAc transferase activity in hamster pancreatic cancers and in normal hamster alimentary tissues

Masahiko Hirota 1, Parviz M. Pour 1 and William G. Chaney 1 2 3

1The Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center Omaha, NE 68198–4525, USA
2Department of Biochemistry & Molecular Biology, University of Nebraska Medical Center Omaha, NE 68198–4525, USA

3To whom correspondence should be addressed

Ductal adenocarcinomas induced by N-nitrosobis(2-oxopropyl)amine treatment in Syrian hamsters produce blood group-A antigen, which is not present in normal hamster pancreas. To understand the underlying mechanism of A antigen neoexpression in pancreatic cancer cells, we examined the activity of UDP-GalNAc: Fuc{alpha}1–2Gal{alpha}1–3GalNAc transferase (A-transferase), the enzyme responsible for blood group-A antigen production. The specific activity of A-transferase in the pancreatic cancers was ~8 nmol/mg protein/h in membrane preparations, 0.3 nmol/mg protein/h in whole cell extracts, and undetectable in normal hamster pancreas. Significant A-transferase activity was found in normal tissues expressing blood group-A antigen. Although both normal (gastric antrum, colon) and pancreatic cancer cells showed similar enzymatic characteristics (optimal pH, substrate affinity, optimal [Mn2+]), there was a difference in the requirement for divalent cations. The A-transferase in cancer cells showed a more stringent requirement for Mn2+. These results suggest that A-transferase is activated during nitrosamine-induced pancreatic carcinogenesis, which results in the neoexpression of blood group-A antigen. The difference in divalent cation requirements between A-transferase activities of cancer and normal cells may indicate that there are multiple A-transferases present in hamster tissues.


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