Immunohistochemical localization of beta-1,4-galactosyltransferase in human pancreatic tissues

beta-1,4-Galactosyltransferase (GalTase) is the glycosyltransferase in the Golgi apparatus that transfers galactose from UDP-galactose to terminal N-acetylglucosamine residues in glycoconjugates with formation of a beta-1,4 linkage. Neoplasms undergo various changes in the carbohydrate moieties of their glycoconjugates. This process also indicates the possibility of changes in glycosyltransferases themselves. Therefore, we compared the binding pattern of a monoclonal antibody (MAb8628) against GalTase in both normal and neoplastic exocrine pancreatic tissues. Ten normal and 11 neoplastic human exocrine pancreatic tissues obtained from surgery were used. Frozen sections were incubated with this antibody. Supranuclear regions and terminal bars of normal duct cells and acinar cells revealed positive staining for GalTase at the light microscopic level. Centroacinar cells revealed positive staining in their perinuclear region. Neoplastic cells were also stained in their supranuclear regions and terminal bars. Supranuclear regions were well developed in neoplastic cells and intensely stained compared with those in normal cells. The supranuclear regions and the terminal bars corresponded to the trans cisternae of the Golgi apparatus and the junctional complex (i.e., tight junction and adherens junction), respectively, seen at the electron microscopic level. Pancreatic neoplastic changes thus led to an increase in the expression of GalTase in the Golgi apparatus, the increase of which may have an important effect on the intercellular adhesion and communication among pancreatic epithelial cells. Measurement of this enzyme is useful for diagnosis of exocrine pancreatic neoplastic changes from normal tissues.