Immunohistochemical localization of beta1,4-galactosyltransferase in human normal and neoplastic pancreatic tissues

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beta1, 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 beta1,4 linkage. Neoplasms undergo various changes in the carbohydrate moieties of their glycosyltransferase themselves. This process also indicates the possibility of changes in glycosyltransferase themselves. Therefore, we examined the binding pattern of a monoclonal antibody (MAb8628) against GalTase in both normal and neoplastic exocrine tissues. Ten normal and II neoplastic human exocrine pancreatic tissues obtained from surgical operations were used. Frozen sections were incubated with this antibody. Supra-nuclear 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 pen-nuclear region. Neoplastic cells were also stained in their supra-nuclear regions and terminal bars. Supra-nuclear regions were well developed in neoplastic cells and intensely stained compared with those in normal cells. The supra-nuclear regions and the terminal bars corresponded to the trans cistern 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 lead to an increase in the expression of GalTase in the Golgi apparatus, which increase may have an important effect on the intercelluar adhesion and communication among pancreatic epithelial cells. Measurement of this enzyme is useful for diagnois of exocnine pancreatic neoplastic change from normal tissues.