Abstract
An immunohistochemical investigation of β1,4-galactosyltransferase (β1,4-GalT) on human skin tissue was performed on formalin-fixed paraffin-embedded sections using a monoclonal antibody, MAb8628, which specifically recognizes a protein moiety of human β1,4-GalT. Distribution of the galactose β1,4- N-acetylglucosamine (Gal β1,4GlcNAc)-R epitope was also detected by staining with Ricinus communis agglutinin (RCA) 120. The β1,4-GalT was observed to be localized at the perinuclear region of epidermal keratinocytes. The fine localization was also observed at the supranuclear region in the cells of apocrine glands, eccrine ducts and glands. The positive staining with RCA 120 was well colocalized with the cells expressing the β1,4-GalT. An electron microscopic study revealed that positive signals of β1,4-GalT definitely reside in the Golgi apparatus. No immunoreactivity was observed in any other intracellular structure or on the cell surface. These findings strongly indicated that the β1,4-GalT is the major enzyme responsible for the Gal β1,4GlcNAc-R epitope synthesis in human skin tissue.
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