Glycoconjugates in sweat glands and other structures of skin from normal and cystic fibrosis subjects.

Abstract

In this study, glycoconjugates of human skin varied in structure between cell types in an individual and often between individuals for a given cell type. Stored secretory material in dark cells of the sweat gland coil contained complex carbohydrate with terminal alpha-galactose, N-acetylgalactosamine, fucose, or sialic acid. The plasmalemma of clear cells in the secretory coil stained conspicuously for terminal alpha-N-acetylgalactosamine, and the cytosol of clear cells contained lectin-reactive glycogen in the majority of specimens. Superficial and deep cells of the sweat duct evidenced plasmalemmal glycoconjugate with terminal N-acetylgalactosamine. However, only the superficial cell plasmalemma in the duct stained for terminal alpha-N-acetylgalactosamine, fucose, and sialic acid. In several specimens, only the deep cells in the sweat duct revealed plasmalemmal glycoconjugate with terminal beta-galactose. Sebaceous glands alone displayed lectin affinity demonstrative of terminal alpha-galactose and like other sites stained for terminal beta-galactose and alpha-N-acetylgalactosamine. The epithelium in epidermis and hair follicles appeared similar, except for epidermis failing to evidence fucose and alpha-N-acetylgalactosamine with certain lectins. Both underwent changes in glycoconjugate composition with cell maturation. Skin from control subjects and patients with cystic fibrosis did not differ in lectin-binding properties. Abnormalities observed in cystic fibrosis specimens included decreased volume of sebaceous glands and, in two cases, increased infiltration of macrophages staining for terminal N-acetylgalactosamine.