CccamCLineManagerExe
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Lens fiber cells naturally contain a large amount of asparagine-linked glycans which are likely to undergo modification in pathologies such as cataract. This study focuses on the degradation of dextran, a model glycan, in lens epithelial cells. Cells grown for 24 h in serum-free medium containing [14C]dextran were either untreated or incubated with various inhibitors. Autoradiography of the cultures showed that dextran undergoes lysosomal degradation, and this was confirmed by electron microscopy. Activity of various glycanases in the extracts of lysosomes isolated from cells treated with dextran was analysed. Most of the alpha-L-fucosidase activity was associated with this fraction, while the beta-galactosidase activity was low. On the other hand, alpha-mannosidase activity was much lower than that of lysosomal proteases and was mainly associated with the supernatant fractions. It was concluded that alpha-L-fucosidase is the major enzyme responsible for the degradation of dextran in the lens.Lipid peroxidation in rat thymus and spleen induced by xenobiotic agents.
We investigated the effects of various xenobiotic agents on the lipid peroxidation in the rat thymus and spleen. Ethanol, acetaldehyde, retinol and terbutryn were
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