Induction of beta-galactosidase in beta-galactosidase-alpha-neuraminidase deficiency: effects of leupeptin and sucrose.
Copyright policy )Induction of beta-galactosidase in beta-galactosidase-alpha-neuraminidase deficiency: effects of leupeptin and sucrose.
beta-Galactosidase was normalized by a serine-thiol protease inhibitor, leupeptin with concentration of 10 micrograms/ml in cultured skin fibroblasts from patients with beta-galactosidase-alpha-neuraminidase deficiency (beta-Gal-/Neu-). The induction of this enzyme was not observed in normal cells. Because the enzymic activity of cathepsin B1 increased significantly both in beta-Gal-/Neu- and normal cells by leupeptin loading, the restoration of beta-galactosidase in beta-Gal-/Neu- cells can not be explained by the theory that leupeptin inhibited intracellular degradation of beta-galactosidase molecules. The effects of leupeptin and sucrose on lysosomal hydrolase induction were compared.
Sucrose, Hydrolases, Leupeptins, Neuraminidase, Fibroblasts, beta-Galactosidase, Cathepsins, Cathepsin B, Cell Line, Galactosidases, Lactose Intolerance, Enzyme Induction, Humans, Lysosomes, Oligopeptides
Sucrose, Hydrolases, Leupeptins, Neuraminidase, Fibroblasts, beta-Galactosidase, Cathepsins, Cathepsin B, Cell Line, Galactosidases, Lactose Intolerance, Enzyme Induction, Humans, Lysosomes, Oligopeptides
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