Change of isoforms' spectra of alpha-L-fucosidase from human skin fibroblasts in intracellular storage of nonhydrolyzable substances.
The effect of exogenous and endogenous products storage in lysosomes on the activity and multiple forms of alpha-L-fucosidase from human skin fibroblasts was investigated. It was shown that sucrose load, modelling intralysosomal accumulation of nonhydrolyzable products, causes certain changes in secretion level of alpha-L-fucosidase and multiple forms' spectra of the intracellular and secreted enzymes. These changes were different for the enzyme from embryonal and postnatal normal fibroblasts. Some changes of secreted alpha-L-fucosidase isoforms' spectra were found in fibroblasts from a patient with Fabry's disease, characterized by the intralysosomal storage of di- and trihexosylceramides. The alterations of isoforms' profiles in Fabry fibroblasts at the early and late accumulation stages were similar to those in sucrose-loaded embryonal and postnatal fibroblasts, respectively. It is proposed that intralysosomal accumulation of nonhydrolyzable compounds influences the alpha-L-fucosidase posttranslational processing.
Beyer
E
E
Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, Moscow.
Ivleva
T
T
Artykova
G
G
Wiederschain
G
G
D002478:Cells, Cultured; D005347:Fibroblasts / Q000201:enzymology / Q000473:pathology; D006801:Humans; D007525:Isoelectric Focusing; D016464:Lysosomal Storage Diseases / Q000201:enzymology / Q000473:pathology; D012867:Skin / Q000196:embryology / Q000201:enzymology*; D005644:alpha-L-Fucosidase / Q000737:chemistry*
D005644:alpha-L-Fucosidase