Change of isoforms' spectra of alpha-L-fucosidase from human skin fibroblasts in intracellular storage of nonhydrolyzable substances.

Abstract

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.

• Authors: E Beyer, T Ivleva, G Artykova, G Wiederschain
• Journal: Biochimica et biophysica acta (Biochim Biophys Acta) Vol. 1270 Issue 1 Pg. 7-11 (Jan 25 1995) ISSN: 0006-3002 [Print] Netherlands
• PMID: 7827138 (Publication Type: Journal Article)

Chemical References

• alpha-L-Fucosidase

Topics

• Cells, Cultured
• Fibroblasts (enzymology, pathology)
• Humans
• Isoelectric Focusing
• Lysosomal Storage Diseases (enzymology, pathology)
• Skin (embryology, enzymology)
• alpha-L-Fucosidase (chemistry)