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Pathochemistry, pathogenesis and enzyme replacement in multiple-sulfatase deficiency

Y Eto1, I Gomibuchi, F Umezawa

  • 1Department of Pediatrics, Tokyo Jikei University School of Medicine, Japan.

Enzyme
|January 1, 1987
PubMed

Insights

Multiple-sulfatase deficiency (MSD) is a heterogeneous disorder. In neonatal MSD, decreased arylsulfatase A activity stems from accelerated enzyme degradation, distinct from other forms.

Area of Science:

  • Biochemistry
  • Genetics
  • Metabolic Disorders

Background:

  • Multiple-sulfatase deficiency (MSD) presents with heterogeneous clinical phenotypes.
  • Neonatal MSD exhibits severe symptoms and minimal arylsulfatase A, B, and C activity in fibroblasts.
  • Neonatal MSD is distinguished from late infantile-type MSD by lack of thiosulfate enhancement of arylsulfatase A activity.

Purpose of the Study:

  • To investigate the underlying mechanisms of arylsulfatase A deficiency in neonatal MSD.
  • To explore potential therapeutic strategies for MSD using enzyme replacement and cell-based therapies.

Main Methods:

  • Cultured skin fibroblasts from MSD patients were used.
  • Enzyme activities (arylsulfatase A, B, C) and 14C-sulfatide degradation were measured.
  • Enzyme replacement therapy with human and fungal arylsulfatases was performed.
  • Leukocyte co-culture was utilized to assess therapeutic potential.

Main Results:

  • Degradation of 14C-sulfatide was significantly higher in MSD fibroblasts compared to late infantile-type MLD.
  • Leupeptin treatment enhanced arylsulfatase A activity and 14C-sulfatide degradation in MSD fibroblasts, suggesting accelerated enzyme degradation.
  • Human-derived arylsulfatases A and B were effectively taken up by MSD cells.
  • Co-culture with leukocytes corrected arylsulfatase A and B activities in MSD fibroblasts.

Conclusions:

  • Accelerated degradation of arylsulfatase A is a key factor in neonatal MSD.
  • Enzyme replacement with human arylsulfatases and leukocyte-based therapy show promise for treating MSD.

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