Synthesis and stability of arylsulfatase A and B in fibroblasts from multiple sulfatase deficiency.

Abstract

Fibroblasts from patients with multiple sulfatase deficiency were analyzed for activities of arylsulfatase A and B, iduronate 2-sulfatase and sulfamatase. A group of patients (group I) severely deficient in all sulfatases (residual activities less than or equal to 10% of control) were differentiated from patients (group II) with residual sulfatase activities of up to 90% of control. The synthesis and stability of arylsulfatase A and B were determined in pulse-chase labelling experiments. The apparent rate of synthesis of arylsulfatase A and B varied from 30% to normal in both fibroblasts from group I and II multiple sulfatase deficiency. In group I the molecular activity of the arylsulfatase A and B was more than 10-fold lower than in control fibroblasts. In group II the molecular activity of the arylsulfatase A was twofold to threefold lower and that of arylsulfatase B half of normal. In fibroblasts of both groups the stability of arylsulfatase A polypeptides was significantly diminished. For arylsulfatase B the instability was restricted to the mature 47000-Mr polypeptide and was variable within both groups. These results demonstrate that multiple sulfatase deficiency is a heterogeneous disorder, in which the primary defects can impair both the catalytic properties and the stability of sulfatases.

• Authors: F Steckel, A Hasilik, K von Figura
• Journal: European journal of biochemistry (Eur J Biochem) Vol. 151 Issue 1 Pg. 141-5 (Aug 15 1985) ISSN: 0014-2956 [Print] England
• PMID: 2863138 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Affinity Labels
• Sulfatases
• Cerebroside-Sulfatase
• Chondro-4-Sulfatase

Topics

• Affinity Labels
• Cerebroside-Sulfatase (biosynthesis)
• Chemical Precipitation
• Chondro-4-Sulfatase (biosynthesis)
• Fibroblasts (enzymology)
• Humans
• Immunochemistry
• Lysosomes (enzymology)
• Sulfatases (biosynthesis, deficiency)