Synthesis and stability of arylsulfatase A and B in fibroblasts from multiple sulfatase deficiency.
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.
Steckel
F
F
Hasilik
A
A
von Figura
K
K
D000345:Affinity Labels; D002553:Cerebroside-Sulfatase / Q000096:biosynthesis*; D011232:Chemical Precipitation; D002803:Chondro-4-Sulfatase / Q000096:biosynthesis*; D005347:Fibroblasts / Q000201:enzymology; D006801:Humans; D007120:Immunochemistry; D008247:Lysosomes / Q000201:enzymology; D013429:Sulfatases / Q000096:biosynthesis* / Q000172:deficiency*
D000345:Affinity Labels; D013429:Sulfatases; D002553:Cerebroside-Sulfatase; D002803:Chondro-4-Sulfatase