Activities of sulfatases for the degradation of acidic glycosaminoglycans in cultured skin fibroblasts from two siblings with multiple sulfatase deficiency.
Cultured skin fibroblasts from two siblings with multiple sulfatase deficiency (MSD) were assayed for the activities of sulfatases known to degrade acidic glycosaminoglycans (AGAG). There were iduronate sulfatase, arylsulfatase B, heparan sulfate (HS) sulfatase, N-acetylgalactosamine-6-sulfate sulfatase, HS-derived N-acetylglucosamine-6-sulfate sulfatase, and two keratan sulfate (KS)-derived N-acetylglucosamine-6-sulfate sulfatases. The activities of sulfatases required for the degradation of HS were reduced to a greater extent than those for the degradation of dermatan sulfate (DS), and those of sulfatases associated with basic defect of Morquio disease type A were moderately decreased or normal. On the other hand, urinary excretion of AGAG in both patients was increased about 10-fold compared to controls, and especially, the excretion of HS and DS was increased about 150-fold and 50-fold, respectively. Keratan sulfate was not detected. The results suggest that in patients with MSD the degradation of HS might be affected to a greater extent than that of DS.
D002478:Cells, Cultured; D002648:Child; D002675:Child, Preschool; D005260:Female; D005347:Fibroblasts / Q000201:enzymology; D006025:Glycosaminoglycans / Q000378:metabolism* / Q000652:urine; D006801:Humans; D013429:Sulfatases / Q000172:deficiency / Q000378:metabolism*
D006025:Glycosaminoglycans; D013429:Sulfatases