Summaryiduronide 2-sulfate sulfatase, sulfamidase, and arylsulfatase B (Nacetylgalactosamine 4-sulfate sulfatase) were assayed in four muFibroblasts of four patients affected with mucosulfatidosis (mul-cosulfatidosis fibroblast lines using natural substrates.tiple sulfatase deficiency, Austin variant of metachromatic leukodystrophy) were assayed for activities of the five sulfatases known to degrade mucopolysaccharides. These were iduronide 2-sulfate sulfatase, sulfamidase, N-acetyl-galactosamine 6-sulfate sulfatase, (specific activity 27 mCi/mmole) from hen oviduct (lo), the monosulfated tri-saccharide N-acetylgalactosamine 6-sulfate Speculation (GlcNAC (6s)) D-glucuronic acid (G1cu~)-[1-3H]anhydromannit01 (specific activity 68.8 mCi/mmole) prepared from heparin Mucosulfatidosis is a disease characterized by the deficiency of sulfate (9), and the disulfated trisaccharide GalNAc(6S)-GlcUAmultiple sulfatases in cultured fibroblasts in contrast to the defi-~-acet~l-[l-~H]galactosaminitol(6S) (specific activity 24.9 mCi/ ciencies of singe sulfatases that are known for the five mucopoly-mmole) prepared from chondroitin 6-sulfate (12) were obtained saccharide degrading sulfatases and arylsulfatase A. The genes as described. responsible for the expression of the sulfatases are located both on autosomes and the X-chromosomes. Mucosulfatidosis fibroblasts should provide an experimental model for the study of a PATIENTS hitherto unknown common mechanism responsible for the exPresSkin biopsies or fibroblast cultures from patients with mucosulsion of sulfatase activities. fatidosis were kindly provided by Drs. J. Couchot (Reims), cell line 1, U. Wiesmann (Bern), cell line 2, and M. Niermeijer Mucosulfatidosis is a lysosomal storage disease characterized by (Rotterdam), line 3. line (GM 2407)9 was from the storage of sulfatides, glycosaminoglycans, and steroid sulfates. the Human Genetic Mutant Camden* N.J.The storage is caused by the deficiency of multiple sulfatases (for review, see refs. I and 2). In fibroblasts and tissues so far the METHODS deficiency of arylsulfatases A, B, and C, cholesteryl sulfatase and dehydroepiandrosterone sulfatase are known (3,4). It is, however, Cell Culture. Human skin fibroblasts from normal individuals still unclear whether activities of arylsulfatase C and the steroid and from patients of various genotypes were cultured in 25 cm2 sulfatases reside in the same enzyme or whether different enzymes Falcon plastic flasks with Eagle's Minimal Essential Medium (18) catalyze these reactions (2). Furthermore, mucosulfatidosis fibro-containing 10% fetal calf serum (LS-Labor Service, Miinchen), blasts do not correct the deranged mucopolysaccharide catabolism nonessential amino acids, and antibiotics as described previously in fibroblasts derived from patients affected with Hunter or Sari-(14). Cultures grown to confluency were harvested by trypsinizafilippo A syndrome which implies that mucosulfatidosis fibre-tion, the cells were washed twice with 0.15 M NaCI, and cell blasts are deficient in iduron...

The plasma levels of corticosterone, insulin and glucagon, and the concomitant changes in the levels of several liver enzymes and metabolites were measured in intact rats in the basal state during 24 hours and under conditions of food deprivation and hypoxia. The levels of the following enzymes and metabolites were examined: phosphoenolpyruvate carboxykinase, glucose-6-phosphatase, pyruvate kinase, phosphofructokinase, glutamic-oxaloacetic transaminase, glutamic-pyruvic transaminase, glucose, glucose-6-phosphate, glycogen, fructose-6-phosphate, hexokinase, tyrosine amino-transferase and tryptophan oxygenase. During food deprivation, the increased gluconeogenesis is possibly a result of glucagon activity. In contrast, however, during hypoxia the increase in gluconeogenesis seems to be a result of the higher plasma level of corticosterone. During starvation, the insulin concentration dropped steadily and came close to zero.

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The coenzyme nicotinamide adenine dinucleotide (NADH) has been used in an open label trial as novel medication in 34 patients with Parkinson's disease, using an intravenous administration technique. In all patients a beneficial clinical effect was observed. 21 patients (61.7%) showed a very good (better than 30%) improvement of disability, 13 patients (38.3%) a moderate (up to 30%) improvement. Concomitant with the improvement of the disability the urine level of homovanillic acid (HVA) increased significantly in all patients (in some patients by more than a 100%). The daily "on phases" of the patients could be increased from 2 up to 9 hours in the individual patients by NADH administration.