Activity of peroxisomal enzymes and intracellular distribution of catalase in Zellweger syndrome

• Published in: Biochemical and biophysical research communications Vol. 123; no. 3; pp. 1054 - 1061
• Main Authors: Wanders, R.J.A., Kos, M., Roest, B., Meijer, A.J., Schrakamp, G., Heymans, H.S.A., Tegelaers, W.H.H., van den Bosch, H., Schutgens, R.B.H., Tager, J.M.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 28.09.1984
• Subjects: Acyltransferases - metabolism; Alcohol Oxidoreductases - metabolism; Brain Diseases - enzymology; Catalase - metabolism; Cells, Cultured; D-Amino-Acid Oxidase - metabolism; Digitonin - pharmacology; Fibroblasts - enzymology; Humans; Kidney Diseases - enzymology; Kinetics; Liver Diseases - enzymology; Microbodies - metabolism; Skin - enzymology; Syndrome
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/S0006-291X(84)80240-5

The activity of peroxisomal enzymes was studied in human liver and cultured human skin fibroblasts in relation to the finding (Goldfischer, S. et al. (1973) Science 182, 62–64) that morphologically distinct peroxisomes are not detectable in patients with the cerebro-hepato-renal (Zellweger) syndrome. In homogenates of liver from the patients, dihydroxyacetone phosphate acyltransferase, a membrane-bound peroxisomal enzyme, is deficient (Schutgens, R.B.H., et al. (1984) Biochem. Biophys. Res. Commun. 120, 179–184). In contrast, there is no deficiency of the soluble peroxisomal matrix enzymes catalase, L-α-hydroxyacid oxidase and D-aminoacid oxidase. Catalase is also not deficient in homogenates of cultered skin fibroblasts from the patients. The results of digitonin titration experiments showed that in control fibroblasts at least 70% of the catalase activity is present in subcellular particles distinct from mitochondria or lysosomes. In contrast, all of the catalase activity in fibroblasts from Zellweger patients is found in the same compartment as the cytosolic marker enzyme lactate dehydrogenase.