Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P04040 (Catalase)
 3,577 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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-alpha-hydroxyacid oxidase and E-aminoacid oxidase. Catalase is also not deficient in homogenates of cultured 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.
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PMID:Activity of peroxisomal enzymes and intracellular distribution of catalase in Zellweger syndrome. 614 39

Diabetes is a multifactorial disease that has now been recognized to involve overproduction of reactive oxygen species and pro-inflammatory cytokines. Peroxisomes are subcellular organelles with several important metabolic functions, and their role in the regulation of cellular oxidative stress is now well established. Despite having their own antioxidant system, peroxisomes undergo functional alterations during various conditions that are associated with free radical production such as inflammation, ischemia-reperfusion, carcinogenesis and diabetes. In this study we investigated the effect of diabetes on peroxisomal functions in rat kidneys and show for the first time that experimental diabetes induces redox-sensitive enhancement of peroxisomal activities. Streptozotocin-induced diabetes significantly increased (p < 0.01) beta-oxidation of lignoceric acid and the enzymic activity of acyl coenzyme A oxidase. Catalase activity was significantly reduced (p < 0.01) in the kidneys of diabetic rats, whereas the enzymic activity of DHAPATase (dihydroxyacetone phosphate acyltransferase) was not markedly affected by diabetes. Treatment of diabetic rats with antioxidants, thiocetic acid and vitamin C attenuated the diabetes-induced modulation of peroxisomal functions. The present study shows that the diabetes-induced effects on kidney peroxisomal functions are redox sensitive, and antioxidants might prove useful tools to alleviate nephropathy in diabetes.
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PMID:Antioxidants attenuate diabetes-induced activation of peroxisomal functions in the rat kidney. 1531 30