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

Wanders, Ronald J. A.; Kos, Milan; Roest, B.; Meijer, Alfred J.; Schrakamp, G.; Heymans, H. S. A.; Tegelaers, W. H. H.; Bosch, H. van den; Schutgens, R. B. H.; Tager, J. M.

doi:10.1016/s0006-291x(84)80240-5

Cited by 204 publications

(93 citation statements)

References 22 publications

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“…2). The small amount of soluble enzyme in control and RCDP fibroblasts is in the range previously reported for controls (26,43), and may be due to breakage of some peroxisomes under the experimental conditions, or may represent newly synthesized enzyme in the cytosol, which has not yet transported to the peroxisomes. The authentic existence of extraperoxisomal catalase has been demonstrated in the liver of several mammalian species by cytochemistry and by immunoelectron microscopy (44-46).…”

Section: B O T T O Mmentioning

confidence: 47%

Aberrant Subcellular Localization of Peroxisomal 3-Ketoacyl-CoA Thiolase in the Zellweger Syndrome and Rhizomelic Chondrodysplasia Punctata

et al. 1990

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ABSTRACT. Fibroblasts from patients with the inherited disorder Zellweger syndrome have few or no peroxisomes; multiple biochemical processes that normally occur in this organelle are defective. Rhizomelic chondrodysplasia punctata (RCDP) is another inherited disorder in which two unrelated peroxisomal metabolic processes, plasmalogen synthesis and phytanic acid oxidation, are impaired despite the normal appearance of peroxisomal structure. It was previously reported that one of the enzymes of peroxisomal fatty acid ,f3-oxidation, 3-ketoacyl-CoA thiolase (P-ketothiolase), was present in precursor rather than mature form in both of these diseases. Immunofluorescent staining for peroxisomal ,f3-ketothiolase showed the immunoreactivity to be localized in subcellular particles in fibroblasts from both Zellweger syndrome and RCDP patients, even though the former lack normal peroxisomes. Immunoblot studies were performed to determine the subcellular location of the thiolase precursor in fractionated fibroblasts from Zellweger and RCDP patients. In both disorders, thiolase immunoreactivity was detected in subcellular fractions having a lower density than normal peroxisomes and mitochondria, and was resistant to digestion by proteinase K.

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Section: B O T T O Mmentioning

confidence: 47%

Aberrant Subcellular Localization of Peroxisomal 3-Ketoacyl-CoA Thiolase in the Zellweger Syndrome and Rhizomelic Chondrodysplasia Punctata

et al. 1990

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“…peroxisome have little activity (4)(5)(6)(7)(8)(9). When patients with Zellweger syndrome and hyperpipecolic acidemia were given oral loading doses of pipecolic acid, their serum pipecolic acid levels were elevated for a prolonged period of time relative to controls (10)(11)(12)(13)(14).…”

mentioning

confidence: 99%

Peroxisomal L-Pipecolic Acid Oxidation Is Deficient in Liver from Zellweger Syndrome Patients

Mihalik

Moser²,

Watkins³

et al. 1989

Pediatr Res

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“…This suggests that further improvements of the presently available immunocytochemical methods may be useful for the detection of the nascent peroxisomal enzyme antigens in the cytoplasm. This is of particular interest because in patients with Zellweger syndrome, whose hepatocytes lack morphologically identifiable peroxisomes, most of the catalase is present in the cytosolic compartment (16,43). To the best of our knowledge, however, the exact immunocytochemical localization of the cytosolic catalase in the liver of patients with Zeliweger syndrome has not yet been reported.…”

Section: Discussionmentioning

confidence: 99%

Biogenesis of peroxisomes in regenerating rat liver. II. Immunoelectron microscopical investigation of catalase and acylCoA oxidase.

Yamamoto

Völkl

Fahimi

1989

Acta Histochem. Cytochem

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The intracellular localization of two peroxisomal enzymes, catalase and acylCoA oxidase, in regenerating rat liver after partial hepatectomy has been investigated by means of postembedding protein A-gold immunocytochemical technique. The peroxisomes in regenerating rat liver underwent marked changes in shape and size as revealed by catalase cytochemistry with DAB. By immunoelectron microscopy, all peroxisomes, irrespective of size and configuration were strongly positive for catalase showing numerous gold particles distributed over their matrix sparing the electron dense nucleoid region. Sections incubated with the monospecific antibody against acyl-CoA oxidase showed essentially a similar distribution of gold particles, although the labeling density was weaker than with catalase. In all sections the endoplasmic reticulum and the Golgi complex were negative for both catalase and acyl-CoA oxidase, thus ruling out any involvement of the secretory apparatus in the biosynthesis of those proteins. The uniform distribution of catalase and acyl-CoA oxidase in all peroxisomes (presumably new and old) is consistent with the concept of transfer of matrix proteins from preexisting particles to new ones.In addition to the localization of catalase in the matrix of peroxisomes, some gold particle aggregates were also noted apparently on ribosomes in the cytoplasmic matrix.Serial section analysis, however, revealed that all cytoplasmic labeling was due to tangentially sectioned peroxisomes, especially those with abnormal shapes. Our observations suggest that the concentration of nascent peroxisomal proteins in the cytoplasm of rat liver cells under physiological conditions is too low to be detectable by the presently available immunocytochemical techniques.The model of regenerating rat liver after partial hepatectomy (PH) has been used extensively for the investigation of the problem of biogenesis of peroxisomes (15,32,34,36,37,41). Based on observations in this model Novikoff and Shin suggested that peroxisomes originate by budding from the terminal cisternae of the endoplasmic reticulum (32). Subsequent biochemical studies, using an in vitro translation system, however, have clearly established that all peroxisomal proteins are synthesized on free * Present address of Dr .

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

Cited by 204 publications

References 22 publications

Aberrant Subcellular Localization of Peroxisomal 3-Ketoacyl-CoA Thiolase in the Zellweger Syndrome and Rhizomelic Chondrodysplasia Punctata

Aberrant Subcellular Localization of Peroxisomal 3-Ketoacyl-CoA Thiolase in the Zellweger Syndrome and Rhizomelic Chondrodysplasia Punctata

Peroxisomal L-Pipecolic Acid Oxidation Is Deficient in Liver from Zellweger Syndrome Patients

Biogenesis of peroxisomes in regenerating rat liver. II. Immunoelectron microscopical investigation of catalase and acylCoA oxidase.

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