Peroxisomes and reactive oxygen species, a lasting challenge

Oxidases generating and enzymes scavenging H₂O₂ predestine peroxisomes (PO) to a pivotal organelle in oxygen metabolism. Catalase, the classical marker enzyme of PO, exhibits both catalatic and peroxidatic activity. The latter is responsible for the staining with 3,3'-diamino-benzidine, which g...

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Bibliographic Details
Published in:Histochemistry and cell biology 2009-04, Vol.131 (4), p.459-463
Main Authors: Angermüller, Sabine, Islinger, Markus, Völkl, Alfred
Format: Article
Language:English
Subjects:
Animals
Biochemistry
Biomedical and Life Sciences
Biomedicine
Catalase - metabolism
Cell Biology
Cellular biology
Developmental Biology
Enzymes
Histology
Hydrogen
Hydrogen Peroxide - metabolism
Kidney - enzymology
Kidney - ultrastructure
Liver - enzymology
Liver - ultrastructure
Molecular biology
Oxidoreductases - metabolism
Oxygen
Peroxisomes - enzymology
Peroxisomes - ultrastructure
Rats
Reactive Oxygen Species - metabolism
Review
Superoxide Dismutase - metabolism
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Summary:Oxidases generating and enzymes scavenging H₂O₂ predestine peroxisomes (PO) to a pivotal organelle in oxygen metabolism. Catalase, the classical marker enzyme of PO, exhibits both catalatic and peroxidatic activity. The latter is responsible for the staining with 3,3'-diamino-benzidine, which greatly facilitated the visualization of the organelle and promoted further studies on PO. d-Amino acid oxidase catalyzes with strict stereospecificity the oxidative deamination of d-amino acids. The oxidase is significantly more active in the kidney than in liver and more in periportal than pericentral rat hepatocytes. Peroxisomes in these tissues differ in their enzyme activity and protein concentration not only in adjacent cells but even within the same one. Moreover, the enzyme appears preferentially concentrated in the central region of the peroxisomal matrix compartment. Urate oxidase, a cuproprotein catalyzing the oxidation of urate to allantoin, is confined to the peroxisomal core, yet is lacking in human PO. Recent experiments revealed that cores in rat hepatocytes appear in close association with the peroxisomal membrane releasing H₂O₂ generated by urate oxidase to the surrounding cytoplasma. Xanthine oxidase is exclusively located to cores, oxidizes xanthine thereby generating H₂O₂ and O₂ ⁻ radicals. The latter are converted to O₂ and H₂O₂ by CuZn superoxide dismutase, which has been shown recently to be a bona fide peroxisomal protein.
ISSN:0948-6143
1432-119X
DOI:10.1007/s00418-009-0563-7