Literature DB >> 8863047

In situ heterogeneity of peroxisomal oxidase activities: an update.

R J Van den Munckhof1.   

Abstract

Oxidases are a widespread group of enzymes. They are present in numerous organisms and organs and in various tissues, cells, and subcellular compartments, such as mitochondria. An important source of oxidases, which is investigated and discussed in this study, are the (micro)peroxisomes. Oxidases share the ability to reduce molecular oxygen during oxidation of their substrate, yielding an oxidized product and hydrogen peroxide. Besides the hydrogen peroxide-catabolizing enzyme catalase, peroxisomes contain one or more hydrogen peroxide-generating oxidases, which participate in different metabolic pathways. During the last four decades, various methods have been developed and elaborated for the histochemical localization of the activities of these oxidases. These methods are based either on the reduction of soluble electron acceptors by oxidase activity or on the capture of hydrogen peroxide. Both methods yield a coloured and/or electron dense precipitate. The most reliable technique in peroxisomal oxidase histochemistry is the cerium salt capture method. This method is based on the direct capture of hydrogen peroxide by cerium ions to form a fine crystalline, insoluble, electron dense reaction product, cerium perhydroxide, which can be visualized for light microscopy with diaminobenzidine. With the use of this technique, it became clear that oxidase activities not only vary between different organisms, organs, and tissues, but that heterogeneity also exists between different cells and within cells, i.e. between individual peroxisomes. A literature review, and recent studies performed in our laboratory, show that peroxisomes are highly differentiated organelles with respect to the presence of active enzymes. This study gives an overview of the in situ distribution and heterogeneity of peroxisomal enzyme activities as detected by histochemical assays of the activities of catalase, and the peroxisomal oxidases D-amino acid oxidase, L-alpha-hydroxy acid oxidase, polyamine oxidase and uric acid oxidase.

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Year:  1996        PMID: 8863047     DOI: 10.1007/bf02331433

Source DB:  PubMed          Journal:  Histochem J        ISSN: 0018-2214


  280 in total

1.  Microbodies (peroxisomes) containing catalase in myocardium: morphological and biochemical evidence.

Authors:  V Herzog; H D Fahimi
Journal:  Science       Date:  1974-07-19       Impact factor: 47.728

2.  Cytochemical detection of catalase with 3,3'-diaminobenzidine. A quantitative reinvestigation of the optimal conditions.

Authors:  M LeHir; V Herzog; H D Fahimi
Journal:  Histochemistry       Date:  1979-11

Review 3.  Ultrastructural aspects of the biogenesis of peroxisomes in rat liver.

Authors:  H D Fahimi; E Baumgart; A Völkl
Journal:  Biochimie       Date:  1993       Impact factor: 4.079

4.  An electron microscopic and enzymic study of rat liver peroxisomal nucleoid core and its association with urate oxidase.

Authors:  G F Lata; F Mamrak; P Bloch; B Baker
Journal:  J Supramol Struct       Date:  1977

5.  Oxidation of spermidine and spermine in rat liver: purification and properties of polyamine oxidase.

Authors:  E Hölttä
Journal:  Biochemistry       Date:  1977-01-11       Impact factor: 3.162

Review 6.  Towards the physiological function of uric acid.

Authors:  B F Becker
Journal:  Free Radic Biol Med       Date:  1993-06       Impact factor: 7.376

7.  Firefly luciferase is targeted to peroxisomes in mammalian cells.

Authors:  G A Keller; S Gould; M Deluca; S Subramani
Journal:  Proc Natl Acad Sci U S A       Date:  1987-05       Impact factor: 11.205

8.  Use of 1-methoxy-5-methylphenazinium methyl sulfate (1-methoxyPMS) in the assay of some enzymes of diagnostic importance.

Authors:  S Nakamura; K Arimura; K Ogawa; T Yagi
Journal:  Clin Chim Acta       Date:  1980-02-28       Impact factor: 3.786

Review 9.  Polyamine metabolism and function.

Authors:  A E Pegg; P P McCann
Journal:  Am J Physiol       Date:  1982-11

10.  Formalin fixation in the cytochemical demonstration of succinic dehydrogenase of mitochondria.

Authors:  D G WALKER; A M SELIGMAN
Journal:  J Biophys Biochem Cytol       Date:  1961-02
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  2 in total

1.  Activation of flavin-containing oxidases underlies light-induced production of H2O2 in mammalian cells.

Authors:  P E Hockberger; T A Skimina; V E Centonze; C Lavin; S Chu; S Dadras; J K Reddy; J G White
Journal:  Proc Natl Acad Sci U S A       Date:  1999-05-25       Impact factor: 11.205

2.  Identification and characterization of autoantibodies against catalase and alpha-enolase in patients with primary sclerosing cholangitis.

Authors:  T Orth; R Kellner; O Diekmann; J Faust; K H Meyer zum Büschenfelde; W J Mayet
Journal:  Clin Exp Immunol       Date:  1998-06       Impact factor: 4.330

  2 in total

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