Ultrastructural localization of catalase and D-amino acid oxidase in ‘normal’ fetal mouse liver

Dabholkar, Arun S.

doi:10.1007/bf01952437

Cited by 14 publications

(5 citation statements)

References 19 publications

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“…8 We, therefore, examined whether G72 can function as a physiological regulator of DAO activity in mammalian cells, as originally suggested. In agreement with previous reports, 27,28 we found that in Cos7 cells transfected with an expression construct containing flag-tagged human DAO, the enzyme is predominantly targeted to peroxisomes ( Figure 6A, a-c) with no evidence of mitochondrial localization ( Figure 6A, d-f). G72 does not colocalize with the peroxisomal marker PMP70 ( Figure 6A, g-i), and in cotransfection experiments we could not demonstrate colocalization with DAO ( Figure 6A, j-l).…”

Section: Increase In G72 Levels Results In Mitochondrial Fragmentatiosupporting

confidence: 93%

Evidence implicating the candidate schizophrenia/bipolar disorder susceptibility gene G72 in mitochondrial function

et al. 2007

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G72 is a strong candidate susceptibility gene for schizophrenia and bipolar disorder, whose function remains enigmatic. Here we show that one splicing isoform of the gene (LG72 ) encodes for a mitochondrial protein. We also provide convergent lines of evidence that increase of endogenous or exogenous G72 levels promotes robust mitochondrial fragmentation in mammalian cell lines and primary neurons, which proceeds in a manner that does not depend on induction of apoptosis or alteration in mitochondrial transmembrane potential. Finally, we show that increase in G72 levels in immature primary neurons is accompanied by a marked increase in dendritic arborization. By contrast, we failed to confirm the originally proposed functional interaction between G72 and D-amino acid oxidase (DAO) in two tested cell lines. Our results suggest an alternative role for G72 in modulating mitochondrial function.

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Section: Increase In G72 Levels Results In Mitochondrial Fragmentatiosupporting

confidence: 93%

Evidence implicating the candidate schizophrenia/bipolar disorder susceptibility gene G72 in mitochondrial function

et al. 2007

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“…64,2007 Review Article expression pattern observed in other animal species, no evidence of the presence of the DAAO mRNA, or of DAAO activity [139], was found in other tissues. Although the enzyme activity has been detected in hepatocytes from mouse fetuses [140], it disappears during the developmental stage and cannot be detected in the liver of the adult animals. During postnatal development, the transcriptional level of DAAO in the kidney and skeletal muscle reached the adult level at day 21, when it was also high in cerebellum [139].…”

Section: Daao Activity In Mammalsmentioning

confidence: 95%

Physiological functions of D-amino acid oxidases: from yeast to humans

Pollegioni

Piubelli

Sacchi

et al. 2007

Cell. Mol. Life Sci.

320

304

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D-Amino acid oxidase (DAAO) is a FAD-containing flavoenzyme that catalyzes the oxidative deamination of D-isomers of neutral and polar amino acids. This enzymatic activity has been identified in most eukaryotic organisms, the only exception being plants. In the various organisms in which it does occur, DAAO fulfills distinct physiological functions: from a catabolic role in yeast cells, which allows them to grow on D-amino acids as carbon and energy sources, to a regulatory role in the human brain, where it controls the levels of the neuromodulator D-serine. Since 1935, DAAO has been the object of an astonishing number of investigations and has become a model for the dehydrogenase-oxidase class of flavoproteins. Structural and functional studies have suggested that specific physiological functions are implemented through the use of different structural elements that control access to the active site and substrate/product exchange. Current research is attempting to delineate the regulation of DAAO functions in the contest of complex biochemical and physiological networks.

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“…Horiike et al, 1985 (IHC/DAB/HRP)) mouse kidney (Wohlrab, 1965 (TSR)) guinea pig kidney (Wohlrab, 1965 (TSR)) rabbit kidney (Wohlrab, 1965 (TSR)) sheep kidney (Wohlrab, 1965 (TSR)) cat kidney (Wohlrab, 1965 (TSR)) dog kidney (Wohlrab, 1965 (TSR)) mink kidney (Wohlrab, 1965 (TSR)) hog kidney (Wohlrab, 1965 (TSR)) hog brain (Weimar & Neims, 1977 (IHC/AEC/HRP)) bovine liver (Angermfiller, 1989 (DHC)) bovine kidney (Angermi]ller, 1989 (DHC)) mouse liver (Dabholkar, 1986) teleost kidney (Veenhuis & Wendelaar Bonga, 1977 (DHC)) yeast (Veenhuis et al, 1976 (DHC)(IHC/DAB/CAT)) L-c~-hydroxy acid oxidase) protein rat kidney (Yokota et al, 1985) human liver (Angermfiller, 1989) rat liver (Usuda et aL, 1991) rat kidney (Yokota et aL, 1985(Yokota et aL, , 1987 mouse liver (Angermfiller, 1989) activity rat liver (Hand, 1975 (FCR); Angermiiller et al, 1986a (DHC); Angermfller and Fahimi, 1988b (DHC)) rat kidney (Allen et al, 1965 (TSR), (IHC/AEC/HRP); Beard & Novikoff, 1969 (TSR); Shnitka & Talibi, 1971 (TSR);…”

Section: L-c(-hydroxy Acid Oxidasementioning

confidence: 99%

In situ heterogeneity of peroxisomal oxidase activities: An update

Munchof

1996

Histochem J

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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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Ultrastructural localization of catalase and D-amino acid oxidase in ‘normal’ fetal mouse liver

Cited by 14 publications

References 19 publications

Evidence implicating the candidate schizophrenia/bipolar disorder susceptibility gene G72 in mitochondrial function

Evidence implicating the candidate schizophrenia/bipolar disorder susceptibility gene G72 in mitochondrial function

Physiological functions of D-amino acid oxidases: from yeast to humans

In situ heterogeneity of peroxisomal oxidase activities: An update

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