<scp>d</scp>-aspartate oxidase in rat, bovine and sheep kidney cortex is localized in peroxisomes

Zaar, K; Völkl, Alfred; Fahimi, H. Dariush

doi:10.1042/bj2610233

Cited by 40 publications

(24 citation statements)

References 31 publications

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“…In an earlier biochemical study (Zaar et al 1989), we demonstrated that, in all steps of a subcellular fractionation procedure for kidney cortex homogenates, D-ASPOX activity co-fractionates with peroxisomal marker enzymes. Specific D-ASPOX activity in different species was highest in a peroxisome fraction purified from bovine kidney cortex.…”

Section: Immunoblot Analysis Of Bovine Renal D-aspoxmentioning

confidence: 73%

“…Using highly purified peroxisome preparations from beef, sheep, and rat kidney cortex, as well as rat liver, we demonstrated first that D-ASPOX in these tissues is a peroxisomal enzyme located in the matrix of peroxisomes (Zaar et al, 1989). This peroxisomal localization was later confirmed in isolated organelle fractions from rat and human liver by Van Veldhoven et al (1991).…”

Section: Introductionmentioning

confidence: 73%

“…No significant labcling could be observed in other tubule segments (Figures 3a and 3c). D-ASPOX activity has also been found in purified peroxisome fractions from rat and human liver (Van Veldhoven et al, 1991: Zaar et al, 1989. After incubation of floating cryostat sections of bovine liver tissue with anti-D-ASPOX a granular localization was also found in hepatocytes (Figure 3d).…”

Section: Immunohistochemistrymentioning

confidence: 83%

“…D-ASPOX activity was determined by measuring hydrogen peroxide production from D-aspartate (Sigma Chemical; St Louis, MO) according to Osumi and Hashimoto (1978). Sodium benzoate was used as a potent inhibitor for D-AAOX activity (Zaar et al, 1989).…”

Section: Biochemical Studiesmentioning

confidence: 99%

“…Light mitochondrial (D)-fractions from porcine and bovine kidney cortex, as well as a highly purified peroxisome fraction from bovine kidney cortex, were isolated essentially according to the method described earlier by Zaar et al (1989) and were used for characterization of D-ASPOX in Western blots. SDSPAGE and Immunoblotting.…”

Section: Biochemical Studiesmentioning

confidence: 99%

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Light and electron microscopic localization of D-aspartate oxidase in peroxisomes of bovine kidney and liver: an immunocytochemical study.

Zaar

1996

J Histochem Cytochem.

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D-Aspartate oxidase (EC 1.4.3.1; D-ASPOX) specifically oxidizes the D-isomers of dicarboxylic amino acids such as aspartic or glutamic acid. Subcellular fractionation experiments in the past showed its association with peroxisome preparations in kidney cortex and liver. However, no information exists on the in situ localization and distribution of the enzyme in different cell types. We have purified the enzyme from the bovine kidney and raised an antibody against it in rabbits. The monospecificity of the antibody has been confirmed by Western blotting and it does not crossreact with D-amino, acid oxidase. Immunohistochemical localization of the antigen in bovine kidney and liver with the streptavidin-biotin-peroxidase technique revealed a punctate localization in the epithelial cells of proximal nephron tubules, particularly in the straight P-3 segment, as well as in hepatocytes. This is consistent with a localization in peroxisomes. Best results have been obtained with Carnoy-fixed material after paraffin embedding or after fixation with formaldehyde-glutaraldehyde in cryostat sections. Immunoelectron microscopy with protein A-gold confirms the peroxisomal localization of D-ASPOX. Gold particles are distributed over the matrix, suggestive of a peroxisomal matrix enzyme. This is the first report on the localization of D-ASPOX, a little-known peroxisomal enzyme. The techniques described and the antibody prepared will now allow systematic investigation of its tissue distribution.

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Section: Immunoblot Analysis Of Bovine Renal D-aspoxmentioning

confidence: 73%

Section: Introductionmentioning

confidence: 73%

Section: Immunohistochemistrymentioning

confidence: 83%

Section: Biochemical Studiesmentioning

confidence: 99%

Section: Biochemical Studiesmentioning

confidence: 99%

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Light and electron microscopic localization of D-aspartate oxidase in peroxisomes of bovine kidney and liver: an immunocytochemical study.

Zaar

1996

J Histochem Cytochem.

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D‐Aspartate Oxidase: The Sole Catabolic Enzyme Acting on Free D‐Aspartate in Mammals

Katane

Homma

2010

Chemistry & Biodiversity

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Comparative Characterization of Three D‐Aspartate Oxidases and One D‐Amino Acid Oxidase from Caenorhabditis elegans

Katane

Saitoh

Seida

et al. 2010

Chemistry & Biodiversity

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Previously, we cloned cDNAs for four Caenorhabditis elegans genes (F20 Hp, C47Ap, F18Ep, and Y69Ap genes) that were annotated in the database as encoding D-amino acid oxidase (DAO) or D-aspartate oxidase (DDO) proteins. These genes were expressed in Escherichia coli, and the recombinant C47Ap and F18Ep were shown to have functional DDO activities, while Y69Ap had functional DAO activity. In this study, we improved the E. coli culture conditions for the production of recombinant F20 Hp and, following purification of the protein, revealed that it has functional DDO activity. The kinetic properties of recombinant C47Ap (DDO-1), F18Ep (DDO-2), F20 Hp (DDO-3), and Y69Ap (DAO) were also determined and compared with recombinant human DDO and DAO. In contrast to the low catalytic efficiency of human DDO for D-Glu, all three C. elegans DDOs showed higher catalytic efficiencies for D-Glu than D-Asp or N-methyl-D-Asp. The catalytic efficiency of C. elegans DAO for D-Ser was substantially lower than that of human DAO, while the C. elegans DAO was more efficient at deamination of basic D-amino acids (D-Arg and D-His) than human DAO. Collectively, our results indicate that C. elegans contains at least three genes that encode functional DDOs, and one gene encoding a functional DAO, and that these enzymes have different and distinctive properties.

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d-aspartate oxidase in rat, bovine and sheep kidney cortex is localized in peroxisomes

Cited by 40 publications

References 31 publications

Light and electron microscopic localization of D-aspartate oxidase in peroxisomes of bovine kidney and liver: an immunocytochemical study.

Light and electron microscopic localization of D-aspartate oxidase in peroxisomes of bovine kidney and liver: an immunocytochemical study.

D‐Aspartate Oxidase: The Sole Catabolic Enzyme Acting on Free D‐Aspartate in Mammals

Comparative Characterization of Three D‐Aspartate Oxidases and One D‐Amino Acid Oxidase from Caenorhabditis elegans

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