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On the compartmentalization of catalase, fatty acyl-CoA oxidase and urate oxidase in mammalian livers, and the influence of clofibrate treatment on this microlocalization

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Abstract

The compartmentalization of catalase, fatty acyl-CoA oxidase and urate oxidase was examined in the livers of mice, rats and guinea pigs, using the technique of digitonin extraction in order to avoid the trauma associated with centrifugation procedures. The results are interpreted as indicating that an appreciable proportion of catalase activity occurs in the cytoplasmic compartment of these cells. Following treatment of the animals with clofibrate, the specific activity in both peroxisomal and cytoplasmic compartments was increased, with a higher proportion of cytoplasmic catalase being evident in mice. The results for catalase were compared with those for fatty acyl-CoA oxidase and urate oxidase both of which were indicated as showing a closer association with the peroxisomal compartment than was the case for catalase. These data have been discussed in relation to their significance on present understanding of peroxisomal structure and function.

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References

  1. Poole B, Higashi T, De Duve C: Synthesis and turnover of rat liver peroxisomes III. Size distribution of peroxisomes and incorporation of new catalase. J Cell Biol 45:408–415, 1970

    Google Scholar 

  2. Lazarow PB, De Duve C: Synthesis and turnover of rat liver peroxisomes V. Intracellular pathway of catalase synthesis. J Cell Biol 59:507–524, 1973

    Google Scholar 

  3. Inestrosa NC, Bronfman M, Leighton F: Properties of fatty acyl-CoA oxidase from rat liver, a peroxisomal flavoprotein. Life Sci 25:1127–1135, 1979

    Google Scholar 

  4. Inestrosa NC, Bronfman M, Leighton F: Detection of peroxisomal fatty acyl-coenzyme-A oxidase activity. Biochem J 182:779–788, 1979

    Google Scholar 

  5. De Duve C, Baudhin P: Peroxisomes (microbodies and related particles). Physiol Rev 46:323–357, 1966

    PubMed  Google Scholar 

  6. Holmes RS, Masters CJ: Species specific features of distribution and multiplicity of mammalian liver catalase. Arch Biochem Biophys 148:217–223, 1972

    Google Scholar 

  7. Crane DI, Hemsley AC, Masters CJ: Purification of peroxisomes from livers of normal and clofibrate-treated mice. Anal Biochem 148:436–445, 1985

    Google Scholar 

  8. Klucis E, Masters CJ: An immunological investigation of catalase in three mammalian species. Biochem Int 8:513–519, 1984

    Google Scholar 

  9. Moody DE, Reddy JK: Hepatic effects of hypolipidemic drugs (clofibrate, nafenopin, tibric acic, and Wy-14,6–43) on hepatic peroxisomes and peroxisome-associated enzymes. Am J Pathol 90(2):435–445, 1978

    Google Scholar 

  10. Gray TJB, Beamand JA, Lake BG, Foster JR, Gangolli SD: Peroxisome proliferation in cultured rat hepatocytes produced by clofibrate and phthalate-ester metabolites. Toxicol Lett 10:273–279, 1982

    Google Scholar 

  11. Gray TJB, Lake BG, Beamand JA, Foster JR, Gangolli SD: Peroxisome proliferation in primary cultures of rat hepatocytes. Toxicol and Appl Pharmacol 67:15–25, 1983

    Google Scholar 

  12. Klucis E, Crane DI, Masters CJ: Sequential alterations in the micro-localization of catalase in mouse liver after treatment with hypolipidemic drugs. Mol Cell Biochem 65:73–82, 1984

    Google Scholar 

  13. Windaus A: Deduction of the toxicity of saponin by cholesterol. Ber Dtsch Chem Ges 42:238–246, 1909

    Google Scholar 

  14. Colbeau A, Nachbaur J, Vignais PM: Enzymic characterization and lipid composition of rat liver subcellular membranes. Biochim Biophys Acta 249:462–492, 1971

    Google Scholar 

  15. Zuurendonk PJ, Tager JM: Rapid separation of particulate components and soluble cytoplasm of isolated rat liver cells. Biochim Biophys Acta 333:393–399, 1973

    Google Scholar 

  16. Wanders RJA, Kos M, Roest B, Meijer AJ, Schrakamp G, Heymans HSA, Tegelaers WHH, van den Bosch H, Schutgens RBM, Tager JM: Enzymes and intracellulardistribution of catalase in Zellweger Syndrome. Biochem Biophys Res Comm 123:1054–1061, 1984

    Google Scholar 

  17. Zuurendonk PF, Tischler ME, Akerboom TPM, van der Meer R, Williamson JR, Tager JM: Rapid separation of particulate and soluble fractions from isolated cell preparations (Digitonin and cell cavitation procedures). Meth Enzymol 56:207–233, 1979

    Google Scholar 

  18. Davis RA, Engelhorn SC, Pangburn SH, Weinstein DB, Steinberg D: Very low-density lipoprotein synthesis and secretion by cultured rat hepatocytes. J Biol Chem 254:2010–2016, 1979

    Google Scholar 

  19. Crane DI, Holmes RS, Masters CJ: Synthesis and incorporation of phospholipid by peroxisomes of mouse liver. Biochim Biophys Acta 712:57–64, 1982

    Google Scholar 

  20. Walusiambi-Kisitu M, Harrison EH: Fluorometric assay for rat liver peroxisomal fatty aryl-coenzyme-A oxidase activity. J Lipid Res 24:1077–1084, 1983

    Google Scholar 

  21. Leighton F, Poole B, Beaufay H, Baudhuin P, Coffey JW Fowler S, De Duve C: Large-scale separation of peroxisomes, mitochondria, and lysosomes from livers of rats injected with Triton WR-1339-improved isolation procedures, automated analysis, biochemical and morphological properties of fractions. J Cell Biol 37:482–512, 1968

    Google Scholar 

  22. Peterson GL: A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal Biochem 83:346–356, 1977

    CAS  PubMed  Google Scholar 

  23. Janski AM, Cornell NW: Subcellular distribution of enzymes determined by rapid digitonin fractionation of isolated hepatocytes. Biochem J 186:423–429, 1980

    Google Scholar 

  24. Hruban Z, Swift H: Uricase: localization in hepatic microbodies. Science 146:1316–1318, 1964

    Google Scholar 

  25. Leighton F, Poole B, Lazarow PB, De Duve C: Synthesis and turnover of rat liver peroxisomes I. Fractionation of peroxisome proteins. J Cell Biol 41:521–535, 1969

    Google Scholar 

  26. Alexson SFH, Fujiki Y, Shio H, Lazarow PB: Partial disassembly of peroxisomes. J Cell Biol 101:294–305, 1985

    Google Scholar 

  27. Mackall J, Meredith M, Lane MD: A mild procedure for the rapid release of cytoplasmic enzymes from cultured animal cells. Anal Biochem 95:270–274, 1979

    Google Scholar 

  28. Fukami MH, Flatmark T: Studies on catalase compartmentation in digitonin-treated rat hepatocytes. Biochim Biophys Acta 889:91–94, 1986

    Google Scholar 

  29. Roels F: Cytochemical demonstration of extra-peroxisomal catalase I. Sheep liver. J Histochem Cytochem 24:713–724, 1976

    Google Scholar 

  30. Roels F, De Coster W, Goldfischer S: Cytochemical demonstration of extraperoxisomal catalase II Liver of Rhesusmonkey and Guinea-pig. J Histochem Cytochem 25:157–160, 1977

    Google Scholar 

  31. Geerts A, Roels F: Quantitation of catalase activity by microspectrophotometry after diaminobenzidine staining. Histochemistry 72:357–367, 1981

    Google Scholar 

  32. 32. Pegg M, Crane D, Masters CJ: Interactions of catalase with subcellular membranes. Biochem Intl (in press), 1988

  33. Yokota S, Fahimi HD: Immuno-cytochemical localization of catalase in rat liver. J Histochem Cytochem 29(7):805–812, 1981

    Google Scholar 

  34. Jones GL, Masters CJ: On the turnover and proteolysis of catalase in tissues of guinea pigs and acatalasemic mice. Arch Biochem Biophys 173:463–471, 1976

    Google Scholar 

  35. Geerts A, De Prest B, Roels F: On the topology of catalase biosynthesis and bio-degradation in the guinea-pig liver — a cytochemical study. Histochemistry 80:339–345, 1984

    Google Scholar 

  36. Feinstein RW, Faulhaber JT, Howard JB: Acatalasemia and hypocatalasemia in the dog and the duck. Proc Soc Exptl Biol Med 127:1051–1054, 1968

    Google Scholar 

  37. Aebi H, Suter H, Feinstein RN: Activity and stability of catalase in blood and tissues of normal and acatalasemic mice. Biochem Genet 2:245–251, 1968

    Google Scholar 

  38. Feinstein RW: Acatalasemia in the mouse and other species. Biochem Genet 4:135–155, 1970

    Google Scholar 

  39. Holmes RS: Catalase multiplicity in normal and acatalasemic mice. FEBS Letters 24:161–164, 1972

    Google Scholar 

  40. Zimniak P, Hartter E, Ruis H: Biosynthesis of catalase during oxygen adaptation of Saccharomyces cerevisiae. FEBS Letters 59:300–304, 1975

    Google Scholar 

  41. Zimniak P, Hartter E, Woloszczuk W, Ruis H: Catalase biosynthesis in yeast: formation of catalase A and catalase T during oxygen adaptation of Saccharomyces cerevisiae. Eur J Biochem 71:393–398, 1976

    Google Scholar 

  42. Masters CJ, Holmes RS: Peroxisomes: new aspects of cell physiology and biochemistry. Physiol Rev 57:816–882, 1977

    Google Scholar 

  43. Lazarow PB, Shio H, Robbi M: Biogenesis of Peroxisomes and the Peroxisome Reticulum Hypothesis. In 31st Mosbach Colloquium. Biological Chemistry of Organelle Formation. T Bucher, W Sebald and H Weiss, editors. Springer-Verlag, New York, 1980, pp. 187–206

    Google Scholar 

  44. Jones GL, Masters CJ: On the synthesis and degradation of the multiple forms of catalase in mouse liver. Arch Biochem Biophys 161:601–609, 1974

    Google Scholar 

  45. Masters C, Pegg M, Crane D: On the multiplicity of the enzyme catalase in mammalian liver. Mol Cell Biochem 70:113–120, 1986

    Google Scholar 

  46. Crane DI, Masters CJ: The effect of clofibrate on the phospholipid composition of the peroxisomal membranes in mouse liver. Biochim Biophys Acta 876:256–263

  47. Hayashi H, Nakata K: Study on membrane fluidity of liver peroxisomes. Eur J Cell Biol 41:18, 1986

    Google Scholar 

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Hemsley, A., Pegg, M., Crane, D. et al. On the compartmentalization of catalase, fatty acyl-CoA oxidase and urate oxidase in mammalian livers, and the influence of clofibrate treatment on this microlocalization. Mol Cell Biochem 83, 187–194 (1988). https://doi.org/10.1007/BF00226146

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  • DOI: https://doi.org/10.1007/BF00226146

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