Abstract
The interaction of mouse liver catalase with subcellular membranes was studied, and an ionic interaction with a variety of membranes, including those derived from the microsomes, was observed. The interaction with microsomal membranes was found to be abolished by pre-treatment of catalase with neuraminidase, indicating a functional significance for catalase-bound sialic acid. Catalase activity was found to be enhanced when bound to membranes, and evidence for a weak association of catalase with peroxisomal structure in mouse liver was also obtained. It is concluded that mouse liver catalase has a capacity to bind to a variety of subcellular membranes in vivo and that this interaction may be consistent with a general protective role for the enzyme, as well as being compatible with a model of peroxisomal biogenesis which involves the interaction of catalase with microsomal membranes.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
Abbreviations
- LGF:
-
Large Granule Fraction
References
Masters C, Pegg M, Crane D: On the multiplicity of the enzyme catalase in mammalian liver. Mol Cell Biochem 70:113–120, 1986
Masters CJ, Holmes RS: Peroxisomes: New aspects of cell physiology and biochemistry. Physiol Rev 57:816–882, 1977
Jones GL, Masters CJ: On the nature and characteristics of the multiple forms of catalase in mouse liver. Arch Biochem Biophys 169:7–21, 1975
Masters CJ: On the turnover and multiplicity of peroxisomal catalases. Ann NY Acad Sci 386:301–313, 1982
Tobe T, Higashi T: Studies on rat liver catalase XI. Site of synthesis and segregation by stripped ER membranes. J Biochem 88:1341–1347, 1980
Allen DW, Cadman S, McCann SR, Finkel B: Increased membrane binding of erythrocyte catalase in hereditary spherocytosis and in metabolically stressed normal cells. Blood 9:113–123, 1977
Aviram I, Shaklai H: The association of human erythrocyte catalase with cell membrane. Arch Biochem Biophys 212:329–337, 1981
Takei, Higashi: Interaction with deoxycholate of rat liver peroxisomal and cytosolic catalase. J Biochem 97:685–692, 1985
Alexson SEH, Fujiki Y, Shio H, Lazarow PB: Partial disassembly of peroxisomes. J Cell Biol 101:294–305, 1985
Crane DI, Hemsley AC, Masters CJ: Purification of peroxisomes from livers of normal and clofibrate-treated mice. Anal Biochem 148:436–445, 1985
Price VE, Sterling WR, Tarantola VA, Hartley Jr RW Rechcigl Jr M: The kinetics of catalase synthesis and destruction in vivo. J Biol Chem 237:3468–3475, 1962
Crane D, Holmes R, Masters C: Proteolytic modification of mouse liver catalase. Biochem Biophys Res Commun 104:1567–1572, 1982
Laemmli UK: Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 227:680–685, 1970
Petersen GL: A simplification of the protein assay of Lowry et al. which is more generally applicable. Anal Biochem 83:346–356, 1977
Schonbaum GR, Chance B: Catalase in ‘The Enzymes’ (2nd ed.) PD Boyer (ed) Academic Press NY, Vol XIII, 1976, pp 363–408
Holmes RS, Masters CJ: On the latency, multiplicity and subcellular distribution of catalase activity in mammalian tissues. Int J Biochem 1:474–482, 1970
Holmes RS, Masters CJ: Species specific features of the distribution and multiplicity of mammalian liver catalase. Arch Biochem Biophys 148:217–223, 1972
Fukami MH, Flatmark T: Studies on catalase compartmentation in digitonin-treated rat hepatocytes. Biochim Biophys Acta 889:91–94, 1986
Hemsley A, Pegg M, Crane D, Masters C: On the compartmentalization of catalase, fatty acyl-CoA oxidase and urate oxidase in murine and cavian livers: influence of clofibrate. Mol Cell Biochem in press, 1988
Roels F, Geerts A, de Coster W, Goldfischer S: Cytoplasmic catalase: cytochemistry and physiology. Ann NY Acad Sci 386:535–536, 1982
Holmes RS, Masters CJ: Catalase heterogeneity. Arch Biochem Biophys 109:197–205, 1965
Drezeniek R: Viral and bacterial neuraminidases. Curr Top Microbiol Immunol 59:35–74, 1972
Pegg MS, Crane DI, Masters CJ: The glycoprotein nature of mammalian catalases. Biochem Int 12:831–838, 1986
Furuta S, Hayashi H, Hijikata M, Miyazawa S, Osumi T, Hashimoto T: Complete nucleotide sequence of cDNA and deduced amino acid sequence of rat liver catalase. Proc Natl Acad Sci USA 83:313–317, 1986
Murthy MRN, Reid TJ, Sicignamo A, Tamaha N, Rossman MG: Structure of beef liver catalase. J Mol Biol 152:465–499, 1981
Schauer R: Chemistry, metabolism and biological functions of sialic acids. Adv Carb Chem Biochem 40:131–234, 1982
Goldman BM, Blobel G: Biogenesis of peroxisomes: intracellular site of synthesis of catalase and uricase. Proc Natl Acad Sci USA 75:5066–5070, 1978
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Pegg, M., Crane, D. & Masters, C. On the interactions of catalase with subcellular structure. Mol Cell Biochem 86, 77–85 (1989). https://doi.org/10.1007/BF00231692
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00231692