Abstract
Recent experiments have demonstrated that egasyn not only sequesters β-glucuronidase in microsomes by forming high molecular weight complexes with β-glucuronidase, but also has carboxyl esterase activity. We have found several new phenotypes of egasyn-esterase after electrophoresis and isoelectric focusing of liver homogenates and purified egasyn of inbred and wild mouse strains. Several phenotypes corresponded in relative mobility and relative isoelectric point among inbred strains to that recently reported for esterase-22 by Eisenhardt and von Deimling [(1982). Comp. Biochem. Physiol. 73B:719]. This genetic evidence, plus a wide variety of comparative biochemical and physiological data, indicates that egasyn is identical to esterase-22. Both parental types of egasyn isozymes are expressed in heterozygous F1 progeny, suggesting that alterations in the egasyn structural gene are responsible for the altered isoelectric points. Also, egasyn is a monomer since no new esterase bands appear in F1 progeny. The variants in isoelectric point of egasyn map at or near the egasyn (Eg) gene within the esterases of cluster 1 near Es-9 on chromosome 8.
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Belinsky, S. A., Kauffman, F. C., Sokolove, P. M., Tsukuda, T., and Thurman, R. G. (1984). Calcium-mediated inhibition of glucuronide production by epinephrine in the perfused rat liver. J. Biol. Chem. 2597705.
Chapman, V. M., Paigen, K., Siracusa, L., and Womack, J. E. (1979). In Altman, P. L., and Katz, D. D. (eds.), Inbred and Genetically Defined Strains of Laboratory Animals, Part I. Mouse and Rat Federation of American Societies for Experimental Biology, Bethesda, Md., p. 83.
Davisson, M., and Roderick, T. H. (1985). The mouse linkage map. Mouse News Lett. 737.
Eisenhardt, E., and von Deimling, O. (1982). Interstrain variation of esterase-22, a new isozyme of house mouse. Comp. Biochem. Physiol. 73B719.
Ganschow, R., and Bunker, B. G. (1970). Genetic control of glucuronidase in mice. Biochem. Genet. 4127.
Ganschow, R., and Paigen, K. (1967). Separate genes determining the structure and intracellular location of hepatic glucuronidase. Proc. Natl. Acad. Sci. USA 58938.
Hayashi, M., Nakajima, Y., and Fishman, W. H. (1964). The cytologic demonstration of β-glucuronidase employing naphthol AS-BI glucuronide and hexazonium pararosanline; A preliminary report. J. Histochem. Cytochem. 12293.
Heymann, E. (1980). Carboxyl esterases and amidases. In Enzymatic Basis of Detoxification, Vol. II Academic Press, New York, pp. 291–323.
Hilgers, J., and Arends, J. (1986). The novel immunological responses of the BALB/c mouse. In Potter, M. (ed.), Current Topics in Microbiology and Immunology Monograph on the “Wild Mouse in Immunology,” Proceedings of a meeting at the National Institutes of Health, Nov. 4–6, 1985, Springer-Verlag, New York.
Karl, T. R., and Chapman, V. M. (1974). Linkage and expression of the Eg locus controlling inclusion of β-glucuronidase into microsomes. Biochem. Genet. 11367.
Komma, D. J. (1963). Characteristics of the esterases of human cells grown in vitro. J. Histochem. Cytochem. 11619.
Laemmli, U. K. (1970). Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227680.
Lipps, A., Ronai, A., and von Deimling, O. (1979). Esterase-7, a common constituent of numerous mouse tissues. Comp. Biochem. Physiol. 62B201.
Lusis, A. J., and Paigen, K. (1977). In Ratazzi, M. C., Scandalios, J. G., and Whitt, G. S. (eds.), Isozymes: Current Topics in Biological and Medical Research, Vol. 2, pp. 63–106. Alan R. Liss, N.Y.
Lusis, A. J., Tomino, S., and Paigen, K. (1976). Isolation, characterization and radioimmunoassay of murine egasyn, a protein stabilizing glucuronidase membrane binding. J. Biol. Chem. 2517752.
Maurer, H. R. (1977). Disc Electrophoresis and Related Techniques of Polyacrylamide Gel Electrophoresis DeGruyter, New York.
Medda, S., and Swank, R. T. (1985). Egasyn, a protein which determines the subcellular distribution of β-glucuronidase, has esterase activity. J. Biol. Chem. 26015802.
Nash, H. R., and von Deimling, O. (1982). Kidney esterase of Mus musculus: Further polymorphism of esterase-6, esterase-9 and a new esterase, esterase-20. Biochem. Genet. 20537.
Owens, J. W., Gammon, K. L., and Stahl, P. D. (1975). Multiple forms of β-glucuronidase in rat liver lysosomes and microsomes. Arch. Biochem. Biophys. 166258.
Peters, J. (1982). Nonspecific esterases of Mus musculus. Biochem. Genet. 20585.
Peters, J., and Nash, H. R. (1977). Polymorphisms of esterase 11 in Mus musculus, a further esterase locus on chromosome 8. Biochem. Genet. 15217.
Petras, M. L. (1963). Genetic control of a serum esterase component in Mus musculus. Proc. Natl. Acad. Sci. USA 50112.
Petras, M. L., and Biddle, F. G. (1967). Serum estarase in the house mouse, Mus musculus. Can. J. Genet. Cytol. 9704.
Petras, M. L., and Sinclair, P. (1969). Another esterase variant in the kidney of the house mouse, Mus musculus. Can. J. Genet. Cytol. 1197.
Popp, R. A., and Popp, D. M. (1962). Inheritance of serum esterases having different electrophoretic pattern. J. Hered. 53111.
Robbi, M., and Beaufay, H. (1983). Purification and characterization of various esterases from rat liver. Eur. J. Biochem. 137293.
Schollen, J., Bender, K., and von Deimling, O. (1975). Esterase. XXI. Es-9, a possibly new polymorphic esterase in Mus musculus genetically linked to Es-2. Biochem. Genet. 13369.
Swank, R. T., and Paigen, K. (1973). Biochemical and genetic evidence for a macromolecular β-glucuronidase complex in microsomal membranes. J. Mol. Biol. 77371.
Wassmer, B., de Looze, S. M., and von Deimling, O. (1985). Biochemistry and genetics of esterase-20 (ES-20), a second trimeric carboxyl esterase of the house mouse (Mus musculus). II. A unique recombination reveals ES-20 as a hybrid enzyme. Biochem. Genet. 23 759.
Wray, W., Boulikas, T., Wray, V. P., and Hancock, R. (1981). Silver staining of proteins in polyacrylamide gels. Anal. Biochem. 118197.
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This work was supported by Grant GM-33559 from the National Institutes of Health.
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Medda, S., von Deimling, O. & Swank, R.T. Identity of esterase-22 and egasyn, the protein which complexes with microsomal β-glucuronidase. Biochem Genet 24, 229–243 (1986). https://doi.org/10.1007/BF00502791
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DOI: https://doi.org/10.1007/BF00502791