Abstract
The substrate specificities of aldehyde and pyridoxal oxidases in Drosophila melanogaster have been determined with a variety of aliphatic and aromatic aldehydes. This analysis has led to the discovery that 2,4,5-trimethoxy-benzaldehyde is a specific substrate for pyridoxal oxidase, as based on the histochemical distribution of oxidase activity, the absence of enzymatic activity in the lpo 1strains, and the dosage dependence on the number of lpo +genes present. The tissue-specific localization of aldehyde oxidase (AO) and pyridoxal oxidase (PO) in the larval and adult structures showed that AO was present in all the major internal organs of the larvae and adults, including brain, imaginal discs, Malpighian tubules, digestive system, and reproductive structures. Pyridoxal oxidase is present in many of the same structures which possess AO, but is missing from the cardia, crop, imaginal discs, ovarian follicle cells, paragonia, pericardial cells, and wreath cells. The only structure which possesses PO but lacks AO is the larval salivary gland. These histochemical differences in AO and PO distribution were also confirmed by enzymatic analysis of the activities present in homogenates of ovaries, paragonia, and salivary glands. The general pattern of enzyme expression appears to be established during embryogenesis and maintained throughout the life of the individual.
Similar content being viewed by others
References
Aggarwal, S. K., and King, R. C. (1967). The ultrastructure of the wreath cells of Drosophila melanogaster larvae. Protoplasma 63343.
Baker, B. S. (1973). The maternal and zygotic control of development by cinnamon, a new mutant in Drosophila melanogaster. Dev. Biol. 33429.
Bentley, M. M., and Williamson, J. H. (1979). A new mutant affecting aldehyde oxidase in Drosophila melanogaster. Z. Naturforsch. 34c304.
Bradford, M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of dye binding. Anal. Biochem. 72248.
Browder, L. W., and Williamson, J. H. (1976). The effect of cinnamon on xanthine dehydrogenase, aldehyde oxidase, and pyridoxal oxidase activity during development in Drosophila melanogaster. Dev. Biol. 53241.
Bryant, P. J. (1978). Pattern formation in imaginal discs. In Ashburner, M., and Wright, T. R. F. (eds.), The Genetics and Biology of Drosophila, Vol. 2c Academic Press, New York, p. 230.
Courtright, J. B. (1967). Polygenic control of aldehyde oxidase in Drosophila. Genetics 5725.
Courtright, J. B. (1975). Evidence for a new type of complementation among the cin, lxd, and ma-l loci in Drosophila melanogaster. Mol. Gen. Genet. 142231.
Courtright, J. B. (1976). Drosophila gene enzyme systems. Adv. Genet. 18249.
Crossley, A. C. (1972). The ultrastructure and function of pericardial cells and other nephrocytes in an insect: Calliphora erythrocephala. Tissue Cell 4529.
Dickinson, W. J. (1970). The genetics of aldehyde oxidase in Drosophila melanogaster. Genetics 66487.
Dickinson, W. J. (1978). Genetic control of enzyme expression in Drosophila: A locus influencing tissue specificity of aldehyde oxidase. J. Exp. Zool. 206333.
Dickinson, W. J., and Carson, H. L. (1979). Regulation of the tissue specificity of an enzyme by a cis-acting genetic element: Evidence from interspecific Drosophila hybrids. Proc. Natl. Acad. Sci. USA 764559.
Dickinson, W. J., and Gaughan, S. (1981). Aldehyde oxidases of Drosophila: contributions of several enzymes to observed activity patterns. Biochem. Genet. 19567.
Dickinson, W. J., and Sullivan, D. T. (1975). Gene Enzyme Systems in Drosophila Springer Verlag, New York.
Dickinson, W. J., and Weisbrod, E. (1976). Gene regulation in Drosophila: Independent expression of closely linked, related structural loci. Biochem. Genet. 14709.
Finnerty, V., and Johnson, G. (1979). Post-translational modification as a potential explanation of high levels of enzyme polymorphism. Modification of xanthine dehydrogenase and aldehyde oxidase in Drosophila melanogaster. Genetics 91695.
Finnerty, V. G., Duck, P., and Chovnick, A. (1970). Studies on genetic organization in higher organisms. II. Complementation and fine structure of the maroon-like locus of Drosophila melanogaster. Proc. Natl. Acad. Sci. USA 65939.
Forrest, H. S., Hanly, E., and Lagowski, J. M. (1961). Biochemical differences between the mutants rosy-2 and maroon-like of Drosophila melanogaster. Genetics 461455.
Hayden, T. J., and Duke, E. J. (1975). Aldehyde oxidizing enzymes in Locusta migratoria. In Market, C. L. (ed.), Isozymes II. Physiological Function Academic Press, New York, p. 501.
Keller, E. C., Jr., and Glassman, E. (1964). A third locus (lxd) affecting xanthine dehydrogenase in Drosophila melanogaster. Genetics 49663.
Kuhn, D. T., and Cunningham, G. N. (1977a). Aldehyde oxidase compartmentalization in Drosophila melanogaster wing imaginal disks. Science 196875.
Kuhn, D. T., and Cunningham, G. N. (1977b). Aldehyde oxidase distribution in haltere discs of homeotic bithorax mutants in Drosophila melanogaster. Mol. Gen. Genet. 15037.
Kuhn, D. T., and Cunningham, G. N. (1978). Aldehyde oxidase distribution in Drosophila melanogaster mature imaginal discs, histoblasts and rings of imaginal cells. J. Exp. Zool. 2041.
Lindsley, D. L., and Grell, E. H. (1968). Genetic Variations of Drosophila melanogaster Carnegie Institution of Washington, Washington, D.C.
Rizki, T. M. (1978). The circulatory system and associated cells and tissues. In Ashburner, M., and Wright, T. R. F. (eds.), The Genetics and Biology of Drosophila, Vol. 2b Academic Press, New York, p. 397.
Sprey, Th. E., Segal, D., Sprey-Pieters, H. E., and Kuhn, D. T. (1981). Influence of homoeotic genes on the aldehyde oxidase pattern in imaginal discs of Drosophila melanogaster. Dev. Genet. 275.
Underwood, E. M., and Mahowald, A. P. (1980). The chorion defect of the ocelliless mutation caused by abnormal follicle cell function. Dev. Genet. 1247.
Ursprung, H., and Leone, J. (1965). Alcohol dehydrogenases: A polymorphism in Drosophila melanogaster. J. Exp. Zool. 160147.
Warner, C. K., and Finnerty, V. G. (1981). Molybdenum hydroxylases in Drosophila. II. Molybdenum cofactor in xanthine dehydrogenase, aldehyde oxidase and pyridoxal oxidase. Mol. Gen. Genet. 18492.
Warner, C. K., Watts, D. T., and Finnerty, V. (1980). Molybdenum hydroxylases in Drosophila. I. Preliminary studies of pyridoxal oxidase. Mol. Gen. Genet. 180449.
Wigglesworth, V. B. (1970). The pericardial cells of insects: Analogue of the reticuloendothelial system. J. Reticuloendothel. Soc. 7208.
Wilkinson, G. N. (1961). Statistical estimations in enzyme kinetics. Biochem. J. 80324.
Author information
Authors and Affiliations
Additional information
This paper is dedicated to Professor Donald F. Poulson, Yale University, a pioneer in Drosophila developmental genetics.
This work was supported by NIH Grants AG01975 and GM27866.
Rights and permissions
About this article
Cite this article
Cypher, J.J., Tedesco, J.L., Courtright, J.B. et al. Tissue-specific and substrate-specific detection of aldehyde and pyridoxal oxidase in larval and imaginal tissues of Drosophila melanogaster . Biochem Genet 20, 315–332 (1982). https://doi.org/10.1007/BF00484427
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF00484427