Summary
The use of monoclonal antibodies against Drosophila alcohol dehydrogenase (ADH) provides a powerful tool in the analysis of the tissue and temporal patterns of Adh gene expression. Immunocytochemical techniques at the light- and electron-microscopic levels have been used to determine the distribution of ADH in the ovarian follicles of D. melanogaster during oogenesis. In the early stages of oogenesis, small amounts of ADH are detectable in the cystocytes. At the beginning of vitellogenesis (S7), ADH appears to be located mainly in the nurse cells. From stage S9 onwards, the ADH protein is evenly distributed in the ooplasm until the later stages of oogenesis (S13–14), when multiple ADH-positive bodies of varying size appear in the ooplasm. This change in distribution is a result of the compartmentalization of the ADH protein within the glycogen yolk or β-spheres. Yolk becomes enclosed within the lumen of the primitive gut during embryonic development, and thus our results suggest a mechanism for the transfer of maternally-inherited enzymes to the gut lumen via yolk spheres.
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References
Anderson S, McDonald J (1981) A method for determining the “in vivo” stability of Drosophila alcohol dehydrogenase (E.C. 1.1.1.1.) Biochem Genet 19:411–419
Berry S (1985) RNA synthesis and storage during insect oogenesis. In: Browder LW (ed) Developmental biology: a comprehensive synthesis, vol 1. Plenum Press, New York, pp 351–384
Chambers G (1988) The Drosophila alcohol dehydrogenase gene-enzyme system. Adv Genet 25:39–107
Fibla J, Enjuanes L, Gonzàlez-Duarte R (1989) Inter-specific analysis of Drosophila alcohol dehydrogenase by an immunoenzymatic assay using monoclonal antibodies. Biochem Biophys Res Commun 160:638–646
Fullilove SL, Jacobson AG, Turner FR (1978) Embryonic development: descriptive. In: Ashburner M, Wright TRF (eds) The genetics and biology of Drosophila, vol 2c. Academic Press, New York, pp 105–227
Goldberg DA, Posakony JW, Maniatis T (1983) Correct developmental expression of a cloned alcohol dehydrogenase gene transduced into the Drosophila germ line. Cell 34:59–73
Griffiths G, McDowall A, Back R, Dubochet J (1984) On the preparation of cryosections for immunocytochemistry. J Ultrastruct Res 89:65–78
Herxheimer G (1903) Zur Fettfärbung. Centralbl Allg Pathol Anat 14:841–842
Hough-Evans BR, Jacobson-Lorena M, Cummings MR, Britten RJ, Davidson EH (1980) Complexity of RNA in eggs of Drosophila melanogaster and Musca domestica. Genetics 95:81–94
Jiménez G, Correa I, Melgosa MP, Bullido MJ, Enjuanes L (1986) Critical epitopes in transmissible gastroenteritis virus neutralization. J Virol 60:131–139
King R (1960) Oogenesis in adult Drosophila melanogaster. IX. Studies on the cytochemistry and ultrastructure of developing oocytes. Growth 24:265–323
King R (1970) Ovarian development in Drosophila melanogaster. Academic Press, New York London
Koch E, Spitzer R (1982) Autoradiographic studies of protein and polysaccharide synthesis during vitellogenesis in Drosphila. Cell Tissue Res 224:315–333
Lillie R (1965) Histopathologic technique and practical histochemistry, 3rd edn. McGraw Hill, New York
Lockett TJ, Ashburner M (1989) Temporal and spatial utilization of the alcohol dehydrogenase gene promoters during development of Drosophila melanogaster. Dev Biol 134:430–437
Madhavan K, Conscience-Egli M, Sieber F, Ursprung H (1973) Farnesol metabolism in Drosophila melanogaster: ontogeny and tissue distribution of octanol dehydrogenase and aldehyde oxidase. J Insect Physiol 19:235–241
Mahowald A (1972) Ultrastructural observations on oogenesis in Drosphila. J Morphol 137:29–48
Postlethwait J, Giorgi F (1985) Vitellogenesis in insects. In: Browder LW (ed) Development biology: a comprehensive synthesis, vol 1. Plenum Press, New York, pp 85–126
Savakis C, Ashburner M (1985) A simple gene with a complex pattern of transcription: the alcohol dehydrogenase gene of Drosophila melanogaster. Cold Spring Harb Symp Quant Biol 50:505–514
Sofer W, Martin PF (1987) Analysis of alcohol dehydrogenase gene expression in Drosophila. Annu Rev Genet 21:203–227
Tanaka A (1977) Immunohistochemical studies of vitellogenin during embryogenesis in the cockroach Blatella germanica. J Embryol Exp Morphol 38:49–62
Thatcher D (1980) The complete amino acid sequence of three alcohol dehydrogenase alleloenzymes (AdhN-11, AdhS and AdhUF) from the fruitfly Drosophila melanogaster. Biochem J 187:875–886
Thiéry J (1967) Mise en évidence des polysaccharides sur coupes fines en microscopie electronique. J Microscopie 6:987–1018
Tokuyasu K (1980) Immunochemistry on ultrathin frozen sections. Histochem J 12:381–403
Ursprung H, Sofer WH, Burroughs N (1970) Ontogeny and tissue distribution of alcohol dehydrogenase in Drosophila melanogaster. Wilhelm Roux' Arch 164:201–208
Visa N, Fibla J, Santa-Cruz MC, Gonzàlez-Duarte R (1992) Developmental profile and tissue distribution of Drosophila alcohol dehydrogenase: an immunochemical analysis with monoclonal antibodies. J Histochem Cytochem 40:39–49
Winberg J, Thatcher D, McKinley-McKee J (1982) Alcohol dehydrogenase from the fruitfly Drosophila melanogaster: substrate specificity of the alleloenzymes AdhS and AdhUF. Biochim Biophys Acta 704:7–16
Yamashita O, Irie K (1980) Larval hatching from vitellogenindeficient eggs developed in male hosts of the silkworm. Nature 283:385–386
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Visa, N., Fibla, J., Gonzàlez-Duarte, R. et al. Progressive redistribution of alcohol dehydrogenase during vitellogenesis in Drosophila melanogaster: characterization of ADH-positive bodies in mature oocytes. Cell Tissue Res 268, 217–224 (1992). https://doi.org/10.1007/BF00318789
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DOI: https://doi.org/10.1007/BF00318789