Stress Responses in Drosophila Cells

  • Eiko Akaboshi
  • Yutaka Inoue

Abstract

The environmental stresses (e.g., pollution, radiation, and chemicals) increase in the modern society. Various kinds of stress attack all living organisms. All organisms appear to have innate ability to overcome these stresses (sometimes threats) for survival. Their sensitivity and responses, however, are varied, depending on the organism and on the developmental stage, age, tissue, and cell. Immune and inflammation reactions also play important roles in the processes in which organisms recover from the stress and rescue themselves (for reviews, see Cociancich et al., 1994; Hultmark, 1993; Wilder, 1995). When organisms are exposed to above the threshold threats, they either die or survive with severe damage. The survivors, lucky as it may sound, must undergo sustained agonies. Further, the damage in their DNA, either in eggs or spermatozoa, may result in the appearance of mutated or aberrant progeny. An increasingly large number of people recognize such stresses as a serious problem for the society and for all living organisms. Thus, a worldwide campaign to keep the earth clean and safe has been boosted. Accordingly, the stress and stress-response have emerged recently as an important topic in cell biology.

Keywords

Cystic Fibrosis Polytene Chromosome Drosophila Cell Heat Shock Element Gadd45 Gene 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Akaboshi, E., and Howard-Flanders, P., 1989, Proteins induced by DNA-damaging agents in cultured Drosophila cells, Mutat. Res. 227: 1–6.PubMedCrossRefGoogle Scholar
  2. Akaboshi, E., Inoue, Y., and Ryo, H., 1994a, Cloning of the cDNA and genomic DNA that correspond to the recA-like gene of Drosophila melanogaster, Jpn. J. Genet. 69: 663–670.PubMedCrossRefGoogle Scholar
  3. Akaboshi, E., Inoue, Y., Ryo, H., and Yamamoto, M. T., 1994b, Cloning and mapping of genes activated by MMS treatment in Drosophila cultured cells, Dros. Inf. Serv. 75: 149.Google Scholar
  4. Amin, J., Ananthan, J., and Voellmy, R., 1988, Key features of heat shock regulatory elements, Moi. Cell. Biol. 8: 3761–3769.Google Scholar
  5. Ashburner, M., and Bonner, J. J., 1979, The induction of gene activity in Drosophila by heat shock, Cell 17: 241–254.PubMedCrossRefGoogle Scholar
  6. Bishop, D. K., Park, D., Xu, L., and Kleckner, N., 1992, DMC1: A meiosis-specific yeast homolog of E. coil recA required for recombination, synaptonemal complex formation, and cell cycle progression, Cell 69: 439–456.Google Scholar
  7. Bohr, V. A., Evans, M. K., and Fornace, A. J., Jr., 1989, Biology of disease: DNA repair and its pathogenetic implications, Lab. Invest. 61: 143–161.PubMedGoogle Scholar
  8. Carrier, F., Gatignol, A., Hollander, M. C., Jeang, K.-T., and Fornace, A. J., Jr., 1994, Induction of RNA-binding proteins in mammalian cells by DNA-damaging agents, Proc. Natl. Acad. Sci. USA 91: 1554–1558.PubMedCrossRefGoogle Scholar
  9. Chen, C.-Y., Oliner, J. D., Zhan, Q., Fornace, A. J., Jr., and Vogelstein, B., 1994, Interactions between p53 and MDM2 in a mammalian cell cycle, Proc. Natl. Acad. Sci. USA 91: 2684–2688.PubMedCrossRefGoogle Scholar
  10. Cociancich, S., Bulet, P., Hetru, C., and Hoffmann, J. A., 1994, The inducible antibacterial peptides of insects, ParasitoL Today 10: 132–139.CrossRefGoogle Scholar
  11. Doige, C. A., and Ames, G. F.-L., 1993, ATP-dependent transport systems in bacteria and humans: Relevance to cystic fibrosis and multidrug resistance, Annu. Rev. Microbiol. 47: 291–319.CrossRefGoogle Scholar
  12. Ellis, R. J., 1993, The general concept of molecular chaperones, Philos. Trans. R. Soc. London Ser. B 339: 257–261.CrossRefGoogle Scholar
  13. Engels, W. R., Preston, C. R., Thompson, P., and Eggleston, W. B., 1986, In situ hybridization to Drosophila salivary chromosomes with biotinylated DNA probes and alkaline phosphatase, Focus 8: 6–8.Google Scholar
  14. Finley, D., and Chau, V., 1991, Ubiquitination, Annu. Rev. Cell Biol. 7: 25–69.CrossRefGoogle Scholar
  15. Fornace, A. J., Jr., 1992, Mammalian genes induced by radiation; activation of genes associated with growth control, Annu. Rev. Genet. 26: 507–526.CrossRefGoogle Scholar
  16. Friedberg, E. C., 1988, Deoxyribonucleic acid repair in the yeast, Microbiol. Rev. 52: 70–102.PubMedGoogle Scholar
  17. Hendrick, J. P., and Hartl, F.-U., 1993, Molecular chaperone functions of heat-shock proteins, Annu. Rev. Biochem. 62: 349–384.CrossRefGoogle Scholar
  18. Herrlich, P., Ponta, H., and Rahmsdorf, H. J., 1992, DNA damage-induced gene expression: Signal transduction and relation to growth factor signaling, Rev. Physiol. Biochem. Pharmacol. 119: 187–223.PubMedGoogle Scholar
  19. Hultmark, D., 1993, Immune reactions in Drosophila and other insects: A model for innate immunity, Trends Genet. 9: 178–182.PubMedCrossRefGoogle Scholar
  20. Ip, Y. T., Kraut, R, Levine, M., and Rushlow, C. A., 1991, The dorsal morphogen is a sequence-specific DNA-binding protein that interacts with a long-range repression element in Drosophila., Cell 64: 439–446.PubMedCrossRefGoogle Scholar
  21. Ip, Y. T., Reach, M., Engstrom, Y., Kadalayil, L., Cai, H., Gonzalez-Crespo, S., Tatei, K., and Levine, M., 1993, Dif, a dorsal-related gene that mediates an immune response in Drosophila, Cell 75: 753–763.Google Scholar
  22. Kelley, P. M., and Schlesinger, M. J., 1978, The effect of amino acid analogues and heat shock on gene expression in chicken embryo fibroblasts, Cell 15: 1277–1286.PubMedCrossRefGoogle Scholar
  23. Lee, H., Simon, J. A., and Lis, J. T., 1988, Structure and expression of ubiquitin genes of Drosophila melanogaster, Mol. Cell. Biol. 8: 4727–4735.PubMedGoogle Scholar
  24. Lemaitre, B., Meister, M., Govind, S., Georgel, P., Steward, S., Reichhart, J.-M., and Hoffmann, J. A., 1995, Functional analysis and regulation of nuclear import of dorsal during the immune response in Drosophila, EMBO J. 14: 536–545.Google Scholar
  25. Lindquist, S., 1986, The heat-shock response, Annu. Rev. Biochem, 55: 1151–1191.CrossRefGoogle Scholar
  26. Lindsley, D. L., and Zimm, G. G., 1992, The Genome of Drosophila melanogaster, Academic Press, San Diego.Google Scholar
  27. Lommel, L., Carswell-Crumpton, C., and Hanawalt, P. C., 1995, Preferential repair of the transcribed DNA strand in the dihydrofolate reductase gene throughout the cell cycle in UV-irradiated human cells, Mutat. Res. 336: 181–192.Google Scholar
  28. Love, J. D., Vivino, A. A., and Minton, K. W., 1986, Hydrogen peroxide toxicity may be enhanced by heat shock gene induction in Drosophila, J. Cell. Physiol. 126: 60–68.PubMedCrossRefGoogle Scholar
  29. Modrich, P., 1991, Mechanisms and biological effects of mismatch repair, Annu. Rev. Genet. 25: 229–253.CrossRefGoogle Scholar
  30. Nover, L., 1991, Structure of eukaryotic heat shock genes, in: Heat Shock Response ( L. Nover, ed.), CRC Press, Boca Raton, FL, pp. 129–150.Google Scholar
  31. Papathanasiou, M. A., Kerr, N. C. K., Robbins, J. H., McBride, O. W., Alamo, I., Jr., Barrett, S. F., Hickson, I. D., and Fornace, A. J., Jr., 1991, Induction by ionizing radiation of the gnrid45 gene in cultured human cells: lack of mediation by protein kinase C, Mol. Cell. Biol. 11: 1009–1016.PubMedGoogle Scholar
  32. Parsell, D. A., and Lindquist, S., 1993, The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins, Annu. Rev. Genet. 27: 437–496.CrossRefGoogle Scholar
  33. Pelham, H. R. B., 1986, Speculations on the functions of the major heat shock and glucose-regulated proteins, Cell 46: 959–961.PubMedCrossRefGoogle Scholar
  34. Prakash, S., Sung, P., and Prakash, L., 1993, DNA repair genes and proteins of Saccharomyces cerevisiae, Annu. Rev. Genet. 27: 33–70.PubMedCrossRefGoogle Scholar
  35. Price, B. D., and Park, S. J., 1994, DNA damage increases the levels of MDM2 messenger RNA in wtp53 human cells, Cancer Res. 54: 896–899.PubMedGoogle Scholar
  36. Ritossa, F., 1962, A new puffing pattern induced by a temperature shock and DNP in Drosophila, Experientia 18: 571–573.CrossRefGoogle Scholar
  37. Schmitz, M. L., Henkel, T., and Baeuerle, P. A., 1991, Proteins controlling the nuclear uptake of NF-KB, rel and dorsal, Trends Cell BioL 1: 130–137.PubMedCrossRefGoogle Scholar
  38. Sferra, T. J., and Collins, F. S., 1993, The molecular biology of cystic fibrosis, Annu. Rev. Med. 44: 133–144.PubMedCrossRefGoogle Scholar
  39. Shinohara, A., Ogawa, H., and Ogawa, T., 1992, Rad51 protein involved in repair and recombination in S. cerevisiae is a RecA-like protein, Cell 69: 457–470.PubMedCrossRefGoogle Scholar
  40. Siebenlist, U., Franzoso, G., and Brown, K., 1994, Structure, regulation and function of NF-KB, Annu. Rev. Cell BioL 10: 405–455.CrossRefGoogle Scholar
  41. Steward, R, and Govind, S., 1993, Dorsal-ventral polarity in the Drosophila embryo, Carr. Opin. Genet. Dey. 3: 556–561.Google Scholar
  42. Tchurikov, N. A., Ebralidze, A. K., and Georgiev, G. P., 1986, The suffix sequence is involved in processing the 3’ ends of different mRNAs in Drosophila melanogaster, EMBO J. 5: 2341–2347.Google Scholar
  43. Tomasovic, S. P., and Koval, T. M., 1985, Relationship between cell survival and heat-stress protein synthesis in a Drosophila cell line, Int. J. Radiat. Biol 48: 635–650.Google Scholar
  44. Toung, Y.-P. S., Hsieh, T.-S., and Tu, C.-P. D., 1990, Drosophila glutathione 5-transferase 1–1 shares a region of sequence homology with the maize glutathione S-transferase III, Proc. Natl. Acad. Sci. USA 87: 31–35.Google Scholar
  45. Toung, Y.-P. S., Hsieh, T.-S., and Tu, C.-P. D., 1993, The glutathione S-transferase D genes. A divergently organized, intronless gene family in Drosophila melanogaster, J. BioL Chem. 268: 9737–9746.PubMedGoogle Scholar
  46. Tsuchida, S., and Sato. K., 1992, Glutathione transferases and cancer, Crit. Rev. Biochem. Moi. Biol. 27: 337–384.CrossRefGoogle Scholar
  47. Walker, G. C., 1984, Mutagenesis and inducible responses to deoxyribonucleic acid damage in Escherichia coli, Microbiol. Rev. 48: 60–93.PubMedGoogle Scholar
  48. Welcher, A. A., Torres, A. R., and Ward, D. C., 1986, Selective enrichment of specific DNA, cDNA and RNA sequences using biotinylated probes, avidin and copperchelate agarose, Nucleic Acids Res. 14: 10027–10044.PubMedCrossRefGoogle Scholar
  49. Wilder, R. L., 1995, Neuroendocrine-immune system interactions and auto-immunity, Anna. Rev. ImmunoL 13: 307–338.CrossRefGoogle Scholar
  50. Xiao, H., and Lis, J. T., 1988, Germline transformation used to define key features of heat-shock response elements, Science 239: 1139–1142.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1997

Authors and Affiliations

  • Eiko Akaboshi
    • 1
  • Yutaka Inoue
    • 2
  1. 1.Institute for Molecular and Cellular BiologyOsaka UniversitySuita 565Japan
  2. 2.Osaka University of Foreign StudiesMinoo, Osaka 562Japan

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