Chilling injury in the housefly: Evidence for the role of oxidative stress between pupariation and emergence

Cryobiology

Volumn 33, Issue 4, 1996, Pages 447-458

  Rojas, Robert R ^a   Leopold, Roger A ^a  

^a USDA ARS Red River Valley Agricultural Research Center   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

INSECTA;

EID: 0007635932     PISSN: 00112240     EISSN: None     Source Type: Journal    
DOI: 10.1006/cryo.1996.0045     Document Type: Article

References (45)

1. Ahmad, S., and Pardini, R. S. Evidence for the presence of glutathione peroxidase activity toward an organic hydroperoxide in larvae of the cabbage looper moth, Trichoplusia ni. Insect Biochem. 18, 861-866 (1989).
2. Ahmad, S., and Pardini, R. S. Mechanisms for regulating oxygen toxicity in phytophagous insects. J. Free Rad. Biol Med. 8, 401-413 (1990).
3. Ahamd, S., Pristos, C. A., Bowen, S. M., Heisler, C. R., Blomquist, G. J., and Pardini, R. S. Antioxidant enzymes of larvae of the cabbage looper moth, Trichoplusia ni: Subcellular distribution and activities of superoxide dismutase, catalase and glutathione reductase. Free Rad. Res. Commun. 4, 403-408 (1988).
4. Ålin, P., Danielson, U. H., and Mannervick, B. 4-Hydroxyalk-2-enals are substrates for glutathione transferase. FEBS Lett. 179, 267-270 (1985).
5. Allen, R. D. Dissection of oxidative stress tolerance using transgenic plants. Plant Physiol. 107, 1049-1054 (1995).
6. Allen, R. G., Oberley, L. W., Elwell, J. H., and Sohal, R. S. Developmental patterns in the antioxidant defenses of the housefly, Musca domestica. J. Cell. Physiol. 146, 270-276 (1991).
7. Asada, K., Yoshikawa, K., Takahashi, M.-A., Maeda, Y., and Enmanji, K. Superoxide dismutases from blue-green alga, Plectonema boryanum. J. Biol. Chem. 250, 2801-2807 (1975).
8. Bale, J. S. Insect cold hardiness - An ecological perspective. J. Insect Physiol. 33, 899-908 (1987).
9. Beauchamp, C. O., and Fridovich, I. Isozymes of superoxide dismutase from wheat germ. Biochim. Biophys. Acta 317, 50-64 (1973).
10. Bird, T. G., Salin, M. L., Boyle, J. A., and Heitz, J. R. Superoxide dismutase dismutase in the housefly, Musca domestica (L.). Arch. Insect Biochem. Physiol. 3, 31-43 (1986).
11. Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254 (1976).
12. Bray, R. C., Cockle, S. A., Fielden, E. M., Roberts, P. B., Rotilio, G., and Calabrese, L. Reduction and inactivation of superoxide dismutase by hydrogen peroxide. Biochem. J. 139, 43-48 (1974).
13. Brodie, A. E., and Reed, D. J. Glutathione disulfide reduction in tumor mitochondria after t-butyl hydroperoxide treatment. Chem. Biol. Interact. 84, 125-132 (1992).
14. Bruchhaus, I., and Tannich, E. Induction of the iron-containing superoxide dismutase in Entamoeba histolytica by a superoxide anion-generating system or by iron chelation. Mol. Biochem. Parasitol. 67, 281-288 (1994).
15. Cotty, V. F., and Henry, S. M. Glutathione metabolism in DDT resistant and susceptible house flies. Contribs. Boyce Thompson Inst. 19, 393-401 (1958).
16. De Vos, C. H. R., Kraak, H. L., and Bino, R. J. Ageing of tomato seeds involves glutathione oxidation. Physiol. Plant. 92, 131-139 (1994).
17. Fernandez-Sousa, J. M., and Michelson, A. M. Variation of superoxide dismutases during development of the fruit fly Ceratitis capitata L. Biochem. Biophys. Res. Commun. 73, 217-223 (1976).
18. Fridovich, I. Superoxide dismutases. Adv. Enzymol. Relat. Areas Mol. Biol. 58, 61-97 (1986).
19. Fukuhara, T., Nishio, S., Ono, Y., Kawauchi, M., Asari, S., and Ohmoto, T. Induction of Cu,Zn-superoxide dismutase after cortical contusion injury during hypothermia. Brain Res. 657, 333-336 (1994).
20. Gardiner, C. S., and Reed, D. J. Glutathione redox cycle-driven recovery of reduced glutathione after oxidation by tertiary-butyl hydroperoxide in pre-implantation mouse embryos. Arch. Biochem. Biophys. 321, 6-12 (1995).
21. Hodgson, E. K., and Fridovich, I. The interaction of bovine superoxide dismutase and hydrogen peroxide: Chemiluminescence and peroxidation. Biochemistry 14, 5299-5303 (1975).
22. Jahnkhe, L. S., Hull, M. R., and Long, S. P. Chilling stress and oxygen metabolizing enzymes in Zea mays and Zea diploperennis. Plant Cell Environ. 14, 97-104 (1991).
23. Jahoor, F., Wykes, L. J., Reeds, P. J., Henry, J. F., Del Rosario, M. R., and Frazer, M. E. Protein-deficient pigs cannot maintain reduced glutathione homeostasis when subjected to the stress of inflammation. J. Nutr. 125, 1462-1472 (1995).
24. Kehrer, J. P., and Lund, L. G. Cellular reducing equivalents and oxidative stress. Free Rad. Biol. Med. 17, 65-75 (1994).
25. Lee, R. E. Insect cold-hardiness: To freeze or not to freeze. BioScience 39, 308-313 (1989).
26. Lee, R. E., and Baust, J. G. Respiratory metabolism of the antarctic tick, Ixodes uriae. Comp. Biochem. Physiol. 72A, 161-171 (1982).
27. Lee, R. E., Chen, C. P., and Denlinger, D. L. A rapid cold-hardening process in insects. Science 238, 1415-1417 (1987).
28. Leopold, R. A. Cytological and cytochemical studies on the ejaculatory duct and accessory secretion in M. domestica. J. Insect Physiol. 16, 1859-1872 (1970).
29. Leprince, O., Deltour, R., Thorpe, P. C., Atherton, N. M., and Hendry, G. A. F. The role of free radicals and radical processing systems in loss of desiccation tolerance in germinating maize (Zea mays L.). New Phytol. 116, 573-580 (1990).
30. Leprince, O., Atherton, N. M., Deltour, R., and Hendry, G. A. F. The involvement of respiration in free radical processes during loss of desiccation tolerance in germinating Zea mays L. Plant Physiol. 104, 1333-1339 (1994).
31. Meister, A. Selective modification of glutathione metabolism. Science 220, 472-478 (1988).
32. Morris, G. J., Coulson, G., Meyer, M. A., McLellan, M. R., Fuller, B. J., Grout, B. W. W., Pritchard, H. W., and Knight, S. C. Cold shock - A widespread cellular reaction. Cryo-Letters 4, 179-192 (1983).
33. Morris, G. J., and Watson, P. F. Cold shock injury -A comprehensive bibliography. Cryo-Letters 5, 352-372 (1984).
34. Nickla, H., Anderson, J. A., and Palzkill, T. Enzymes involved in oxygen detoxification during development of Drosophila melanogaster. Experientia 39, 610-612 (1983).
35. Prasad, T. K., Anderson, M. D., Martin, B. A., and Stewart, C. R. Evidence for chilling-induced oxidative stress in maize seedlings and a regulatory role for hydrogen peroxide. Plant Cell 6, 65-74 (1994).
36. Quinn, P. J. A lipid-phase separation model of low-temperature damage to biological membranes. Cryobiology 22, 128-146 (1985).
37. Salo, D. C., Pacifici, R. E., Lin, S. W., Giulivi, C., and Davies, K. J. A. Superoxide dismutase undergoes proteolysis and fragmentation following oxidative modification and inactivation. J. Biol. Chem. 265, 11919-11927 (1990).
38. Senaratna, T., Mackay, C. E., McKersie, B. D., and Fletcher, R. A. Uniconazole-induced chilling tolerance to tomato and its relationship to antioxidant content. J. Plant Physiol. 133, 56-61 (1988).
39. Sen Gupta, A., Heinen, J. L., Holaday, A. S., Burke, J. J., and Allen, R. D. Increased resistance to oxidative stress in transgenic plants that overexpress chloroplastic Cu/Zn superoxide dismutase. Proc. Natl. Acad. Sci. USA 90, 1629-1633 (1993).
40. Sohal, R. S. The free radical hypothesis of aging: An appraisal of the current status. Aging Clin. Exp. Res. 5, 3-17 (1993).
41. Trolinder, N. L., and Allen, R. D. Expression of chloroplast localized Mn SOD in transgenic cotton. J. Cell Biochem. 18A, 97 (1994).
42. Walker, M. A., and McKersie, B. D. Role of ascorbate-glutathione antioxidant system in chilling stress. HortScience 17, 173-186 (1993).
43. Yamashita, N., Nishida, M., Hoshida, S., Kuzuya, T., Hori, M., Taniguchi, N., Kamada, T., and Tada, M. Induction of manganese superoxide dismutase in rat cardiac myocytes increases tolerance to hypoxia 24 hours after preconditioning. J. Clin. Invest. 94, 2193-2199 (1994).
44. Zaman, K., MacGill, R. S., Johnson, J. E., Ahmad, S., and Pardini, R. S. An insect model for assessing mercury toxicity: Effect of mercury on antioxidant enzyme activities of the housefly (Musca domestica) and the cabbage looper moth (Trichoplusia ni). Arch. Environ. Contam. Toxicol. 26, 114-118 (1994).
45. Zhu, D., and Scandalios, J. G. Differential accumulation of manganese-superoxide dismutase transcripts in maize in response to abscisic acid and high osmoticum. Plant Physiol. 106, 173-178 (1994).