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. 1993 Dec;103(4):1385–1391. doi: 10.1104/pp.103.4.1385

Molecular Responses to Photooxidative Stress in Pinus sylvestris (L.) (II. Differential Expression of CuZn-Superoxide Dismutases and Glutathione Reductase.

S Karpinski 1, G Wingsle 1, B Karpinska 1, J E Hallgren 1
PMCID: PMC159130  PMID: 12232032

Abstract

The influence of photooxidative stress on genes expressing superoxide dismutase (Sod) and glutathione reductase (Gor) was analyzed in needles of top and side shoots of 3-year-old Pinus sylvestris (L.) seedlings. The study was carried out in the field during spring recovery. From mid-April the top shoots of seedlings protruded above the snow and thus were exposed to sunlight, whereas the side shoots were covered with snow until May 4. Needles were sampled from top and side shoots on five different occasions. At the beginning of May the mRNA levels for cytosolic CuZn-Sod were significantly higher in top-shoot needles than in side-shoot needles. Similar results were obtained for chloroplastic CuZn-Sod mRNA. After May 6 we could not detect any significant differences between top- and side-shoot needles for either CuZn-Sod mRNA level. Transcript accumulation for the chloroplastic CuZn-Sod was up to 4-fold higher than for cytosolic CuZn-Sod in both types of shoots. On June 1 minimum transcript levels were observed for both CuZn-SOD isoforms. Protein activity analysis for CuZn-SOD isozymes did not reveal any significant differences between top- and side-shoot needles during the whole period of measurements. The mRNA level for chloroplastic Gor was similar in both types of shoots. However, the total GR activity was significantly higher in top-shoot needles than in side-shoot needles at the beginning of May. The analysis of mRNA accumulation for chloroplastic CuZn-Sod and Gor indicates that transcript levels were at least 5- to 20-fold higher for CuZn-Sod than for chloroplastic Gor. The differential expressions of Sod and Gor genes are discussed in relation to regulation of the enzymic scavenging system during photooxidative stress conditions.

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Selected References

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  1. Beauchamp C., Fridovich I. Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal Biochem. 1971 Nov;44(1):276–287. doi: 10.1016/0003-2697(71)90370-8. [DOI] [PubMed] [Google Scholar]
  2. Bowler C., Alliotte T., De Loose M., Van Montagu M., Inzé D. The induction of manganese superoxide dismutase in response to stress in Nicotiana plumbaginifolia. EMBO J. 1989 Jan;8(1):31–38. doi: 10.1002/j.1460-2075.1989.tb03345.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bowler C., Slooten L., Vandenbranden S., De Rycke R., Botterman J., Sybesma C., Van Montagu M., Inzé D. Manganese superoxide dismutase can reduce cellular damage mediated by oxygen radicals in transgenic plants. EMBO J. 1991 Jul;10(7):1723–1732. doi: 10.1002/j.1460-2075.1991.tb07696.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Cakmak I., Marschner H. Magnesium deficiency and high light intensity enhance activities of superoxide dismutase, ascorbate peroxidase, and glutathione reductase in bean leaves. Plant Physiol. 1992 Apr;98(4):1222–1227. doi: 10.1104/pp.98.4.1222. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Creissen G., Edwards E. A., Enard C., Wellburn A., Mullineaux P. Molecular characterization of glutathione reductase cDNAs from pea (Pisum sativum L.). Plant J. 1992 Jan;2(1):129–131. [PubMed] [Google Scholar]
  6. Gupta A. S., Heinen J. L., Holaday A. S., Burke J. J., Allen R. D. Increased resistance to oxidative stress in transgenic plants that overexpress chloroplastic Cu/Zn superoxide dismutase. Proc Natl Acad Sci U S A. 1993 Feb 15;90(4):1629–1633. doi: 10.1073/pnas.90.4.1629. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hodgson E. K., Fridovich I. The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: inactivation of the enzyme. Biochemistry. 1975 Dec 2;14(24):5294–5299. doi: 10.1021/bi00695a010. [DOI] [PubMed] [Google Scholar]
  8. Hollander M. C., Fornace A. J., Jr Estimation of relative mRNA content by filter hybridization to a polythymidylate probe. Biotechniques. 1990 Aug;9(2):174–179. [PubMed] [Google Scholar]
  9. Madamanchi N. R., Anderson J. V., Alscher R. G., Cramer C. L., Hess J. L. Purification of Multiple Forms of Glutathione Reductase from Pea (Pisum sativum L.) Seedlings and Enzyme Levels in Ozone-Fumigated Pea Leaves. Plant Physiol. 1992 Sep;100(1):138–145. doi: 10.1104/pp.100.1.138. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Marklund S. Spectrophotometric study of spontaneous disproportionation of superoxide anion radical and sensitive direct assay for superoxide dismutase. J Biol Chem. 1976 Dec 10;251(23):7504–7507. [PubMed] [Google Scholar]
  11. Matters G. L., Scandalios J. G. Effect of the free radical-generating herbicide paraquat on the expression of the superoxide dismutase (Sod) genes in maize. Biochim Biophys Acta. 1986 Jun 3;882(1):29–38. doi: 10.1016/0304-4165(86)90051-6. [DOI] [PubMed] [Google Scholar]
  12. Perl-Treves R., Galun E. The tomato Cu,Zn superoxide dismutase genes are developmentally regulated and respond to light and stress. Plant Mol Biol. 1991 Oct;17(4):745–760. doi: 10.1007/BF00037058. [DOI] [PubMed] [Google Scholar]
  13. Tsang E. W., Bowler C., Hérouart D., Van Camp W., Villarroel R., Genetello C., Van Montagu M., Inzé D. Differential regulation of superoxide dismutases in plants exposed to environmental stress. Plant Cell. 1991 Aug;3(8):783–792. doi: 10.1105/tpc.3.8.783. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Williamson J. D., Scandalios J. G. Differential response of maize catalases and superoxide dismutases to the photoactivated fungal toxin cercosporin. Plant J. 1992 May;2(3):351–358. doi: 10.1111/j.1365-313x.1992.00351.x. [DOI] [PubMed] [Google Scholar]
  15. Wingsle G., Gardeström P., Hällgren J. E., Karpinski S. Isolation, Purification, and Subcellular Localization of Isozymes of Superoxide Dismutase from Scots Pine (Pinus sylvestris L.) Needles. Plant Physiol. 1991 Jan;95(1):21–28. doi: 10.1104/pp.95.1.21. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Young L. C., Conn E. E. The Reduction and Oxidation of Glutathione by Plant Mitochondria. Plant Physiol. 1956 May;31(3):205–211. doi: 10.1104/pp.31.3.205. [DOI] [PMC free article] [PubMed] [Google Scholar]

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