Abstract
Differnential sensitivity to the oxidant paraquat was observed in pea (Pisum sativum L.) based on cultivar and leaf age. To assess contributions of inductive responses of the antioxidant enzymes in short-term resistance to oxidative damage, activities of glutathione reductase (GR), superoxide dismutase (SOD), and ascorbate peroxidase (APX) and transcript levels for plastidic GR, Cu,Zn SOD, and cytosolic APX were determined. Responses to paraquat exposure from three different leaf age classes of pea were studied. Resistance was correlated with leaf age, photosynthetic rates, enzyme activities, and pretreatment levels of plastid GR and plastid Cu,Zn SOD transcripts. In response to paraquat, small increases in activities of GR and APX were observed in the more resistant leaves. These changes were not reflected at the mRNA level for the plastidic GR or Cu,Zn SOD. Paraquat-mediated increases in cytosolic APX mRNA occurred in all leaf types, irrespective of resistance. Developmentally controlled mechanisms determining basal antioxidant enzyme activities, and not inductive responses, appear to be critical factors mediating short-term oxidative stress resistance.
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- Amsellem Z., Jansen MAK., Driesenaar ARJ., Gressel J. Developmental Variability of Photooxidative Stress Tolerance in Paraquat-Resistant Conyza. Plant Physiol. 1993 Dec;103(4):1097–1106. doi: 10.1104/pp.103.4.1097. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Asada K., Kiso K. Initiation of aerobic oxidation of sulfite by illuminated spinach chloroplasts. Eur J Biochem. 1973 Mar 1;33(2):253–257. doi: 10.1111/j.1432-1033.1973.tb02677.x. [DOI] [PubMed] [Google Scholar]
- 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]
- 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. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
- Casano L. M., Martin M., Sabater B. Sensitivity of Superoxide Dismutase Transcript Levels and Activities to Oxidative Stress Is Lower in Mature-Senescent Than in Young Barley Leaves. Plant Physiol. 1994 Nov;106(3):1033–1039. doi: 10.1104/pp.106.3.1033. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Conklin P. L., Last R. L. Differential accumulation of antioxidant mRNAs in Arabidopsis thaliana exposed to ozone. Plant Physiol. 1995 Sep;109(1):203–212. doi: 10.1104/pp.109.1.203. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Graham I. A., Denby K. J., Leaver C. J. Carbon Catabolite Repression Regulates Glyoxylate Cycle Gene Expression in Cucumber. Plant Cell. 1994 May;6(5):761–772. doi: 10.1105/tpc.6.5.761. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- Hausladen A., Alscher R. G. Cold-hardiness-specific glutathione reductase isozymes in red spruce. Thermal dependence of kinetic parameters and possible regulatory mechanisms. Plant Physiol. 1994 May;105(1):215–223. doi: 10.1104/pp.105.1.215. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kardish N., Magal N., Aviv D., Galun E. The tomato gene for the chloroplastic Cu,Zn superoxide dismutase: regulation of expression imposed in transgenic tobacco plants by a short promoter. Plant Mol Biol. 1994 Aug;25(5):887–897. doi: 10.1007/BF00028883. [DOI] [PubMed] [Google Scholar]
- Kubo A., Saji H., Tanaka K., Kondo N. Expression of Arabidopsis cytosolic ascorbate peroxidase gene in response to ozone or sulfur dioxide. Plant Mol Biol. 1995 Nov;29(3):479–489. doi: 10.1007/BF00020979. [DOI] [PubMed] [Google Scholar]
- 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]
- Madamanchi N. R., Donahue J. L., Cramer C. L., Alscher R. G., Pedersen K. Differential response of Cu,Zn superoxide dismutases in two pea cultivars during a short-term exposure to sulfur dioxide. Plant Mol Biol. 1994 Oct;26(1):95–103. doi: 10.1007/BF00039523. [DOI] [PubMed] [Google Scholar]
- May M. J., Leaver C. J. Oxidative Stimulation of Glutathione Synthesis in Arabidopsis thaliana Suspension Cultures. Plant Physiol. 1993 Oct;103(2):621–627. doi: 10.1104/pp.103.2.621. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mittler R., Zilinskas B. A. Detection of ascorbate peroxidase activity in native gels by inhibition of the ascorbate-dependent reduction of nitroblue tetrazolium. Anal Biochem. 1993 Aug 1;212(2):540–546. doi: 10.1006/abio.1993.1366. [DOI] [PubMed] [Google Scholar]
- Mittler R., Zilinskas B. A. Regulation of pea cytosolic ascorbate peroxidase and other antioxidant enzymes during the progression of drought stress and following recovery from drought. Plant J. 1994 Mar;5(3):397–405. doi: 10.1111/j.1365-313x.1994.00397.x. [DOI] [PubMed] [Google Scholar]
- 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]
- Pitcher L. H., Zilinskas B. A. Overexpression of Copper/Zinc Superoxide Dismutase in the Cytosol of Transgenic Tobacco Confers Partial Resistance to Ozone-Induced Foliar Necrosis. Plant Physiol. 1996 Feb;110(2):583–588. doi: 10.1104/pp.110.2.583. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- 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]