Reactive oxygen species and antioxidants: Relationships in green cells

Physiologia Plantarum - Tập 100 Số 2 - Trang 224-233 - 1997
Ruth G. Alscher1, Janet L. Donahue1, Carole L. Cramer1
1Department of Plant Pathology, Physiology and Weed Science, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061-0330, USA

Tóm tắt

The imposition of oxidative stress leads to increased production of reactive oxygen species (ROS) in plant cells. Orchestrated defense processes ensue that have much in common between stresses, yet are also particular to the site of action of the stress and its concentration. Possible functional roles of these responses include, but are not restricted to, the protection of the photosynthetic machinery, the preservation of membrane integrity and the protection of DNA and proteins. Superimposed upon our understanding of cellular mechanisms for protection against abiotic stress is a newly discovered role of ROS in signalling and defense response to pathogens (J. L. Dangl, R. A. Dietrich and M. S. Richberg. 1996. Plant Cell 8: 1793–1807). Evidence to date suggests a coordinated response to ROS among different members of the superoxide dismutase (SOD) gene families. A further layer of complexity is afforded by reports of coordination of expression between ascorbate peroxidase and SOD genes. Our understanding of the signalling mechanisms that underlie these coordinated events is in its infancy. An exciting future lies ahead in which the orchestration of successful antioxidant stress responses will be gradually revealed. Current data suggest that complex regulatory mechanisms function at both the gene and protein level to coordinate antioxidant responses and that a critical role is played by organellar localization and inter‐compartment coordination.

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Tài liệu tham khảo

10.1104/pp.107.4.1049

Alscher R. G., 1993, Antioxidants in Higher Plants

10.1093/jxb/38.1.99

10.1104/pp.98.2.501

10.1093/oxfordjournals.pcp.a078132

Asada K., 1994, Causes of Photooxidatives Stress and Amelioration of Defense Systems in Plants, 77

AsadaTakahashi M. A., 1977, Biochemical and Medical Aspects of Active Oxygen, 45

10.1016/0003-9861(81)90089-8

10.1080/07352689409701914

10.1104/pp.108.3.1151

Casano L. M., 1994, Hydroxyl radicals and a thylakoid‐bound endopeptidase are involved in light and oxygen‐induced proteolysis in oat chloroplasts, Plant Cell Physiol, 35, 145

10.1007/BF00395175

10.1104/pp.109.1.203

10.1042/bst0240465

Crosti N., 1985, Coordinate expression of Mn‐containing superoxide dismutase and Cu, Zn‐containing superoxide dismutase in human fibroblasts with trisomy 21, J. Cell Sci, 79, 95, 10.1242/jcs.79.1.95

10.2307/3870230

Davies K. J. A., 1987, Protein damage and degradation by oxygen radicals, J. Biol. Chem, 262, 9895, 10.1016/S0021-9258(18)48018-0

Demmig‐Adams B., 1993, Antioxidants in Higher Plants, 91

10.1104/pp.113.1.249

10.1111/j.1469-8137.1993.tb03747.x

Edwards E., 1994, Synthesis and properties of glutathione reductase in stressed peas, Planta, 192, 137

10.1111/j.1399-3054.1997.tb04779.x

10.1104/pp.61.1.119

Foyer C. H., 1993, Antioxidants in Higher Plants, 31

Foyer C. H., 1994, Causes of Photooxidative Stress and Amelioration of Defense Systems in Plants

10.1111/j.1399-3054.1994.tb03042.x

10.1146/annurev.bi.64.070195.000525

10.1016/0168-9452(87)90145-2

10.1104/pp.112.4.1631

10.1016/0005-2728(94)00183-6

Gressel J., 1994, Causes of Photooxidative Stress and Amelioration of Defense Systems in Plants, 237

10.1016/0011-2240(84)90082-8

Hagar H., 1996, Role of reactive oxygen metabolites in DNA damage and cell death in chemical hypoxic injury to LLC‐PK1 cells, Am. J. Physiol, 271, F209

Halliwell B., 1989, Free Radicals in Biology and Medicine

Hammond‐Kosack K. E., 1996, Resistance gene‐dependent plant defense responses, Plant Cell, 8, 1773

10.1128/jb.177.22.6330-6337.1995

Hausladen A., 1993, Antioxidants in Higher Plants, 1

10.1104/pp.105.1.205

10.1104/pp.105.1.215

Hess J. L., 1993, Antioxidants in Higher Plants, 111

Hopkin K. A., 1992, Functional differences between manganese and iron superoxide dismutases in Escherichia coli K‐12, J. Biol. Chem, 267, 24253, 10.1016/S0021-9258(18)35758-2

10.1016/0014-5793(96)00332-8

Kanematsu S., 1990, Characteristic amino acid sequences of chloroplast and cytosol isozymes of CuZn‐superoxide dismutase in spinach, rice and horsetail, Plant Cell Physiol, 31, 99

10.1007/BF00028883

10.1007/BF00040670

10.1007/978-94-015-8927-7_10

10.1104/pp.97.1.88

10.1006/pest.1994.1004

10.1007/BF00039523

10.1016/0168-9452(90)90114-4

10.1016/0304-4165(86)90051-6

Matters G. L., 1987, Synthesis of isozymes of superoxide dismutase in maize leaves in response to O3, SO2 and elevated O. J. Exp. Bot, 38, 842

10.1104/pp.111.4.1177

10.1016/0003-9861(51)90082-3

10.1111/j.1399-3054.1990.tb06756.x

Mittler R., 1992, Molecular cloning and characterization of a gene encoding pea cytosolic ascorbate peroxidase, J. Biol. Chem, 267, 21802, 10.1016/S0021-9258(19)36683-9

10.1111/j.1365-313X.1994.00397.x

Ogawa K., 1995, Attachment of Cu, Zn SOD to thylakoid membranes at the site of superoxide generation (PSI) in spincah chloroplasts: Detection by immunogold labeling after rapid freezing, Plant Cell Physiol, 36, 565

10.1016/S0176-1617(96)80258-6

10.1093/jxb/46.special_issue.1351

Pacifici R. E., 1993, Hydophobicity as the signal for selective degradation of hydroxyl radical‐modified hemoglobin by the multicatalytic proteinase complex, proteasome, J. Biol. Chem, 268, 15405, 10.1016/S0021-9258(18)82272-4

10.1007/BF00220915

10.1007/BF00037058

10.1104/pp.99.4.1388

10.2307/3869675

10.1146/annurev.pp.44.060193.001023

10.1016/S0021-9258(19)38488-1

10.1007/978-94-011-1294-9_8

10.1007/978-94-015-8927-7_8

10.1073/pnas.90.4.1629

10.1007/BF00182394

10.1007/BF00027496

Tsang E. W., 1991, Differential regulation of superoxide dismutases in plants exposed to environmental stress, Plant Cell, 3, 783

10.1073/pnas.87.24.9903

10.1038/nbt0294-165

10.1104/pp.112.4.1703

10.1073/pnas.93.2.856

10.1104/pp.106.3.1007

Williamson J. D., 1992, Differential response of maize catalases and superoxide dismutases to the photoactivated fungal toxin cercosporin, Plant J, 2, 351, 10.1046/j.1365-313X.1992.t01-33-00999.x

10.1016/0891-5849(94)90019-1

10.1074/jbc.271.44.27408