title: Localization of reactive oxygen species and change of antioxidant capacities in mesophyll and bundle sheath chloroplasts of maize under salinity.
abstract: In maize, the structure of bundle sheath cell (BSC) chloroplasts is less subject to salinity stress than that of mesophyll cell (MC) chloroplasts. To elucidate the difference in sensitivity to salinity, antioxidant capacities and localization of reactive oxygen species were investigated in both chloroplasts. Transmission electron microscopic observation showed that O2 (-) localization was found in both chloroplasts under salinity, but the accumulation was much greater in MC chloroplasts. H2 O2 localization was observed only in MC chloroplasts of salt-treated plants. In isolated chloroplasts, the activities of superoxide dismutase (SOD, EC 1.15.1.1), ascorbate peroxidase (APX, EC 1.11.1.11) and dehydroascorbate reductase (DHAR, EC 1.8.5.1) were increased by salinity. While the enhancement of SOD activity was similar in both chloroplasts, the increase of APX and DHAR activities were more pronounced in BSC chloroplasts than in MC chloroplasts. Monodehydroascorbate reductase (MDHAR, EC 1.6.5.4) and glutathione reductase (GR, EC 1.6.4.2) were undetectable in BSC chloroplasts, while they increased in MC chloroplasts under salinity. Although ascorbate content increased by salinity only in BSC chloroplasts, glutathione content increased significantly in both chloroplasts, and was higher in MC chloroplasts than in BSC chloroplasts. The content of thiobarbituric acid-reactive substances, which is an indicator of lipid peroxidation, was significantly increased by salinity in both chloroplasts. These results suggested O2 (-) -scavenging capacity was comparable between both chloroplasts, whereas H2 O2 -scavenging capacity was lower in MC chloroplasts than in BSC chloroplasts. Moreover, the increased lipid peroxidation under salinity was associated with the structural alteration in MC chloroplasts, while it had less impact on the structure of BSC chloroplasts.
authors.affiliation: Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, 464-8601, Japan.
authors.forename: Eiji
authors.initials: E
authors.lastname: Omoto
authors.forename: Haruto
authors.initials: H
authors.lastname: Nagao
authors.forename: Mitsutaka
authors.initials: M
authors.lastname: Taniguchi
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Miyake
mesh_terms: D000975:Antioxidants / Q000378:metabolism*; D060387:Ascorbate Peroxidases / Q000378:metabolism; D001205:Ascorbic Acid / Q000378:metabolism; D002736:Chloroplasts / Q000378:metabolism*; D005978:Glutathione / Q000378:metabolism; D005980:Glutathione Reductase / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000378:metabolism; D015227:Lipid Peroxidation; D058503:Mesophyll Cells / Q000378:metabolism*; D010088:Oxidoreductases / Q000378:metabolism; D017382:Reactive Oxygen Species / Q000378:metabolism*; D054712:Salinity; D013482:Superoxide Dismutase / Q000378:metabolism; D017392:Thiobarbituric Acid Reactive Substances / Q000378:metabolism; D003313:Zea mays / Q000378:metabolism*
chemical_list: D000975:Antioxidants; D017382:Reactive Oxygen Species; D017392:Thiobarbituric Acid Reactive Substances; D006861:Hydrogen Peroxide; D010088:Oxidoreductases; D060387:Ascorbate Peroxidases; D013482:Superoxide Dismutase; D005980:Glutathione Reductase; C020666:glutathione dehydrogenase (ascorbate); D005978:Glutathione; D001205:Ascorbic Acid