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Oxidative Stress Responses Accompanying Photoinactivation of Catalase in NaCI‐treated Rye Leaves
Author(s) -
Streb P.,
Feierabend J.
Publication year - 1996
Publication title -
botanica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.871
H-Index - 87
eISSN - 1438-8677
pISSN - 0932-8629
DOI - 10.1111/j.1438-8677.1996.tb00552.x
Subject(s) - catalase , secale , glutathione reductase , glutathione , oxidative stress , chemistry , biochemistry , antioxidant , peroxidase , oxidative phosphorylation , glutathione peroxidase , enzyme , biology , botany
When segments of rye leaves ( Secale cereale L.) grown at 90 μmol m −2 s −1 PAR were incubated at a higher photon flux of 400–500 μ mol m −2 s −1 PAR in the presence of 0.2‐0.6 M NaCl, a preferential loss of catalase activity was induced. The extent of this decline increased with the concentration of NaCl. In addition, the accumulation of alternative antioxidative components, such as ascorbate, glutathione, glutathione reductase, or peroxidase, was inhibited. The total content of H 2 O 2 was, however, lower in catalase‐depleted than in untreated control leaves. The occurrence of strong oxidative stress in NaCl‐treated leaves was indicated by marked declines in the ratios of reduced to oxidized ascorbate and glutathione and by the degradation of chlorophyll in light. The specific elimination of catalase activity by the inhibitor aminotriazole was also accompanied by a rapid decline in the ratio of reduced to oxidized glutathione but other symptoms of oxidative stress were much less severe than in the presence of NaCl. However, all symptoms of photooxidative damage seen in NaCl‐treated leaves were closely mimicked by treatment with the translation inhibitor, cycloheximlde, in light. The results suggest that NaCl‐induced oxidative damage in light was predominantly mediated by the inhibition of protein synthesis. By this inhibition the resynthesis of catalase, which has a high turnover in light, was blocked and the leaves were thus depleted of catalase activity and, in addition, the intensification of alternative antioxidative systems was also prevented.