Crosstalk of nitric oxide with calcium induced tolerance of tall fescue leaves to high irradiance
- 95 Downloads
Calcium ion (Ca2+) is essential secondary messenger in plant signaling networks. In this study, the effect of Ca2+ on oxidative damage caused by a high irradiance (HI) was investigated in the leaves of two cultivars of tall fescue (Arid3 and Houndog5). Pretreatment of the tall fescue leaves with a CaCl2 solution significantly increased Ca2+ content and intrinsic HI tolerance due to a decreased ion leakage and content of malondialdehyde, hydrogen peroxide, and superoxide radicals. Moreover, the activities of superoxide dismutase, catalase, ascorbate peroxidase, and glutathione reductase increased in both the cultivars in the presence of Ca2+ under the HI stress. In contrast, treatments with a Ca2+ chelator ethylene glycol-bis(2-aminoethylether)-N,N,N′,N′-tetraacetic acid (EGTA) or a plasma membrane Ca2+ channel blocker LaCl3 reversed these effects. On the other hand, a pronounced increase in nitric oxide synthase-like activity and NO release by exogenous Ca2+ treatment was observed in the tolerant Arid3 plants after exposure to the HI, whereas only a small increase was observed in more sensitive Houndog5. Moreover, the inhibition of NO production by 2-(4-carboxy-2-phenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide or N ω-nitro-L-arginine blocked the protective effect of exogenous Ca2+, whereas the inhibition of Ca2+ by EGTA or LaCl3 had no influence on the protective effect of NO. The results indicate that NO might be involved in the Ca2+-induced activities of antioxidant enzymes further protecting against HI-induced oxidative damage. This protective mechanism was found to be more efficient in Arid3 than in Houndog5.
Additional key wordsantioxidant enzymes Festuca arundinacea hydrogen peroxide malondialdehyde
ethylene glycol-bis(2-aminoethylether)-N,N,N′,N′-tetraacetic acid
nitric oxide synthase
photosynthetic photon flux density
reactive oxygen species
Unable to display preview. Download preview PDF.
- Nakano, Y., Asada K.: Hydrogen peroxide is scavenged by ascorbate-specific peroxidase in spinach chloroplasts. — Plant Cell Physiol. 22: 867–880, 1981.Google Scholar