|Title||Antioxidant defences of the apoplast|
|Author(s)||Vanacker, H.; Harbinson, J.; Ruisch, J.; Carver, T.L.W.; Foyer, C.H.|
|Source||Protoplasma 205 (1998)1-4. - ISSN 0033-183X - p. 129 - 140.|
|Department(s)||Horticulture & Product Physiology|
|Publication type||Refereed Article in a scientific journal|
|Keyword(s)||Antioxidants - Apoplast - Chlorophyll a fluorescence - Powdery mildew - Superoxide dismutase|
The apoplast of barley and oat leaves contained superoxide dismutase (SOD), catalase, ascorbate peroxidase, dehydroascorbate reductase, monodehydroascorbate reductase, and glutathione reductase activities. The activities of these enzymes in the apoplastic extracts were greatly modified 24 h after inoculation with the biotrophic fungal pathogen Blumeria graminis. The quantum efficiency of photosystem II, which is related to photosynthetic electron transport flux, was comparable in inoculated and healthy leaves during this period. Apoplastic soluble acid invertase activity was also modified in inoculated leaves. Inoculation-dependent increases in apoplastic SOD activity were observed in all lines. Major bands of SOD activity, observed in apoplastic protein extracts by activity staining of gels following isoelectric focusing, were similar to those observed in whole leaves but two additional minor bands were found in the apoplastic fraction. The apoplastic extracts contained substantial amounts of dehydroascorbate (DHA) but little or no glutathione (GSH). Biotic stress decreased apoplastic ascorbate and DHA but increased apoplastic GSH in resistant lines. The antioxidant cycle enzymes may function to remove apoplastic H2O2 with ascorbate and GSH derived from the cytoplasm. DHA and oxidized glutathione may be reduced in the apoplast or returned to the cytosol for rereduction.