The developmental transition to flowering represses ascorbate peroxidase activity and induces enzymatic lipid peroxidation in leaf tissue in Arabidopsis thaliana
Zz. Ye et al., The developmental transition to flowering represses ascorbate peroxidase activity and induces enzymatic lipid peroxidation in leaf tissue in Arabidopsis thaliana, PLANT SCI, 158(1-2), 2000, pp. 115-127
Leaf senescence in many plant species is associated with increased oxidativ
e damage to cellular macromolecules by reactive oxygen species (ROS). Since
ROS levels and their damage products in many plants are known to increase
during senescence; it is possible that these changes are due to a decline i
n the levels of certain antioxidant enzymes. Using specific assays, we find
that the developmental transition to bolting and flowering is associated w
ith up to a 5-fold decline in ascorbate peroxidase activity and an increase
in chloroplastid superoxide dismutase. As expected, these changes are asso
ciated with a measured increase in lipid peroxidation products. By HPLC sep
aration of the products, we identified the different positional isomers and
find that stereospecific lipid peroxidation occurs after the bolting trans
ition. The product distribution suggests that enzyme-mediated lipid peroxid
ation. via a lipoxygenase, is responsible for the observed increase. Surpri
singly, though consistent with the known induction of antioxidant defenses
by hydrogen peroxide, the activity of APX rebounds with further development
(reproduction and seed setting) and this increase (up to 5-fold) is associ
ated with declines in lipid peroxidation and with the onset of visible sene
scence symptoms. Thus, in Arabidopsis, ROS increases are associated with th
e developmental transition to flowering, perhaps due to programmed declines
in APX activity, and apparently lead to the oxidative activation of lipoxy
genase and subsequent lipid peroxidation. The reactivation of APX at later
stages appears to help reduce the Lipid peroxidation rate, although the sen
escence program continues unabated. (C) 2000 Elsevier Science Ireland Ltd.
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