NDLI: Activation of plasmalemmal NADPH oxidase in etiolated maize seedlings exposed to chilling temperatures

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Activation of plasmalemmal NADPH oxidase in etiolated maize seedlings exposed to chilling temperatures

Content Provider	Springer Nature Link
Author	Piotrovskii, M. S. Shevyreva, T. A. Zhestkova, I. M. Trofimova, M. S.
Copyright Year	2011
Abstract	Five-day-old etiolated seedlings of maize (Zea mays L.) were used to study the kinetics of hydrogen peroxide formation upon lowering growth temperature from 25 to 6°C. The total content of hydrogen peroxide in root and shoot tissues increased by 30–40% after 2-h cooling compared to the control level but returned to the initial level or decreased even lower after 24-h cooling. In order to prove the involvement of plasma membrane NADPH oxidase in changes of hydrogen peroxide content upon cooling, isolated plasma membranes were obtained from untreated plants and from seedlings chilled at 6°C for 2 and 24 h. The NADPH-dependent generation of superoxide anion radical in isolated plasma membranes was quantified by measuring the rate of formazan production from the tetrazolium salt XTT. The activity of plasma membrane NADPH oxidase in shoots was 50 ± 9 nmol O$_{2}$/(mg protein min), which was 1.5 times higher than the activity in roots. The enzyme activity in plasma membranes was inhibited by low concentrations of diphenyleneiodonium. The effective concentration EC$_{50}$ was 5.10 μM for shoots and 9.05 μM for roots. The activity of plasma membrane NADPH oxidase increased after 2-h cooling of seedlings but reversed to the control level after 24-h cooling. This transient activation of NADPH oxidase upon cooling was similar to the pattern of hydrogen peroxide formation in shoots and roots. Analysis of NADPH oxidase activity of plasma membrane proteins after their separation in denaturing conditions followed by subsequent renaturation revealed four diphenyleneiodonium-sensitive bands with mol wt of 130, 88, 51, and 48 kD. Western blot analysis of the reaction with antibodies against the catalytic domain of phagocyte NADPH oxidase revealed the proteins with mol wt of only 88 and 48 kD. The properties of molecular organization of plasma membrane NADPH oxidase are discussed in terms of its role in cell signaling.
Starting Page	290
Ending Page	298
Page Count	9
File Format	PDF
ISSN	10214437
Journal	Russian Journal of Plant Physiology
Volume Number	58
Issue Number	2
e-ISSN	16083407
Language	English
Publisher	SP MAIK Nauka/Interperiodica
Publisher Date	2011-03-12
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Zea mays plasmalemma NADPH oxidase activity in gel immunodetection Plant Sciences Plant Physiology
Content Type	Text
Resource Type	Article
Subject	Plant Science

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