
%0 Journal Article
%A Biasi, Margherita G. De 
%A Astolfi, Stefania 
%A Acampora, Andrea 
%A Zuchi, Sabrina 
%A Fonzo, Valentina 
%A Santangelo, Enrico 
%A Caccia, Riccardo 
%A Badiani, Maurizio 
%A Soressi, Gian Piero 
%T A H<emph type="8">2</emph>O<emph type="8">2</emph>-forming peroxidase rather than a NAD(P)H-dependent O<emph type="8">2</emph><emph type="7">&#8226;&#8211;</emph> synthase may be the major player in cell death responses controlled by the <emph type="2">Pto&#8211;Fen</emph> complex following fenthion treatment
%J Functional Plant Biology
%D 2003/04/17
%V 30
%N 4
%P 409-417
%K antioxidant enzymes, ATPase, fenthion, glucose oxidase, Lycopersicon esculentum Mill., tomato, transgenic plants.
%R https://doi.org/10.1071/FP02187
%U https://www.publish.csiro.au/paper/FP02187 
%X Four tomato (Lycopersicon esculentum Mill.) near-isogenic lines were treated by foliar spraying with the insecticide fenthion. Two, Riogrande and Rimone, differed from each other only for the presence in the latter of the Fen gene, conferring propensity to develop foliar symptoms upon exposure to fenthion. The other two, namely RC332 and RC131, were the transgenic versions of Riogrande and Rimone, respectively, harbouring the Gox gene encoding for glucose oxidase of Aspergillus niger. The production of H2O2 as well as the activities of H+-ATPase, NAD(P)H-dependent superoxide synthase, catalase, peroxidase, and Cu,Zn-superoxide dismutase were evaluated in the foliar tissues up to 24 h after exposure to fenthion. The Fen gene conferred sensitivity to fenthion, regardless of the expression of a Gox transgene. A prolonged accumulation of H2O2 was observed in the leaves of Rimone and of RC131, which was instead transient in Riogrande and in RC332. In all the tomato lines, exposure to fenthion induced rapid but transient changes in the activities of most enzymes. The only exception was peroxidase activity in the leaves of Rimone and of RC131, which steadily increased until the end of the sampling period. It is suggested that the sensitivity of Rimone to fenthion might be due to the sustained activity of a H2O2-forming peroxidase. 
