Plant Physiology Preview
Published on March 10, 2006; 10.1104/pp.106.078683
Received February 3, 2006
Returned for revision February 24, 2006
Accepted February 27, 2006
Cytochrome c is Released in a Reactive Oxygen Species-Dependent Manner and is Degraded via Caspase-like proteases in Tobacco BY-2 Cells en Route to Heat Shock-Induced Cell Death
Rosa Anna Vacca , Daniela Valenti , Antonella Bobba , Riccardo Sandro Merafina , Salvatore Passarella , and Ersilia Marra *
Istituto di Biomembrane e Bioenergetica, Consiglio Nazionale delle Ricerche, Via Amendola 165/A, I-70126 Bari, Italy
Dipartimento di Scienze per la Salute, Università del Molise, Via De Sanctis, I-86100 Campobasso, Italy
* Corresponding author; email: e.marra{at}ibbe.cnr.it.
In order to gain some insight into the mechanism of plant programmed cell death (PCD), certain features of cytochrome c (cyt c) release were investigated in heat-shocked Nicotiana tabacum Bright Yellow-2 (TBY-2) cells, in the 2-6 h time range. We found that two hours after heat shock cyt c is released from intact mitochondria into the cytoplasm as a functionally active protein. Such a release did not occur in the presence of superoxide anion dismutase and catalase thus showing that it depends on reactive oxygen species (ROS). Interestingly, ROS production due to xanthine plus xanthine oxidase results in cyt c release in sister control cultures. Maximum cyt c release was found 2 h after heat shock; later, activation of caspase-3 like protease was found to increase with time. Activation of this protease did not occur in the presence of ROS scavenger enzymes. The released cyt c was found to be progressively degraded in a manner prevented by either the broad range caspase inhibitor (z-VAD-fmk) or the specific inhibitor of caspase-3 (AC-DEVD-CHO) which themselves have no effect on the cyt c release. In the presence of these inhibitors, a significant increase in survival of the cells undergoing PCD was found.
We conclude that ROS can trigger release of cyt c but by themselves do not cause cell death which requires necessarily caspase-like activation.
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