title: Redox control of caspases.
abstract: Caspases are critical mediators of apoptotic cell death. All members of the caspase family contain the sequence QACXG which contains the active site cysteine. The putative active site of caspase 3 contains a cysteine residue that is subject to redox control. Both thioredoxin and glutathione have been shown to be required for caspase-3 activity to induce apoptosis. The regulation of inducible caspase 3 activity by oxidation-reduction (redox) dependent mechanisms is reviewed. Up until a few years ago, reactive oxygen species (ROS) research mostly focussed on oxidative damage and ROS were thought to be a key trigger for cell death. This view has been refined, leading to the understanding that the biological function of ROS is determined by numerous variables such as concentration, chemical type and cellular localization. For example, ROS and reactive nitrogen species may intercept inducible cell death under certain circumstances via the redox regulation of inducible caspase activity and/or by depleting cellular energy stores. Likewise, death of unwanted diseased or degenerative cells may be facilitated by pharmacologically enhancing the thiol status of such cells using redox-active α-lipoic acid.
authors.affiliation: Laboratory of Molecular Medicine, Department of Surgery, 512 Heart and Lung Research Institute, The Ohio State University Medical Center, 473 W. 12th Avenue, Columbus, OH 43210, USA.
authors.forename: C K
authors.initials: CK
authors.lastname: Sen
authors.forename: S
authors.initials: S
authors.lastname: Roy