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The Journal of Neuroscience, October 1, 2000, 20(19):7246-7251
Calcineurin-Mediated BAD Dephosphorylation Activates the Caspase-3 Apoptotic Cascade in Traumatic Spinal Cord Injury
Joe E. Springer, Robert D. Azbill, Stephanie A. Nottingham, and Sarah E. Kennedy Department of Anatomy and Neurobiology, University of Kentucky Medical Center, Center for Spinal Cord and Brain Injury Research, Lexington, Kentucky 40536-0084
We report here that activation of the caspase-3 apoptotic cascade in spinal cord injury is regulated, in part, by calcineurin-mediated BAD dephosphorylation. BAD, a proapoptotic member of the bcl-2 gene family, is rapidly dephosphorylated after injury, dissociates from 14-3-3 in the cytosol, and translocates to the mitochondria of neurons where it binds to Bcl-xL. Pretreatment of animals with FK506, a potent inhibitor of calcineurin activity, or MK801, an NMDA glutamate receptor antagonist, blocked BAD dephosphorylation and abolished activation of the caspase-3 apoptotic cascade. These findings extend previous in vitro observations and are the first to implicate the involvement of glutamate-mediated calcineurin activation and BAD dephosphorylation as upstream, premitochondrial signaling events leading to caspase-3 activation in traumatic spinal cord injury.
Key words: calcineurin; caspase-3; FK506; glutamate receptors; NMDA; Bcl-xL; BAD translocation
Copyright © 2000 Society for Neuroscience 0270-6474/00/20197246-06$05.00/0
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