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P35 proteolysis occurs in a time-dependent manner in a rat model of permanent focal ischemia


, : P35 proteolysis occurs in a time-dependent manner in a rat model of permanent focal ischemia. Society for Neuroscience Abstracts 27(1): 548

Cyclin-dependent kinase 5 (cdk5) is required for proper neuronal development and function. However, increased cdk5 activity is also postulated to be associated with neurodegenerative disease. Notably, the calcium-activated protease calpain mediates the conversion of the cdk5 activator protein p35 to a C-terminal fragment known as p25, causing increased cdk5 activity. Moreover, dysregulation of calcium homeostasis and subsequent activation of calpain is thought to play a role in both Alzheimer's disease (AD) and stroke. In this study, the time course of brain calpain activation and loss of p35 was determined following permanent middle cerebral artery occlusion (pMCAO). Calpain activation was measured as the increase in calpain-mediated spectrin cleavage products. Sprague-Dawley rats were subjected to pMCAO for 30 min to 24 hrs. Contralateral and ipsilateral cortices were analyzed by western blot for p35 proteolysis and formation of the p25 product. p25 was detected in ipsilateral cortical lysates at both 2 and 4 hrs following the insult and decreased to baseline by 24 hrs. Loss of p35 and appearance of spectrin breakdown products followed a similar time course. Selective calpain inhibitors will be tested for their ability to prevent p35 cleavage using this model. Calpain inhibitors will also be tested using an in vitro model of calpain activation. Inhibition of p35 proteolysis to p25 may reduce both cdk5 activation and the abnormal protein phosphorylation found in a number of disease models.

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