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P38 mediates apoptosis in hippocampal slices exposed to hyperosmotic stress


, : P38 mediates apoptosis in hippocampal slices exposed to hyperosmotic stress. Society for Neuroscience Abstract Viewer & Itinerary Planner : Abstract No 303 14

The neuronal response to cellular insults such as osmotic stress or ischemia occurs by signaling via stress-activated protein kinases (SAPKs), p38 and c-Jun N-terminal kinase (JNK). Hyperosmotic stress of rat hippocampal slices, produced by addition of 300 mM sorbitol to the incubation buffer, activates p38 as measured by phospho-immunoblotting and in vitro immunocomplex kinase assay with ATF-2 as substrate. In contrast, sorbitol does not stimulate JNK activity above basal levels. Activation of p38 occurs upon 15 min of osmotic stress and is maintained through 6 hr of hyperosmolarity. Since one process modulated by SAPKs is apoptosis, early apoptotic events (translocation of cytochrome c; activation of caspase-3) were examined by immunoblotting as a function of p38 activation. Cytochrome c is released into the cytosolic fraction of slices incubated for 1.5 hr with sorbitol. Furthermore, 3 hr of hyperosmotic conditions activates caspase-3 with cleavage of the nuclear repair enzyme, poly(ADP-ribose) polymerase (PARP). At this time point, 10 muM staurosporine, another apoptotic stimulus, does not elicit the same responses. Inhibition of p38 kinase activity with the selective compound, SB202190, dose-dependently reduces caspase-3 activation and attenuates PARP cleavage. An inhibitor of JNK, SP600125, does not prevent hyperosmotic activation of caspase-3. These results reveal sorbitol to be a potent stimulator of apoptosis in hippocampal slices. Sorbitol-induced hyperosmolarity selectively produces prolonged p38 activation and identifies the cytochrome c/caspase-3 apoptotic pathway as a downstream correlate of p38 signaling.

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