Inhibition of caspase activity revealed that the bulk of the lamin b both b1 and b2 was mislocalized to the cytoplasm excluding the trivial possibility that failure to incorporate lamin b into the nuclear lamina was due to lamin degradation. Inhibition of caspase activity revealed that the bulk of the lamin b both b1 and b2 was mislocalized to the cytoplasm excluding the trivial possibility that failure to incorporate lamin b into the nuclear lamina was due to lamin degradation. Activation of casp6 was upstream of casp3 7 activation and its inhibition was sufficient to prevent cell death in our system.
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