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Division of Nephrology, Hypertension and Transplantation, Department of Medicine, University of Florida, Gainesville, Florida 32610
Cytochrome
c-mediated activation of caspase-3 is the final common
pathway for most signals that induce apoptosis. Before release of cytochrome c from mitochondria, K+ and
Cl
efflux and intracellular acidification must occur. We
have utilized an in vitro assay to examine the role of pH, cations,
anions, and uncharged molecules on the process of cytochrome
c-mediated activation of procaspase-3. In this cell-free
system, a pH above 7.4 severely suppressed the activation of
procaspase-3 but not the activity of caspase-3. KCl, NaCl, and other
salts all inhibited caspase activation, but uncharged molecules did
not. Comparison of the inhibitory capacity of various salts suggests
that the crucial element in causing suppression is the cation. The
inhibition of alkaline pH could be overcome by increasing
concentrations of cytochrome c, whereas the inhibition of
ionic charge could not, suggesting that pH and salts affect the
activation of caspase-3 by different mechanisms.
apoptosis; cell death; potassium
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