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- W4244482844 abstract "Efflux of intracellular K+ and cell shrinkage are features of apoptosis in many experimental systems, and a regulatory role has been proposed for cytoplasmic [K+] in initiating apoptosis. We have investigated this in both death-receptor-mediated and chemical-induced apoptosis. Using Jurkat T cells pre-loaded with the K+ ion surrogate 86Rb+, we have demonstrated an efflux of intracellular K+ during apoptosis that was concomitant with, but did not precede, other apoptotic changes, including phosphatidylserine externalization, mitochondrial depolarization and cell shrinkage. To further clarify the role of K+ ions in apoptosis, cytoprotection by elevated extracellular [K+] was studied. Induction of apoptosis by diverse death-receptor and chemical stimuli in two cell lines was inhibited prior to phosphatidylserine externalization, mitochondrial depolarization, cytochrome c release and caspase activation. Using a cell-free system, we have demonstrated a novel mechanism by which increasing [K+] inhibited caspase activation. In control dATP-activated lysates, Apaf-1 oligomerized to a biologically active caspase processing ≈ 700kDa complex and an inactive ≈ 1.4 MDa complex. Increasing [K+] inhibited caspase activation by preventing formation of the ≈ 700kDa complex, but not of the inactive complex. Thus intracellular and extracellular [K+] markedly affect caspase activation and the initiation of apoptosis induced by both death-receptor ligation and chemical stress." @default.
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- W4244482844 date "2001-06-25" @default.
- W4244482844 modified "2023-10-15" @default.
- W4244482844 title "Elevated extracellular [K+] inhibits death-receptor- and chemical-mediated apoptosis prior to caspase activation and cytochrome c release" @default.
- W4244482844 doi "https://doi.org/10.1042/bj3570137" @default.
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