Intracellular K+ suppresses the activation of apoptosis in lymphocytes

J Biol Chem. 1997 Nov 28;272(48):30567-76. doi: 10.1074/jbc.272.48.30567.

Abstract

Little is known about the mechanisms of suppression of apoptosis. We have addressed the novel possibility that the level of intracellular K+ regulates the apoptotic process by controlling the activity of death enzymes. We show that K+, at normal intracellular levels, inhibits both apoptotic DNA fragmentation and caspase-3(CPP32)-like protease activation, suggesting that intracellular K+ loss must occur early during apoptosis. Direct measurement of K+ by inductively coupled plasma/mass spectrometry and flow cytometry indicates a major decrease in intracellular K+ concentration in the apoptotic cell. Flow cytometric analysis revealed that caspase and nuclease activity were restricted to the subpopulation of cells with reduced K+. Disruption of the natural K+ electrochemical gradient suppressed the activity of both caspase and nuclease independent of the mode of activation of the apoptotic inducing agent, demonstrating that a decrease in intracellular K+ concentration is a necessary, early event in programmed cell death.

MeSH terms

  • Animals
  • Apoptosis* / drug effects
  • Caspase 3
  • Caspases*
  • Cysteine Endopeptidases / physiology
  • Cytoplasm / physiology
  • DNA Fragmentation
  • Deoxyribonucleases / antagonists & inhibitors
  • Deoxyribonucleases / metabolism
  • Dexamethasone / pharmacology
  • Enzyme Activation / drug effects
  • Enzyme Precursors / metabolism
  • Glucocorticoids / pharmacology
  • Lymphocytes / cytology*
  • Lymphocytes / enzymology
  • Male
  • Nucleosomes / metabolism
  • Potassium / pharmacology
  • Potassium / physiology*
  • Rats
  • Rats, Sprague-Dawley
  • Thymus Gland / cytology

Substances

  • Enzyme Precursors
  • Glucocorticoids
  • Nucleosomes
  • Dexamethasone
  • Deoxyribonucleases
  • Casp3 protein, rat
  • Caspase 3
  • Caspases
  • Cysteine Endopeptidases
  • Potassium