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J Biol Chem, Vol. 274, Issue 6, 3678-3685, February 5, 1999
,,
From the Exposure of mammalian cells to UV light causes
initial changes in the cell membrane, induces phosphorylation and
clustering of growth factor/cytokine receptors, and activates the Jun
N-terminal kinase/stress-activated protein kinase (JNK/SAPK) signaling
pathway leading to programmed cell death (apoptosis). In this study, we found that an early event in the cell membrane of myeloblastic leukemia
(ML-1) cells was the vigorous activation of the voltage-gated K+ channel by UV irradiation. The strong enhancement
by UV irradiation of K+ channel activity in the cell
membrane subsequently activated the JNK/SAPK signaling pathway and
resulted in myeloblastic leukemia cell apoptosis. Suppression of
UV-induced K+ channel activation with specific channel
blockers prevented UV-induced apoptosis through inhibition of
UV-induced activation of the proteins SEK (SPAK kinase) and JNK.
However, suppression of K+ channel activity could not
protect cells from etoposide-induced apoptosis, which bypasses the
membrane event. Elimination of extracellular Ca2+ had no
effect on the UV-induced and K+ channel-mediated JNK/SAPK
activation. Thus, we have identified a novel mechanism in which
activation of K+ channels by UV-irradiation upstream of SEK
and SAPK/JNK mediates UV-induced myeloblastic cell apoptosis.
Department of Physiology and Biophysics,
School of Medicine, Wright State University, Dayton, Ohio 45435 and
¶ Division of Hematology, Department of Medicine, University of
Cincinnati College of Medicine, Cincinnati, Ohio 45243
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