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Phosphatidylserine externalization is a downstream event of interleukin- 1
beta-converting enzyme family protease activation during apoptosis
M Naito, K Nagashima, T Mashima and T Tsuruo
Institute of Molecular and Cellular Biosciences, University of Tokyo,
Japan.
Phosphatidylserine (PS), a class of acidic phospholipids, normally
localizes on the internal surface of cellular plasma membranes. The
internal PS is externalized when cells undergo apoptosis; however, the
mechanism for this is largely unknown. To study the mechanism of PS
externalization during development of apoptosis, we examined the
correlation between the activation of interleukin-1 beta-converting enzyme
(ICE) family protease and PS externalization in human monocytic leukemia
U937 cells and in their apoptosis-resistant variants, UK711 and UK110,
after treatment with etoposide and anti-Fas antibody. We found that PS
externalization accompanied the development of apoptosis and the activation
of ICE family proteases in these cell lines. Furthermore, inhibitors of ICE
family proteases, Z-Asp and Z-VAD, prevented apoptosis and PS
externalization in etoposide-treated U937 cells. These results indicate
that PS externalization is a downstream event of ICE family protease
activation during apoptosis development. Because ICE family proteases play
a crucial role in apoptosis, PS externalization could be a rational and
useful marker for the development of apoptosis.
Volume 89,
Issue 6,
pp. 2060-2066,
03/15/1997
Copyright © 1997 by The American Society of Hematology
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