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J Biol Chem, Vol. 273, Issue 27, 17147-17153, July 3, 1998
From the Trescowthick Research Laboratories, Peter MacCallum Cancer
Institute, St. Andrews Place, East Melbourne, Victoria, Australia, 3002 and the The resistance to stress-induced apoptosis
conferred by the thermotolerant state or by exogenous expression of
HSP72 was measured in mouse embryo fibroblasts. The induction of
thermotolerance protects cells from heat, tumor necrosis factor
Heat Shock Protein 72 Modulates Pathways of Stress-induced
Apoptosis
, Department of Radiation Oncology, Stanford
University, Stanford, California 94305
(TNF), and ceramide-induced apoptosis but not from ionizing
radiation. Because the development of thermotolerance is associated
with increased levels of heat shock proteins, we determined whether
constitutive expression of one of the major inducible heat shock
proteins, HSP72, could also protect cells from stress-induced
apoptosis. Cells expressing constitutive HSP72 were shown to have
significantly reduced levels of apoptosis after heat, TNF, and
ceramide but not after ionizing radiation. Activation of
stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) was
found to be strongly inhibited in thermotolerant cells after heat shock
but not after other stresses. Cells that constitutively express HSP72
did not demonstrate decreased SAPK/JNK activation after any of these
stresses. Thus, factors other than HSP72 that are induced in the
thermotolerant state are able to reduce activation of SAPK/JNK after
heat stress. Notably, the level of activation of SAPK/JNK did not
correlate with the amount of apoptosis detected after different
stresses. Constitutive HSP72 expression inhibited poly(ADP-ribose)
polymerase cleavage in cells after heat shock and TNF but not after
ceramide or ionizing radiation. The results suggest either that
SAPK/JNK activation is not required for apoptosis in mouse embryo
fibroblasts or that HSP72 acts downstream of SAPK/JNK. Furthermore, the
data support the concept that caspase activity, which can be
down-regulated by HSP72, is a crucial step in stress-induced apoptosis.
Based on data presented here and elsewhere, we propose that the heat shock protein family can be classified as a class of anti-apoptotic genes, in addition to the Bcl-2 and inhibitor of apoptosis protein families of genes.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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