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Blood, 1 November 2001, Vol. 98, No. 9, pp. 2603-2614
REVIEW ARTICLE
Cellular stress response and apoptosis in cancer therapy
Ingrid Herr and
Klaus-Michael Debatin
From the Division of Pediatric Oncology, German Cancer
Research Center, Heidelberg, Germany; and University Children's
Hospital, Ulm, Germany.
Anticancer treatment using cytotoxic drugs is considered to
mediate cell death by activating key elements of the apoptosis program
and the cellular stress response. While proteolytic enzymes (caspases)
serve as main effectors of apoptosis, the mechanisms involved in
activation of the caspase system are less clear. Two distinct pathways
upstream of the caspase cascade have been identified. Death receptors,
eg, CD95 (APO-1/Fas), trigger caspase-8, and mitochondria release
apoptogenic factors (cytochrome c, Apaf-1, AIF), leading to the
activation of caspase-9. The stressed endoplasmic reticulum
(ER) contributes to apoptosis by the unfolded protein response pathway,
which induces ER chaperones, and by the ER overload response pathway,
which produces cytokines via nuclear factor- B. Multiple other
stress-inducible molecules, such as p53, JNK, AP-1, NF-B,
PKC/MAPK/ERK, and members of the sphingomyelin pathway have a profound
influence on apoptosis. Understanding the complex interaction between
different cellular programs provides insights into sensitivity or
resistance of tumor cells and identifies molecular targets for rational
therapeutic intervention strategies.
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