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J Biol Chem, Vol. 275, Issue 13, 9244-9250, March 31, 2000

Caspase-8-mediated Intracellular Acidification Precedes Mitochondrial Dysfunction in Somatostatin-induced Apoptosis*

Danni LiuDagger , Giovanni MartinoDagger , Muthusamy ThangarajuDagger , Monika SharmaDagger , Fawaz Halwani§, Shi-Hsiang Shen, Yogesh C. PatelDagger , and Coimbatore B. SrikantDagger ||

From the Dagger  Fraser Laboratories, Department of Medicine, and the § Department of Pathology, McGill University and Royal Victoria Hospital, Montreal, Quebec H3A 1A1 and the  Pharmaceutical Sector, N.R.C. Biotechnology Research Institute, Montreal, Quebec H4P 2R2, Canada

Activation of initiator and effector caspases, mitochondrial changes involving a reduction in its membrane potential and release of cytochrome c (cyt c) into the cytosol, are characteristic features of apoptosis. These changes are associated with cell acidification in some models of apoptosis. The hierarchical relationship between these events has, however, not been deciphered. We have shown that somatostatin (SST), acting via the Src homology 2 bearing tyrosine phosphatase SHP-1, exerts cytotoxic action in MCF-7 cells, and triggers cell acidification and apoptosis. We investigated the temporal sequence of apoptotic events linking caspase activation, acidification, and mitochondrial dysfunction in this system and report here that (i) SHP-1-mediated caspase-8 activation is required for SST-induced decrease in pHi. (ii) Effector caspases are induced only when there is concomitant acidification. (iii) Decrease in pHi is necessary to induce reduction in mitochondrial membrane potential, cyt c release and caspase-9 activation and (iv) depletion of ATP ablates SST-induced cyt c release and caspase-9 activation, but not its ability to induce effector caspases and apoptosis. These data reveal that SHP-1-/caspase-8-mediated acidification occurs at a site other than the mitochondrion and that SST-induced apoptosis is not dependent on disruption of mitochondrial function and caspase-9 activation.

* This work was supported by Canadian Medical Research Council Grant MT-12603 and the U. S. Department of Defense Breast Cancer Program.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed: M3.15, Royal Victoria Hospital, 687 Pine Ave. W., Montreal, Quebec H3A 1A1, Canada. Tel.: 514-842-1231 (ext. 5359); Fax: 514-849-3681; E-mail: mdcs@musica.mcgill.ca.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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