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J. Biol. Chem., Vol. 275, Issue 43, 33574-33584, October 27, 2000
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From the Rayne Laboratory, University of Edinburgh Medical
School, Teviot Place, Edinburgh EH8 9AG, United Kingdom
Apoptosis is essential for the resolution of
neutrophilic inflammation. To define the mechanisms triggering the
execution phase of apoptosis we developed and utilized a model in which culture of human neutrophils at 15 °C for 20 h arrested apoptosis and subsequent warming to 37 °C triggered a synchronous burst of
apoptosis. Treatment of 15 °C cultured neutrophils with the pan-caspase inhibitor zVAD-fmk just before warming to 37 °C
inhibited the morphological changes associated with apoptosis, but did
not prevent the insertion of the proapoptotic protein Bax into
mitochondria nor the inhibition of secretion and the externalization of
phosphatidylserine, indices of neutrophil apoptosis. In both intact
neutrophils and a cell-free extract, cytochrome c released
from mitochondria induced proteolytic cleavage of procaspase-3. At
15 °C the binding of Bax to mitochondria was uncoupled from Bax
insertion into the mitochondrial membrane required for the release of
cytochrome c. Apoptosis was also inhibited by low pH during
warming to 37 °C, suggesting that changes to the conformation of
Bax, necessary for membrane insertion, were being inhibited. Bax
insertion was only sensitive to zVAD-fmk when added at the start of the
15 °C culture period, suggesting that a cytoplasmic substrate of the effector caspases may mediate in the mechanism of Bax insertion into mitochondria.
Temperature-dependent Arrest of Neutrophil
Apoptosis
FAILURE OF Bax INSERTION INTO MITOCHONDRIA AT 15 °C
PREVENTS THE RELEASE OF CYTOCHROME c*
,
*
This work is supported by Program Grant G9016491 from the
Medical Research Council, United Kingdom.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: Respiratory Medicine
Unit, Dept. of Medicine (RIE), Rayne Laboratory, University of
Edinburgh Medical School, Teviot Place, Edinburgh, EH8 9AG. Scotland,
UK. Tel.: 44-131-650-6949; Fax: 44-131-650-4384; E-mail: j.pryde@ed.ac.uk.
§
Supported by University of Edinburgh Faculty of Medicine, Vans
Dunlop, and Shaw McFie Lang Postgraduate Research Scholarships.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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