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J Biol Chem, Vol. 275, Issue 8, 5987-5996, February 25, 2000

Constitutive Death of Platelets Leading to Scavenger Receptor-mediated Phagocytosis
A CASPASE-INDEPENDENT CELL CLEARANCE PROGRAM*

Simon B. BrownDagger §, Murray C. H. ClarkeDagger §, Lorna Magowan||, Heather Sanderson**, and John SavillDagger

From the Dagger  Centre for Inflammation Research, Department of Clinical & Surgical Sciences (Internal Medicine), Royal Infirmary, Edinburgh, EH3 9YW and the Divisions of || Renal & Inflammatory Disease and ** Cardiovascular Medicine, Department of Medicine, University Hospital, Nottingham NG7 2UH, United Kingdom

Apoptosis is a physiological program for the deletion of cells in which caspases govern events leading to safe clearance by phagocytes. However, a growing weight of evidence now suggests that not all forms of programmed cell death are caspase-dependent. We now report a complete and constitutive but caspase-independent program for the specific phagocytic clearance of intact effete platelets, anucleated blood cells of critical importance in health and disease. Platelets aged in vitro not only exhibited increased expression of proapoptotic Bak and Bax but also evidenced constitutive diminution of function such as decreased aggregation to ADP, which was accelerated by culture in the absence of plasma. This abrogation of cell function in plasma-deprived platelets was associated with morphological and biochemical features similar to those of granulocyte apoptosis, that is, cytoplasmic condensation, plasma membrane changes including exposure of phosphatidylserine and the granule protein P-selectin, and recognition by phagocyte scavenger receptors. However, and in contrast with constitutive death of other inflammatory blood cells by apoptosis, these events were not affected by caspase inhibitors, nor was there evidence of caspase-3 activation either by hydrolysis of analog peptide substrates or Western blot analysis, serving to emphasize that neither programmed cell death nor clearance by phagocytes need involve caspases.

* This work was supported in part by Wellcome Trust Program Grant 047273 (to J. S.) and a National Kidney Research Foundation studentship (to M. C. H. C.).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.

§ These authors contributed equally to this work.

To whom correspondence should be addressed: Centre for Inflammation Research, Medical School, University of Edinburgh, Teviot Place, Edinburgh EH8 9AG, UK. Tel.: 44-131-6511577; Fax: 44-131-6511607; E-mail: Simon.Brown@ed.ac.uk.

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