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J. Biol. Chem., Vol. 282, Issue 25, 18357-18364, June 22, 2007

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Regulated Externalization of Phosphatidylserine at the Cell Surface

IMPLICATIONS FOR APOPTOSIS^*

From the Department of Cancer Biology, The University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030

The regulated loss of plasma membrane phosphatidylserine (PS) asymmetry is critical to many biological processes. In particular, the appearance of PS at the cell surface, a hallmark of apoptosis, prepares the dying cell for engulfment and elimination by phagocytes. While it is well established that PS externalization is regulated by activation of a calcium-dependent phospholipid scramblase activity in concert with inactivation of the aminophospholipid translocase, there is no evidence indicating that these processes are triggered and regulated by apoptotic regulatory mechanisms. Using a novel model system, we show that PS externalization is inducible, reversible, and independent of cytochrome c release, caspase activation, and DNA fragmentation. Additional evidence is presented indicating that the outward movement of plasma membrane PS requires sustained elevation in cytosolic Ca²⁺ in concert with inactivation of the aminophospholipid translocase and is inhibited by calcium channel blockers.

Received for publication, January 8, 2007 , and in revised form, April 27, 2007.

^* This work was supported by National Institutes of Health Grant GM70964 (to A. J. S.) and the John Q. Gaines Foundation (to A. J. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement"in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Dept. of Cancer Biology, The University of Texas M. D. Anderson Cancer Center, 1515 Holcombe Blvd., Houston, TX 77030. Tel.: 713-792-8586; Fax: 713-792-8747; E-mail: aschroit{at}mdanderson.org.

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