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J. Biol. Chem., Vol. 276, Issue 7, 5134-5139, February 16, 2001
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From the The phosphatidylserine transmembrane
redistribution at the cell surface is one of the early characteristics
of cells undergoing apoptosis and also occurs in cells fulfilling a
more specialized function, such as the
phosphatidylserine-dependent procoagulant response of platelets
after appropriate activation. Although an increase in cytoplasmic
Ca2+ is essential to trigger the remodeling of the
plasma membrane, little is known about intracellular signals leading to
phosphatidylserine externalization. Here, the role of store-operated
Ca2+ entry on phosphatidylserine exposure was investigated
in human erythroleukemia HEL cells, a pluripotent lineage with
megakaryoblastic properties. Ca2+ entry inhibitors
(SKF-96365, LaCl3, and miconazole) inhibited store-operated
Ca2+ entry in A23187- or thapsigargin-stimulated
cells and reduced the degree of phosphatidylserine externalization
concomitantly, providing evidence for a close link between the two
processes. In cells pretreated with cytochalasin D, an agent that
disrupts the microfilament network of the cytoskeleton, store-operated Ca2+ entry and phosphatidylserine externalization at the
cell surface were inhibited. In a context where most of the key actors
remain to be identified, these results provide evidence for the
implication of both store-operated Ca2+ entry and
cytoskeleton architectural organization in the regulation of
phosphatidylserine transbilayer migration.
Regulation of Phosphatidylserine Transbilayer Redistribution by
Store-operated Ca2+ Entry
ROLE OF ACTIN CYTOSKELETON*
§¶,§, and§
**
Institut d'Hématologie et
d'Immunologie, Université Louis Pasteur, Faculté de
Médecine, 4 rue Kirschleger, Strasbourg 67085, France and the
§ Unité 143 INSERM, Hôpital de Bicêtre, Le
Kremlin-Bicêtre 94275, France
*
This work was supported in part by grants from the Institut
National de la Santé et de la Recherche Médicale and the
Université Louis Pasteur.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.
Supported by a fellowship from the Fondation pour la Recherche
Médicale, France.
**
To whom correspondence should be addressed: Institut
d'Hématologie et d'Immunologie, Faculté de
Médecine, 4 rue Kirschleger, 67085 Strasbourg, France. Tel.:
33-3-88-24-33-39; Fax: 33-3-88-25-58-83; E-mail:
secr600@pharma.u-strasbg.fr.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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