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Volume 272, Number 16,
Issue of April 18, 1997
pp. 10474-10482
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Inhibition of Cytosolic Phospholipase A2 by Annexin V
in Differentiated Permeabilized HL-60 Cells
EVIDENCE OF CRUCIAL IMPORTANCE OF DOMAIN I TYPE II
Ca2+-BINDING SITE IN THE MECHANISM OF
INHIBITION
(Received for publication, September 26, 1996, and in revised form, January 20, 1997)
Jean-Paul
Mira
§
,
Thierry
Dubois
,
Jean-Paul
Oudinet
,
Sandra
Lukowski
,
Françoise
Russo-Marie
and
Blandine
Geny
From Unité 332, Institut Cochin de
Génétique Moleculaire, INSERM, 22 rue Mechain, 75014 Paris,
France and the § Medical Intensive Care Unit, Cochin
University Hospital, 75014 Paris, France
Annexin V belongs to a family of proteins that
interact with phospholipids in a
Ca2+-dependent manner. This protein has
been demonstrated to have anti-phospholipase A2 activity.
However, this effect has never yet been reported with the 85-kDa
cytosolic PLA2 (cPLA2). We studied, in a model
of differentiated and streptolysin O-permeabilized HL-60 cells, the
effect of annexin V on cPLA2 activity after stimulation by
calcium, GTP S (guanosine 5 -O-(3-thiotriphosphate)),
formyl-Met-Leu-Phe, or phorbol 12-myristate 13-acetate. Both
recombinant and human placental purified annexin V inhibit
cPLA2 activity whatever the stimulus used. The decrease of
arachidonic acid release is of 40 and 50%, respectively, at
[Ca2+] of 3 and 10 µM. The mechanism of
inhibition was also analyzed. cPLA2 requires calcium and
protein kinase C (PKC) or mitogen-activated protein kinase
phosphorylation for its activation. As annexin V was shown to be an
endogenous inhibitor of PKC, PKC-stimulated cPLA2 activity
was analyzed. Using GF109203x, a specific PKC inhibitor, we
demonstrated that this pathway is of minor importance in our model.
cPLA2 inhibition by annexin V is not linked to PKC
inhibition. To test the hypothesis of phospholipid depletion, mutants
of annexin V were constructed using mutagenesis directed to
Ca2+ site. We demonstrate that the Ca2+ site
located in domain I is necessary for the inhibitory effect of annexin V
on cPLA2 activity. The site in domain IV is also involved
but with less efficiency. In contrast, mutations in site II and III do
not modify this effect. Moreover, annexin V mutated on all sites does
not inhibit cPLA2. Thus, we propose a predominant role of
module (I/IV) in the biological action of annexin V, which, in
physiological conditions, may control cPLA2 activity by
depletion of the phospholipid substrate.

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Copyright © 1997 by the American Society for Biochemistry and Molecular Biology.
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