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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.

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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, GTPS (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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