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J Biol Chem, Vol. 275, Issue 11, 7492-7496, March 17, 2000

Novel Human Secreted Phospholipase A₂ with Homology to the Group III Bee Venom Enzyme^*

Emmanuel Valentin^§, Farideh Ghomashchi^¶, Michael H. Gelb^¶, Michel Lazdunski, and Gérard Lambeau

From the  Institut de Pharmacologie Moléculaire et Cellulaire, CNRS-UPR 411, 660 route des Lucioles, Sophia Antipolis, 06560 Valbonne, France and the ^¶ Departments of Chemistry and Biochemistry, University of Washington, Seattle, Washington 98195

Venom and mammalian secreted phospholipases A₂ (sPLA₂s) have been associated with numerous physiological, pathological, and toxic processes. So far, structurally related group I and II sPLA₂s have been found in vertebrates such as mammals and snakes, whereas group III sPLA₂s have mainly been found in venom from invertebrates such as bees and scorpions. Here we report the cloning and expression of a cDNA coding for a human group III (hGIII) sPLA₂. The full-length cDNA codes for a signal peptide of 19 residues followed by a protein of 490 amino acids made up of a central sPLA₂ domain (141 residues) flanked by large N- and C-terminal regions (130 and 219 residues, respectively). The sPLA₂ domain is 31% identical to bee venom sPLA₂ and displays all of the features of group III sPLA₂s including 10 cysteines. The hGIII sPLA₂ gene consists of at least 7 exons and maps to chromosome 22q. By Northern blot analysis, a 4.4-kilobase hGIII transcript was found in kidney, heart, liver, and skeletal muscle. Transfection of hGIII sPLA₂ cDNA in COS cells led to accumulation of sPLA₂ activity in the culture medium, indicating that the cDNA codes for a secreted enzyme. Using small unilamellar vesicles as substrate, hGIII sPLA₂ was found to be a Ca²⁺-dependent enzyme showing an 11-fold preference for phosphatidylglycerol over phosphatidylcholine and optimal activity at pH 8.

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^* This work was supported in part by CNRS, the Association pour la Recherche sur le Cancer (ARC), Ministère de la Défense Nationale Grant DGA-DRET 96/096, and National Institutes of Health Grant HL36235 (to M. H. G.).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.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EMBL Data Bank with accession number(s) AF220490

^§ Recipient of a grant from the region Provence Alpes Côte d'azur-CNRS program.

To whom correspondence should be addressed. Tel.: 33-4-93-95-77-02 or -03; Fax: 33-4-93-95-77-04; E-mail: ipmc@ipmc.cnrs.fr.

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

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