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J. Biol. Chem., Vol. 280, Issue 40, 33895-33908, October 7, 2005

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Caspartin and Calprismin, Two Proteins of the Shell Calcitic Prisms of the Mediterranean Fan Mussel Pinna nobilis^*

Frédéric Marin1, Reinout Amons||, Nathalie Guichard, Martin Stigter, Arnaud Hecker**, Gilles Luquet, Pierre Layrolle, Gérard Alcaraz, Christophe Riondet, and Peter Westbroek

From the UMR CNRS 5561 "Biogéosciences," Université de Bourgogne, 6 Boulevard Gabriel, Dijon F-21000, France, IsoTis, NV, 10 Prof. Bronkhorstlaan, Gebouw D., Bilthoven 3723 MB, The Netherlands, ^||Sylvius Laboratories, Leiden University, Leiden 2300 RA, The Netherlands, ^**UMR CNRS/Université Paris-Sud 8621, Institut de Génétique Moléculaire, Equipe BMGE, Orsay Cedex F-91405, France, UMR INRA 692 "Biochimie des Interactions Cellulaires," ENESAD, 26 Boulevard du Dr. Petitjean, F-21079 Dijon cedex, France, and Leiden Institute of Chemistry, Gorlaeus Laboratories, Leiden University, 55 Einsteinweg, P.O. Box 9502, Leiden 2300 RA, The Netherlands

We used the combination of preparative electrophoresis and immunological detection to isolate two new proteins from the shell calcitic prisms of Pinna nobilis, the Mediterranean fan mussel. The amino acid composition of these proteins was determined. Both proteins are soluble, intracrystalline, and acidic. The 38-kDa protein is glycosylated; the 17-kDa one is not. Ala, Asx, Thr, and Pro represent the dominant residues of the 38-kDa protein, named calprismin. An N-terminal sequence was obtained from calprismin. This sequence, which comprises a pattern of 4 cysteine residues, is not related to any known protein. The second protein, named caspartin, exhibits an unusual amino acid composition, since Asx constitutes by far the main amino acid residue. Preliminary sequencing surprisingly suggests that the first 75 N-terminal residues are all Asp. Caspartin self-aggregates spontaneously into multimers. In vitro tests show that it inhibits the precipitation of calcium carbonate. Furthermore, it strongly interferes with the growth of calcite crystals. A polyclonal antiserum raised against caspartin was used to localize this protein in the shell by immunogold. The immunolocalization demonstrates that caspartin is distributed within the prisms and makes a continuous film at the interface between the prisms and the surrounding insoluble sheets. Our finding emphasizes the prominent role of aspartic acid-rich proteins for the building of calcitic prisms among molluscs.

Received for publication, June 15, 2005 , and in revised form, June 30, 2005.

The N-terminal protein sequence of calprismin reported in this paper has been registered in the Swiss-Prot and TrEMBL knowledgebase under the accession number P83631.

^* This work was supported by the "Fondation Simone et Cino Del Duca" (Paris), for the period November 1999 to January 2001, and by the Dutch biotech Company IsoTis, for the period February 2001 to December 2002. This paper is a contribution to an "Aide Concertée Incitative Jeunes Chercheurs" (ACI JC 3049) awarded to F. Marin by the French "Ministère Délégué à la Recherche et aux Nouvelles Technologies." In 2004, the "Conseil Régional de Bourgogne" (Dijon, France) provided financial support for the installation of a biomineralization laboratory in Biogeosciences research unit. 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: UMR CNRS 5561 "BIOGEOSCIENCES," Université de Bourgogne, 6 Bd. Gabriel, 21000 DIJON, France. Tel.: 33-3-80-39-63-72; Fax: 33-3-80-39-63-87; E-mail: frederic.marin{at}u-bourgogne.fr.

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