Evolution of Nacre: Biochemistry and Proteomics of the Shell Organic Matrix of the Cephalopod Nautilus macromphalus

ChemBioChem - Tập 10 Số 9 - Trang 1495-1506 - 2009
Benjamin Marie1, Frédéric Marin1, Arul Marie2, Laurent Bédouet3, Lionel Dubost2, Gérard Alcaraz4, Christian Milet3, Gilles Luquet1
1UMR CNRS 5561 Biogéosciences, Université de Bourgogne, 6, Bd. Gabriel, 21000 Dijon (France), Fax: (+33) 3-80-39-63-87
2Centre National de la Recherche Scientifique, Paris, France
3UMR CNRS 5178, Biologie des Organismes Marins et Ecosystèmes, MNHN, 75231 Paris (France)
4UPSP PROXISS, Département Agronomie Environnement, ENESAD, 21000 Dijon (France)

Tóm tắt

AbstractMatrix evolutions: We have biochemically characterized the nacre matrix of the cephalopod Nautilus macromphalus, in part by a proteomic approach applied to the acetic acid‐soluble and ‐insoluble shell matrices, as well as to spots obtained after 2D gel electrophoresis. Strikingly, most of the obtained partial sequences are entirely new, whereas a few correspond only partly with bivalvian nacre proteins. Our findings shed new light on the macroevolution of nacre matrix proteins. magnified imageIn mollusks, one of the most widely studied shell textures is nacre, the lustrous aragonitic layer that constitutes the internal components of the shells of several bivalves, a few gastropods, and one cephalopod: the nautilus. Nacre contains a minor organic fraction, which displays a wide range of functions in relation to the biomineralization process. Here, we have biochemically characterized the nacre matrix of the cephalopod Nautilus macromphalus. The acid‐soluble matrix contains a mixture of polydisperse and discrete proteins and glycoproteins, which interact with the formation of calcite crystals. In addition, a few bind calcium ions. Furthermore, we have used a proteomic approach, which was applied to the acetic acid‐soluble and ‐insoluble shell matrices, as well as to spots obtained after 2D gel electrophoresis. Our data demonstrate that the insoluble and soluble matrices, although different in their bulk monosaccharide and amino acid compositions, contain numerous shared peptides. Strikingly, most of the obtained partial sequences are entirely new. A few only partly match with bivalvian nacre proteins. Our findings have implications for knowledge of the long‐term evolution of molluskan nacre matrices.

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