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Different secretory repertoires control the biomineralization processes of prism and nacre deposition of the pearl oyster shell

Marie, Benjamin, Joubert, Caroline, Tayalé, Alexandre, Zanella-Cléon, Isabelle, Belliard, Corinne, Piquemal, David, Cochennec-Laureau, Nathalie, Marin, Frédéric, Gueguen, Yannick, Montagnani, Caroline
Proceedings of the National Academy of Sciences of the United States of America 2012 v.109 no.51 pp. 20986-20991
Pinctada margaritifera, Pinctada maxima, biomineralization, oysters, prisms, proteins, shell (molluscs)
Mollusca evolutionary success can be attributed partly to their efficiency to sustain and protect their soft body with an external biomineralized structure, the shell. Current knowledge of the protein set responsible for the formation of the shell microstructural polymorphism and unique properties remains largely patchy. In Pinctada margaritifera and Pinctada maxima , we identified 80 shell matrix proteins, among which 66 are entirely unique. This is the only description of the whole “biomineralization toolkit” of the matrices that, at least in part, is thought to regulate the formation of the prismatic and nacreous shell layers in the pearl oysters. We unambiguously demonstrate that prisms and nacre are assembled from very different protein repertoires. This suggests that these layers do not derive from each other.