The shell matrix of the freshwater mussel Unio pictorum (Paleoheterodonta, Unionoida)

FEBS Journal - Tập 274 Số 11 - Trang 2933-2945 - 2007
Benjamin Marie1, Gilles Luquet1, Jean-Paul Paı̈s de Barros2, Nathalie Guichard1, Sylvain Morel3, Gérard Alcaraz3, Loı̈c Bollache1, Frédéric Marin1
1UMR CNRS 5561 Biogéosciences, Université de Bourgogne, Dijon, France
2 U 498 INSERM, Métabolisme des lipoprotéines humaines et interactions vasculaires, Université de Bourgogne, Dijon, France
3UMR INRA 692, Biochimie des interactions cellulaires, ENESAD, Dijon, France

Tóm tắt

Among molluscs, the shell biomineralization process is controlled by a set of extracellular macromolecular components secreted by the calcifying mantle. In spite of several studies, these components are mainly known in bivalves from only few members of pteriomorph groups. In the present case, we investigated the biochemical properties of the aragonitic shell of the freshwater bivalve Unio pictorum (Paleoheterodonta, Unionoida). Analysis of the amino acid composition reveals a high amount of glycine, aspartate and alanine in the acid‐soluble extract, whereas the acid‐insoluble one is rich in alanine and glycine. Monosaccharidic analysis indicates that the insoluble matrix comprises a high amount of glucosamine. Furthermore, a high ratio of the carbohydrates of the soluble matrix is sulfated. Electrophoretic analysis of the acid‐soluble matrix revealed discrete bands. Stains‐All, Alcian Blue, periodic acid/Schiff and autoradiography with 45Ca after electrophoretic separation revealed three major polyanionic calcium‐binding glycoproteins, which exhibit an apparent molecular mass of 95, 50 and 29 kDa, respectively. Two‐dimensional gel electrophoresis shows that these bands, provisionally named P95, P50 and P29, are composed of numerous isoforms, the majority of which have acidic isoelectric points. Chemical deglycosylation of the matrix with trifluoromethanesulfonic acid induces a drastic shift of both the apparent molecular mass and the isoelectric point of these matrix components. This treatment induces also a modification of the shape of CaCO3 crystals grown in vitro and a loss of the calcium‐binding ability of two of the main matrix proteins (P95 and P50). Our findings strongly suggest that post‐translational modifications display important functions in mollusc shell calcification.

Từ khóa


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FEBS Journal

Tập 274 Số 11

2933-2945

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