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J Proteomics. 2017 Jan 6;150:63-73. doi: 10.1016/j.jprot.2016.08.015. Epub 2016 Aug 26.

First proteomic analyses of the dorsal and ventral parts of the Sepia officinalis cuttlebone.

Author information

1
Unité Biologie des ORganismes et Ecosystèmes Aquatiques (BOREA, UMR 7208), Sorbonne Universités, Muséum National d'Histoire Naturelle, CNRS, Université Pierre et Marie Curie, Université de Caen Normandie, IRD 207, Université des Antilles, CP 26, 43 rue Cuvier, 75005 Paris, France. Electronic address: clepabic@mnhn.fr.
2
UMR 7245 MNHN/CNRS Molécules de Communication et Adaptation des Micro-organismes, Sorbonne Universités, Muséum National d'Histoire Naturelle, CP 54, 43 rue Cuvier, 75005 Paris, France.
3
UMR MONARIS, Sorbonne Universités, de la Molécule aux Nano-objets: Réactivité, Interactions et Spectroscopies, UMR 8233 CNRS-Université Pierre et Marie Curie, 75005 Paris, France.
4
Unité Biologie des ORganismes et Ecosystèmes Aquatiques (BOREA, UMR 7208), Sorbonne Universités, Muséum National d'Histoire Naturelle, CNRS, Université Pierre et Marie Curie, Université de Caen Normandie, IRD 207, Université des Antilles, CP 26, 43 rue Cuvier, 75005 Paris, France.
5
Unité Biologie des ORganismes et Ecosystèmes Aquatiques (BOREA, UMR 7208), Sorbonne Universités, Muséum National d'Histoire Naturelle, CNRS, Université Pierre et Marie Curie, Université de Caen Normandie, IRD 207, Université des Antilles, CP 26, 43 rue Cuvier, 75005 Paris, France. Electronic address: gluquet@mnhn.fr.

Abstract

Protein compounds constituting mollusk shells are known for their major roles in the biomineralization processes. These last years, a great diversity of shell proteins have been described in bivalves and gastropods allowing a better understanding of the calcification control by organic compounds and given promising applications in biotechnology. Here, we analyzed for the first time the organic matrix of the aragonitic Sepia officinalis shell, with an emphasis on protein composition of two different structures: the dorsal shield and the chambered part. Our results highlight an organic matrix mainly composed of polysaccharide, glycoprotein and protein compounds as previously described in other mollusk shells, with quantitative and qualitative differences between the dorsal shield and the chamber part. Proteomic analysis resulted in identification of only a few protein compounds underlining the lack of reference databases for Sepiidae. However, most of them contain domains previously characterized in matrix proteins of aragonitic shell-builder mollusks, suggesting ancient and conserved mechanisms of the aragonite biomineralization processes within mollusks.

BIOLOGICAL SIGNIFICANCE:

The cuttlefish's inner shell, better known under the name "cuttlebone", is a complex mineral structure unique in mollusks and involved in tissue support and buoyancy regulation. Although it combines useful properties as high compressive strength, high porosity and high permeability, knowledge about organic compounds involved in its building remains limited. Moreover, several cuttlebone organic matrix studies reported data very different from each other or from other mollusk shells. Thus, this study provides 1) an overview of the organization of the main mineral structures found in the S. officinalis shell, 2) a reliable baseline about its organic composition, and 3) a first descriptive proteomic approach of organic matrices found in the two main parts of this shell. These data will contribute to the general knowledge about mollusk biomineralization as well as in the identification of protein compounds involved in the Sepiidae shell calcification.

KEYWORDS:

Aragonite; Biomineralization; Cuttlefish; Organic matrix; Proteomics; Sepia officinalis; Shell

PMID:
27576138
DOI:
10.1016/j.jprot.2016.08.015
[Indexed for MEDLINE]

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