Soluble proteins of the nacre of the giant oyster Pinctada maxima and of the abalone Haliotis tuberculata:

Bédouet, Laurent; Schuller, Maria José; Marin, Frédéric; Milet, Christian; Lopez, Évelyne; Giraud, Michel

doi:10.1016/s1096-4959(00)00337-7

Cited by 60 publications

(52 citation statements)

References 33 publications

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“…Firstly, soluble proteins of the shell matrix can become insoluble correlatively to their ability to form homopolymers of increasing size. Self-polymerization of a single shell protein has indeed been observed for P20 [48] and for caspartin. [49] Secondly, soluble proteins can be components of complex insoluble heteropolymers, which result from crosslinking between matrix macromolecules.…”

Section: Discussionmentioning

confidence: 79%

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

Marie¹,

Marin²,

Marie³

et al. 2009

ChemBioChem

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Matrix 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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Section: Discussionmentioning

confidence: 79%

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

Marie¹,

Marin²,

Marie³

et al. 2009

ChemBioChem

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“…This group also includes the recently found prismalin (17), aspein (18), asprich (19), and a histidine-rich protein of the extrapallial fluid (84). Furthermore, the shell protein group includes a few partly sequenced proteins (85)(86)(87)(88)(89)(90).…”

Section: Discussionmentioning

confidence: 99%

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

Marin

Amons

Guichard

et al. 2005

Journal of Biological Chemistry

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133

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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.The secretion of a shell by molluscs is a striking example of a selfassembling process performed outside living tissues. When a mollusc builds its shell, the calcifying epithelium of its mantle extrudes mineral ions, mainly calcium and bicarbonate. In addition, it secretes an extracellular matrix composed of proteins, glycoproteins, proteoglycans, and polysaccharides (1). This mixture is released into the extrapallial space, a microvolume delimited by the epithelium, the growing shell, and the leathery periostracum (2). In this supersaturated space, the released macromolecules interact with bicarbonate and calcium to form biocrystallites that self-aggregate in an orderly manner. The end product is a densely packed organomineral assembly, the shell, in which the mineral phase represents more than 95% by weight (3). As shell proteins exert a control on the biomineralization process, they can be used in the synthesis of biomimetic materials (4 -6). However, the resolution of the primary structure of molluscan shell proteins has been seriously impaired for decades by their polydispersity, their polyanionic properties, and finally their post-translational modifications (3, 7).Despite these obstacles, investigations on molluscan shell proteins have made significant advances in the last 6 years, with the characterization of 16 proteins and, for most of them, the identification of the corresponding transcript (8, 9). Among the different shell textures that molluscs use to produce their shell, mother-of-pearl has received the greatest deal of attention. Its intrinsic bea...

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“…Finally, the membranes were rinsed three times (10min each) in 50mmoll -1 Tris-HCl (pH 7.5; 0.5 moll -1 NaCl, 0.1% Triton X-100 [v/v]), followed by an incubation with alkaline-phosphatase-conjugated avidin at a dilution of 5ϫ10 -3 for 1h at 24°C. The lectin-biotin complexes were visualized with the phosphatase substrate BCIP/NBT (Bédouet et al, 2001). …”

Section: Wheat Germ Agglutinin Labelingmentioning

confidence: 99%

Biosilicification of loricate choanoflagellate: organic composition of the nanotubular siliceous costal strips of Stephanoeca diplocostata

Gong

Wiens

Schröder

et al. 2010

Journal of Experimental Biology

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SUMMARYLoricate choanoflagellates (unicellular, eukaryotic flagellates; phylum Choanozoa) synthesize a basket-like siliceous lorica reinforced by costal strips (diameter of approximately 100nm and length of 3m). In the present study, the composition of these siliceous costal strips is described, using Stephanoeca diplocostata as a model. Analyses by energy-dispersive X-ray spectroscopy (EDX), coupled with transmission electron microscopy (TEM), indicate that the costal strips comprise inorganic and organic components. The organic, proteinaceous scaffold contained one major polypeptide of mass 14kDa that reacted with wheat germ agglutinin. Polyclonal antibodies were raised that allowed mapping of the proteinaceous scaffold, the (glyco)proteins, within the costal strips. Subsequent in vitro studies revealed that the organic scaffold of the costal strips stimulates polycondensation of ortho-silicic acid in a concentration-and pH-dependent way. Taken together, the data gathered indicate that the siliceous costal strips are formed around a proteinaceous scaffold that supports and maintains biosilicification. A scheme is given that outlines that the organic template guides both the axial and the lateral growth of the strips.

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Soluble proteins of the nacre of the giant oyster Pinctada maxima and of the abalone Haliotis tuberculata:

Cited by 60 publications

References 33 publications

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

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

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

Biosilicification of loricate choanoflagellate: organic composition of the nanotubular siliceous costal strips of Stephanoeca diplocostata

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