Soluble Organic Matrices of the Calcitic Prismatic Shell Layers of Two Pteriomorphid Bivalves

Dauphin, Yannicke

doi:10.1074/jbc.m204375200

Cited by 130 publications

(124 citation statements)

References 27 publications

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“…The positive signal was the most intense in the organic sheet, perpendicular to the axis of the prisms (Fig. 8D, arrows), as well as in the organic sheaths around the prisms, in which the main constituent is chitin (54,55) (Fig. 8D, white arrowheads).…”

Section: Characterization Of Deduced Amino Acid Sequence Ofmentioning

confidence: 99%

Cloning and Characterization of Prisilkin-39, a Novel Matrix Protein Serving a Dual Role in the Prismatic Layer Formation from the Oyster Pinctada fucata

Kong

Yan

et al. 2009

Journal of Biological Chemistry

101

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Molluscs form their shells out of CaCO 3 and a matrix of biomacromolecules. Understanding the role of matrices may shed some light on the mechanism of biomineralization. Here, a 1401-bp full-length cDNA sequence encoding a novel matrix protein was cloned from the mantle of the bivalve oyster, Pinctada fucata. The deduced protein (Prisilkin-39), which has a molecular mass of 39.3 kDa and an isoelectric point of 8.83, was fully characterized, and its role in biomineralization was demonstrated using both in vivo and in vitro crystal growth assays. Prisilkin-39 is a highly repetitive protein with an unusual composition of Gly, Tyr, and Ser residues. Expression of Prisilkin-39 was localized to columnar epithelial cells of the mantle edge, corresponding to the calcitic prismatic layer formation. Immunostaining in situ and immunodetection in vitro revealed the presence of a characteristic pattern of Prisilkin-39 in the organic sheet and in sheaths around the prisms. Prisilkin-39 binds tightly with chitin, an insoluble polysaccharide that forms the highly structured framework of the shell. Antibody injection in vivo resulted in dramatic morphological deformities in the inner shell surface structure, where large amounts of CaCO 3 were deposited in an uncontrolled manner. Moreover, Prisilkin-39 strictly prohibited the precipitation of aragonite in vitro. Taken together, Prisilkin-39 is the first protein shown to have dual function, involved both in the chitinous framework building and in crystal growth regulation during the prismatic layer mineralization. These observations may extend our view on the rare group of basic matrices and their functions during elaboration of the molluscan shell.

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Section: Characterization Of Deduced Amino Acid Sequence Ofmentioning

confidence: 99%

Cloning and Characterization of Prisilkin-39, a Novel Matrix Protein Serving a Dual Role in the Prismatic Layer Formation from the Oyster Pinctada fucata

Kong

Yan

et al. 2009

Journal of Biological Chemistry

101

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“…This matrix is thought to be responsible for the choice of the calcite polymorph and for the guidance and correct positioning of the single crystallites, so that the monocrystal-like units emerge (27). But this matrix has been poorly characterized (26,28), and recent data acquired on the bulk matrix (29,30) do not give any information on the molecular mechanisms by which prisms are built. The work described herein aims to elucidate the structure of this acidic macromolecular assemblage.…”

mentioning

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

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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“…Currently, there is a great deal of work relating with the purification and characterization of proteins from mollusk shell [32][33][34][35][36][37][38]. However, less concern is paid attention to the inter-prismatic proteins (insoluble in water) as a whole from a structural perspective.…”

Section: Yang Et Almentioning

confidence: 99%

Inter-prismatic matrix structure characterizationof mollusk shell and its effect on crystal formation

Yang¹,

Huang²,

Pan³

et al. 2010

Nano BioMed ENG

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Mollusk biomineralization is an elaborate process in which cells, organic macromolecules, and calcium carbonate crystals are actively involved.Macromolecules (mainly are proteins and polysaccharide) act as a key role in regulating and limiting the size, orientation, polymorph and texture of inorganic phase. In this work, we focused on the inter-prismatic matrix of mollusk shell combining scanning electron microscopy (SEM), X-ray diffraction (XRD) and transmission electron microscopy (TEM) analytical techniques with CaCO 3 recrystallization experiment to characterize its structure and effects on crystal formation. Our results show that the inter-prismatic matrix is not a sort of pure polymer, calcite nano-crystals are also located inside the inter-prismatic matrix. Interestingly, it seems that these nanocrystals have a preferred orientation, which means the inter-prismatic matrix do impose effect on the crystal formation. In vitro re-crystallization experiment using partially dissolved prismatic fragment as template indicates that the (104) faces of CaCO 3 micro-crystals are closely associated with the walls of inter-prismatic matrix. Furthermore, a possible growth mechanism of mollusk shell prismatic layer was proposed.Key Words: Biomineralization, Mollusk shell, Inter-prismatic matrix, Calcite, Dissolution Citation: D. Yang, et al. Inter-prismatic matrix structure characterization of mollusk shell and its effect on crystal formation. Nano Biomed. Eng.

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Soluble Organic Matrices of the Calcitic Prismatic Shell Layers of Two Pteriomorphid Bivalves

Cited by 130 publications

References 27 publications

Cloning and Characterization of Prisilkin-39, a Novel Matrix Protein Serving a Dual Role in the Prismatic Layer Formation from the Oyster Pinctada fucata

Cloning and Characterization of Prisilkin-39, a Novel Matrix Protein Serving a Dual Role in the Prismatic Layer Formation from the Oyster Pinctada fucata

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

Inter-prismatic matrix structure characterizationof mollusk shell and its effect on crystal formation

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