Structure of the Nacreous Organic Matrix of a Bivalve Mollusk Shell Examined in the Hydrated State Using Cryo-TEM

Levi‐Kalisman, Yael; Falini, Giuseppe; Addadi, Lia; Weiner, Steve

doi:10.1006/jsbi.2001.4372

Cited by 489 publications

(428 citation statements)

References 34 publications

Supporting

Mentioning

408

Contrasting

Unclassified

Order By: Relevance

“…[50,51] It may occur as well in the formation of nacre tissues, in particular for hardening of the chitinoprotein framework. [17] Thirdly, from recent reviews on shell proteins, [12,13] the primary structures of several shell matrix proteins exhibit organization in modules. Some of our recent data suggest that these modules may serve as "functional blocks" in different proteins, soluble or not.…”

Section: Discussionmentioning

confidence: 99%

“…[1] Particular emphasis has been placed on the prominent role played by chitin in spatially structuring the organic framework, [1,14] the distribution of key biochemical functions at the surfaces of nacre tablets, [15] the existence of a transient precursor amorphous phase, [16] and the growth of nacre tablets in a hydrophobic gel, which hardens and becomes insoluble when nacre tablets coalesce. [17] Nacre also constitutes a fascinating model of study from an evolutionary viewpoint. Firstly, nacre appears early in the fossil record, [18] somewhere in the Cambrian period, and since then has been remarkably stable throughout the Phanerozoic eon.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

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

Marie¹,

Marin²,

Marie³

et al. 2009

ChemBioChem

View full text Add to dashboard Cite

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.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

Marie¹,

Marin²,

Marie³

et al. 2009

ChemBioChem

View full text Add to dashboard Cite

show abstract

“…Chitin-binding Ability of Prisilkin-39-Framework proteins are suggested to interact with chitin, a major insoluble component of the organic framework according to the models proposed by Weiner and co-workers (51)(52)(53). In support of the notion that Prisilkin-39 serves a structural role in the formation of the framework during shell growth, a chitin-binding assay was conducted.…”

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

View full text Add to dashboard Cite

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.

show abstract

“…Acidic matrix proteins are believed to be the major components with control over crystal growth, because of their cation-binding capacity (26). Models of the processes of nacre formation have been improved by our increasing knowledge of these proteins (27)(28)(29). Mollusks build their shells using a hydrophobic silk gel, highly acidic aspartic acid-rich proteins in a highly structured chitinous framework (30).…”

mentioning

confidence: 99%

Novel Basic Protein, PfN23, Functions as Key Macromolecule during Nacre Formation

Dong

Pan

Lin

et al. 2012

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

Structure of the Nacreous Organic Matrix of a Bivalve Mollusk Shell Examined in the Hydrated State Using Cryo-TEM

Cited by 489 publications

References 34 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

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

Novel Basic Protein, PfN23, Functions as Key Macromolecule during Nacre Formation

Contact Info

Product

Resources

About