Molluscan shell proteins: primary structure, origin, and evolution.

Molluscan shell proteins: primary structure, origin, and evolution. Research Abstract Details 

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Molluscan shell proteins: primary structure, origin, and evolution. Abstract Text:

Marin,Gilles Luquet,Benjamin Marie,Davorin Medakovic,

In the last few years, the field of molluscan biomineralization has known a tremendous mutation, regarding fundamental concepts on biomineralization regulation as well as regarding the methods of investigation. The most recent advances deal more particularly with the structure of shell biominerals at nanoscale and the identification of an increasing number of shell matrix protein components. Although the matrix is quantitatively a minor constituent in the shell of mollusks (less than 5% w/w), it is, however, the major component that controls different aspects of the shell formation processes: synthesis of transient amorphous minerals and evolution to crystalline phases, choice of the calcium carbonate polymorph (calcite vs aragonite), organization of crystallites in complex shell textures (microstructures). Until recently, the classical paradigm in molluscan shell biomineralization was to consider that the control of shell synthesis was performed primarily by two antagonistic mechanisms: crystal nucleation and growth inhibition. New concepts and emerging models try now to translate a more complex reality, which is remarkably illustrated by the wide variety of shell proteins, characterized since the mid-1990s, and described in this chapter. These proteins cover a broad spectrum of pI, from very acidic to very basic. The primary structure of a number of them is composed of different modules, suggesting that these proteins are multifunctional. Some of them exhibit enzymatic activities. Others may be involved in cell signaling. The oldness of shell proteins is discussed, in relation with the Cambrian appearance of the mollusks as a mineralizing phylum and with the Phanerozoic evolution of this group. Nowadays, the extracellular calcifying shell matrix appears as a whole integrated system, which regulates protein-mineral and protein-protein interactions as well as feedback interactions between the biominerals and the calcifying epithelium that synthesized them. Consequently, the molluscan shell matrix may be a source of bioactive molecules that would offer interesting perspectives in biomaterials and biomedical fields.

Molluscan shell proteins: primary structure, origin, and evolution. Publishing Authors By Initials

F Marin,G Luquet,B Marie,D Medakovic,

For similar proteins research abstracts see: proteins research

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Molluscan shell proteins: primary structure, origin, and evolution. Journal Published:

PUBLICATION TYPE: Review

Journal: Current topics in developmental biology

VOLUME: 80

Page Numbers: 209-76

Journal Abbreviation: Curr. Top. Dev. Biol.

ISSN: 0070-2153

DAY: 21

MONTH: 11

YEAR: 2008

Molluscan shell proteins: primary structure, origin, and evolution. Information

Number of References: 258

LANGUAGE: eng

NlmUniqueID: 163114

Molluscan shell proteins: primary structure, origin, and evolution. Keywords Mesh Terms:

KEYWORDS: Proteins

MESH TERMS: genetics

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Substance Name: Proteins

Registry Number: 0

Grant and Affiliation Information for Molluscan shell proteins: primary structure, origin, and evolution.

AFFILIATION: UMR CNRS 5561 Biogéosciences, Université de Bourgogne 6 Boulevard Gabriel, 21000 DIJON, France.

Country: United States

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MEDLINETA: Curr Top Dev Biol

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