Molluscan Shell Proteins: Primary Structure, Origin, and Evolution

• Published in: Current Topics in Developmental Biology Vol. 80; pp. 209 - 276
• Main Authors: Marin, Frédéric, Luquet, Gilles, Marie, Benjamin, Medakovic, Davorin
• Format: Book Chapter Journal Article
• Language: English
• Published: United States Elsevier Science & Technology 2007; Elsevier
• Subjects: Animals; Bioengineering; Biomaterials; Calcification, Physiologic; Cellular biology; Developmental biology; Evolution, Molecular; Hydrogen-Ion Concentration; Life Sciences; Marine; Molecular Structure; Mollusca; Mollusca - chemistry; Mollusca - genetics; Mollusca - growth & development; Phylogeny; Proteins; Proteins - chemistry; Proteins - genetics
• ISBN: 9780123739148; 0123739144
• ISSN: 0070-2153; 1557-8933
• DOI: 10.1016/S0070-2153(07)80006-8

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.