A novel matrix protein participating in the nacre framework formation of pearl oyster, Pinctada fucata

Publication Type:Journal Article
Year of Publication:2003
Authors:Y. Zhang, Xie, L. P., Meng, Q. X., Jiang, T. M., Pu, R. L., Chen, L., Zhang, R. Q.
Journal:Comparative Biochemistry and Physiology B-Biochemistry & Molecular Biology
Volume:135
Pagination:565-573
Date Published:JUL
Accession Number:ISI:000183967400016
Keywords:biomineralization, bivalvia, matrix protein, molecules, mollusca, nacre, pinctada, pinctada fucata, pteriidae, pterioida, pterioidea, shell formation
Abstract:

Understanding the molecular composition is of great interest for both nacre formation mechanism and biomineralization in mollusk shell. A cDNA clone encoding an MSI31 relative, termed MSI7 because of its estimated molecular mass of 7.3 kDa, was isolated from the pearl oyster, Pinctada fucata. This novel protein shares similarity with MSI31, a prismatic framework protein of R fucata. It is peculiar that MSI7 is much shorter in size, harboring only the Gly-rich sequence that has been proposed to be critical for Ca2+ binding. In situ hybridization result showed that MSI7 mRNA was expressed specifically at the folds and outer epithelia of the mantle, indicating that MSI7 participates in the framework formation of both the nacreous layer and prismatic layer. In vitro experiment on the function of MSI7 suggested that it accelerates the nucleation and precipitation of CaCO3. Taken together, we have identified a novel matrix protein of the pearl oyster, which may play an important role in determining the texture of nacre. (C) 2003 Elsevier Science Inc. All rights reserved.

URL:<Go to ISI>://000183967400016
Alternate Journal:Comp Biochem Phys BComp Biochem Phys B
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