@article {7912, title = {A novel ferritin subunit involved in shell formation from the pearl oyster (Pinctada fucata)}, journal = {Comparative Biochemistry and Physiology B-Biochemistry \& Molecular Biology}, volume = {135}, number = {1}, year = {2003}, note = {ABSTRACT ONLYTimes Cited: 2ArticleEnglishCited References Count: 31686vy}, month = {MAY}, pages = {43-54}, abstract = {Iron is one of the most important minor elements in the shell of bivalves. This study was designed to investigate the involvement of ferritin, the principal protein for iron storage, in shell formation. A novel ferritin cDNA from the pearl oyster (Pinctada fucata) was isolated and characterized. The ferritin cDNA encodes a 206 amino acid polypeptide, which shares high similarity with snail soma ferritin and the H-chains of mammalian ferritins. Oyster ferritin mRNA shows the highest level of expression in the mantle, the organ for shell formation. In situ hybridization analysis revealed that oyster ferritin mRNA is expressed at the highest level at the mantle fold, a region essential for metal accumulation and contributes to metal incorporation into the shell. Taken together, these results suggest that ferritin is involved in shell formation by iron storage. The identification and characterization of oyster ferritin also helps to further understand the structural and functional properties of molluscan ferritins. (C) 2003 Elsevier Science Inc. All rights reserved.}, keywords = {biomineralization, evolution, ferritin, mantle, molecules, mollusca, pinctada, pinctada fucata, pteriidae, pterioida, pterioidea, shell formation}, url = {://000183342700006}, author = {Zhang, Y. and Meng, Q. X. and Jiang, T. M. and Wang, H. Z. and Xie, L. P. and Zhang, R. Q.} } @article {7913, title = {A novel matrix protein participating in the nacre framework formation of pearl oyster, Pinctada fucata}, journal = {Comparative Biochemistry and Physiology B-Biochemistry \& Molecular Biology}, volume = {135}, number = {3}, year = {2003}, note = {DO NOT HAVETimes Cited: 7ArticleEnglishCited References Count: 20697wz}, month = {JUL}, pages = {565-573}, 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.}, keywords = {biomineralization, bivalvia, matrix protein, molecules, mollusca, nacre, pinctada, pinctada fucata, pteriidae, pterioida, pterioidea, shell formation}, url = {://000183967400016}, author = {Zhang, Y. and Xie, L. P. and Meng, Q. X. and Jiang, T. M. and Pu, R. L. and Chen, L. and Zhang, R. Q.} } @article {7583, title = {Tough as shells}, journal = {Natural History}, volume = {115}, number = {5}, year = {2006}, note = {Journal issue}, pages = {28-29}, keywords = {biomechanics, biomimetics, biomineralization, nacre}, author = {Summers, Adam} } @article {6952, title = {Conservation of signal molecules involved in biomineralisation control in calcifying matrices of bone and shell}, journal = {C. R. Palevol}, volume = {3}, year = {2004}, note = {PDF}, pages = {493{\textendash}501}, keywords = {biomineralization, calcification, matrix protein, mollusca, nacre, pinctada, pinctada fucata, pteriidae, pterioidea}, author = {Milet, Christian and Berland, Sophie and Lamghari, Meriem and Mouries, Lucilia and Jolly, C{\'e}cile and Borzeix, Sandrine and Doumenc, Dominique and Lopez, Evelyne} } @article {6802, title = {Nacre, osteogenic and osteoinductive properties}, journal = {Bulletin de L{\textquoteright}institut Oc{\'e}anographique}, volume = {14}, number = {3}, year = {1995}, pages = {49-57}, keywords = {biomineralization, bivalvia, mollusca, nacre, pinctada, pinctada maxima, pteriidae, pterioida, pterioidea}, author = {Lopez, Evelyne and Berland, Sophie and Le Faou, Anne} } @article {6765, title = {Cloning and expression of a pivotal calcium metabolism regulator: calmodulin involved in shell formation from pearl oyster (Pinctada fucata)}, journal = {Comparative Biochemistry and Physiology B-Biochemistry \& Molecular Biology}, volume = {138}, number = {3}, year = {2004}, note = {DO NOT HAVETimes Cited: 0ArticleEnglishCited References Count: 36852vg}, month = {JUL}, pages = {235-243}, abstract = {The shells of bivalves are mainly composed of calcium carbonate, a product of calcium metabolism. In the process of shell formation, the uptake, transport and recruitment of calcium ion are highly regulated and involved in many factors. Among these regulatory factors, calmodulin (CaM), a pivotal multifunction regulator of calcium metabolism in nearly all organisms, is thought to play an important role in the calcium metabolism involved in shell formation. In this study, a full-length CaM cDNA was isolated from the pearl oyster (Pinctada fucata). The oyster calmodulin encodes a 16.8 kDa protein which shares high similarity with vertebrate calmodulin. The oyster CaM mRNA shows the highest level of expression in the gill, a key organ involved in calcium uptake in oyster calcium metabolism. In situ hybridization results revealed that oyster CaM mRNA is expressed at the folds and the outer epithelial cells of the dorsal region of the mantle, suggesting that CaM is involved in regulation of calcium transport and secretion. Oyster CaM also showed a typical Ca2+ dependent electrophoretic shift characterization and calcium binding activity. Taken together, we have identified and characterized a pivotal calcium metabolism regulator of the oyster that may play an important role in regulation of calcium uptake, transport and secretion in the process of shell formation. (C) 2004 Elsevier Inc. All rights reserved.}, keywords = {biomineralization, bivalvia, calcium metabolism, calmodulin, molecules, mollusca, pinctada, pinctada fucata, pteriidae, pterioidea}, url = {://000223784200005}, author = {Li, S. and Xie, L. P. and Zhang, C. and Zhang, Y. and Gu, M. Z. and Zhang, R. Q.} } @article {6005, title = {Organization pattern of nacre in Pteriidae (Bivalvia: Mollusca) explained by crystal competition}, journal = {Proceedings of the Royal Society of London. Series B}, volume = {273}, year = {2006}, note = {PDF}, pages = {1329-1337}, keywords = {atrina, atrina pectinata, biomineralization, bivalvia, isognomon, isognomon radiatus, isognomonidae, mollusca, nacre, pinctada, pinctada martensii, pinnidae, Pteria, pteria avicular, pteria hirundo, pteriidae, pterioidea}, author = {Checa, Antonio G. and Okamoto, Takashi and Ram{\'\i}rez, Joaqu{\'\i}m} }