@article {7912,
	title = {A novel ferritin subunit involved in shell formation from the pearl oyster (<i>Pinctada fucata</i>)},
	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 = {<Go to ISI>://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, <i>Pinctada fucata</i>},
	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 = {<Go to ISI>://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.}
}
