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

被引:115
作者
Zhang, Y
Xie, LP
Meng, QX
Jiang, TM
Pu, RL
Chen, L
Zhang, RQ [1 ]
机构
[1] Tsing Hua Univ, Dept Biol Sci & Biotechnol, Beijing 100084, Peoples R China
[2] Fourth Mil Med Univ, Dept Histol & Embryol, Xian 710032, Peoples R China
[3] Tsing Hua Univ, Prot Sci Lab, Minist Educ, Beijing 100084, Peoples R China
来源
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 2003年 / 135卷 / 03期
基金
国家高技术研究发展计划(863计划); 中国国家自然科学基金;
关键词
MSI7; MSI31; matrix protein; nacre; biomineralization; framework formation; pearl oyster; Pinctada fucata;
D O I
10.1016/S1096-4959(03)00138-6
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:565 / 573
页数:9
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