Immunolocalization of matrix proteins in nacre lamellae and their in vivo effects on aragonitic tablet growth

被引:25
作者
Gong, Ningping [1 ]
Shangguan, Junlong [1 ]
Liu, Xiaojun [1 ]
Yan, Zhenguang [1 ]
Ma, Zhuojun [1 ]
Xie, Liping [1 ,2 ]
Zhang, Rongqing [1 ,2 ]
机构
[1] Tsinghua Univ, Dept Biol Sci & Biotechnol, Inst Marine Biotechnol, Beijing 100084, Peoples R China
[2] Tsinghua Univ, Minist Educ, Prot Sci Lab, Beijing 100084, Peoples R China
基金
国家高技术研究发展计划(863计划);
关键词
Mollusk shell nacre; matrix protein; BMP-2; nacrein; antibodies;
D O I
10.1016/j.jsb.2008.05.009
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
How matrix proteins precisely control the growth of nacre lamellae is an open question in biomineralization research. Using the antibodies against matrix proteins for immunolabeling and in vivo experiments. we investigate the structural and functional roles of EDTA-soluble matrix (SM) and EDTA-insoluable matrix (ISM) proteins in nacre biomineralization of the pearl oyster Pinctada fucata. Immunolabeling reveals that a SM proteins, nacrein, distributes within aragonitic tablets and intertabular matrix. An ISM protein. Which we named P43, has been specifically recognized by polyclonal antibodies raised against the recombinant protein of P.fucata bone morphogenetic protein 2 in immunoblot analysis. Immunolabeling indicates that P43 is localized to interlamellar sheet and also embedded within aragonitic tablets. Although nacrein and P43 both distribute within aragnoitic tablets, they function differently in aragonitic tablet growth. When nacrein in suppressed by the antibodies agaisnt it in vivo, crystal over-growth occurs, indicating that this SM protein is a negative regulator in aragonitic tablet growth. When P43 is suppressed in vivo, the organo-mineral assemblage is distrupted, suggesting that P43 is a frame-work matrix. Taken together, SM and ISM proteins are indispensable factors for the growth of nacre lamellae, controlling crystal growth and constructing and the framework of aragonitic tablets. (c) 2008 Elsevier Inc. All rights reserved.
引用
收藏
页码:33 / 40
页数:8
相关论文
共 35 条
[1]   Mollusk shell formation: A source of new concepts for understanding biomineralization processes [J].
Addadi, L ;
Joester, D ;
Nudelman, F ;
Weiner, S .
CHEMISTRY-A EUROPEAN JOURNAL, 2006, 12 (04) :981-987
[2]   Control of crystal phase switching and orientation by soluble mollusc-shell proteins [J].
Belcher, AM ;
Wu, XH ;
Christensen, RJ ;
Hansma, PK ;
Stucky, GD ;
Morse, DE .
NATURE, 1996, 381 (6577) :56-58
[3]   A technique for detecting matrix proteins in the crystalline spicule of the sea urchin embryo [J].
Cho, JW ;
Partin, JS ;
Lennarz, WJ .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (03) :1282-1286
[4]  
Crenshaw M.A., 1972, Biomineralization Res Rep, V6, P6
[5]  
Crenshaw M. A., 1976, The mechanisms of Mineralization in the Invertebrates and Plants, P355
[7]   Culture of outer epithelial cells from mantle tissue to study shell matrix protein secretion for biomineralization [J].
Gong, Ningping ;
Li, Qi ;
Huang, Jing ;
Fang, Zi ;
Zhang, Guiyou ;
Xie, Liping ;
Zhang, Rongqing .
CELL AND TISSUE RESEARCH, 2008, 333 (03) :493-501
[8]   Stimulation of bone marrow cells and bone formation by nacre: In vivo and in vitro studies [J].
Lamghari, M ;
Almeida, MJ ;
Berland, S ;
Huet, H ;
Laurent, A ;
Milet, C ;
Lopez, E .
BONE, 1999, 25 (02) :91S-94S
[9]  
Levi Y, 1998, CHEM-EUR J, V4, P389, DOI 10.1002/(SICI)1521-3765(19980310)4:3<389::AID-CHEM389>3.0.CO
[10]  
2-X