文献类型: 外文期刊
作者: Gao, Peng 1 ; Liao, Zhi 2 ; Wang, Xin-xing 2 ; Bao, Lin-fei 2 ; Fan, Mei-hua 2 ; Li, Xiao-min 3 ; Wu, Chang-wen 2 ; Xia, 1 ;
作者机构: 1.Ocean Univ Chinese, Coll Chem & Chem Engn, Qingdao, Peoples R China
2.Zhejiang Ocean Univ, Lab Marine Biol Prot Engn, Zhoushan, Zhejiang, Peoples R China
3.Chinese Acad Fishery Sci, Ctr Biotechnol, Beijing, Peoples R China
期刊名称:PLOS ONE ( 影响因子:3.24; 五年影响因子:3.788 )
ISSN: 1932-6203
年卷期: 2015 年 10 卷 7 期
页码:
收录情况: SCI
摘要: Bivalve shell is a biomineralized tissue with various layers/microstructures and excellent mechanical properties. Shell matrix proteins (SMPs) pervade and envelop the mineral crystals and play essential roles in biomineralization. Despite that Mytilus is an economically important bivalve, only few proteomic studies have been performed for the shell, and current knowledge of the SMP set responsible for different shell layers of Mytilus remains largely patchy. In this study, we observed that Mytilus galloprovincialis shell contained three layers, including nacre, fibrous prism, and myostracum that is involved in shell-muscle attachment. A parallel proteomic analysis was performed for these three layers. By combining LC-MS/ MS analysis with Mytilus EST database interrogations, a whole set of 113 proteins was identified, and the distribution of these proteins in different shell layers followed a mosaic pattern. For each layer, about a half of identified proteins are unique and the others are shared by two or all of three layers. This is the first description of the protein set exclusive to nacre, myostracum, and fibrous prism in Mytilus shell. Moreover, most of identified proteins in the present study are novel SMPs, which greatly extended biomineralization-related protein data of Mytilus. These results are useful, on one hand, for understanding the roles of SMPs in the deposition of different shell layers. On the other hand, the identified protein set of myostracum provides candidates for further exploring the mechanism of adductor muscle-shell attachment.
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