| ZHU Yaoyao,SUN Chengjun,SONG Yingfei,JIANG Fenghua,YIN Xiaofei,TANG Min,DING Haibing.The study of the adductor muscle-shell interface structure in three Mollusc species[J].Acta Oceanologica Sinica,2016,35(8):57-64 |
| 三种软体动物闭壳肌-壳界面结构研究 |
| The study of the adductor muscle-shell interface structure in three Mollusc species |
| 投稿时间：2015-05-11 修订日期：2015-09-14 |
| DOI：10.1007/s13131-016-0878-x |
| 中文关键词: 软体动物壳 闭壳肌-壳界面 壳蛋白 壳微结构 |
| 英文关键词:mollusc shell adductor muscle-shell interface shell protein shell microstructure |
| 基金项目:The Basic Scientific Fund for National Public Research Institutes of China under contract No. 2011T10; the National Natural Science Foundation of China-Shandong Joint Grant U1406402-5; Qingdao Talents Program under contract No. 13-CX-20; the National Natural Science Foundation of China under contract Nos 31100567, 41176061, 41521064, 41306074 and 31160098; the Taishan Scholar Program. |
| 作者 | 单位 | E-mail | | 朱曜曜 | 国家海洋局第一海洋研究所生态中心, 中国青岛, 266001
中国海洋大学化学化工学院, 中国青岛, 266100 | | | 孙承君 | 国家海洋局第一海洋研究所生态中心, 中国青岛, 266001
海洋科学与技术国家实验室海洋药物与生物制品功能实验室, 中国青岛, 266071 | | | 宋影飞 | 中国海洋大学化学化工学院, 中国青岛, 266100 | | | 蒋凤华 | 国家海洋局第一海洋研究所生态中心, 中国青岛, 266001 | | | 尹晓斐 | 国家海洋局第一海洋研究所生态中心, 中国青岛, 266001 | | | 唐敏 | 海南大学热带岛屿资源先进材料教育部重点实验室, 中国海南, 570228
海南大学材料与化工学院, 中国海南, 570228 | | | 丁海兵 | 中国海洋大学海洋化学理论与工程技术教育部重点实验室, 中国青岛, 266100
中国海洋大学海洋科学与技术青岛协同创新中心, 中国青岛, 266100 | dinghb@ouc.edu.cn |
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| 中文摘要: |
| 闭壳肌的疤痕部位（AMS）是闭壳肌和壳的固定点。它是一个重要的有机-无机界面和应力分布面。尽管有一些近期的研究进展，我们对AMS组成和结构的了解仍然是有限的。这里，我们研究比较了三种双壳类动物：厚壳贻贝、栉孔扇贝、菲律宾蛤仔的AMS。结果表明这三种动物的AMS明显不同。厚壳贻贝和栉孔扇贝在AMS的壳结构珍珠片层上部有一柱状层，该层在厚壳贻贝中的结构更有规律。菲律宾蛤仔缺乏此柱状层。原子力显微镜结果显示在三种软体动物中AMS的结构比珍珠层结构更光滑。傅立叶变换红外分析结果显示珍珠层和AMS层组成成分略有不同。聚丙烯酰胺凝胶电泳蛋白分离结果显示在厚壳贻贝界面柱状层存在一种约70 kDa的蛋白。对这种蛋白的进一步分析显示其还有较高摩尔比的Asx（Asp+Asn），Glx（Glu+Gln）和Gly。AMS的特殊结构和组成对其稳定性、粘性以及在该应力分散部位的功能有重要作用。 |
| 英文摘要: |
| The adductor muscle scar (AMS) is the fixation point of adductor muscle to the shell. It is an important organicinorganic interface and stress distribution area. Despite recent advances, our understanding of the structure and composition of the AMS remain limited. Here, we report study on the AMS of three bivalves:Mytilus coruscus, Chlamys farreri and Ruditapes philippinarum. Results showed that there were significant differences among their AMS structures. Both M. coruscus and C. farreri were found to have a columnar layer above the nacreous platelet shell structure at the AMS and this layer was more organized in M. coruscus. There was no distinguishable twolayer structure in R. philippinarum. Atomic force microscopy (AFM) and Fourier transform infrared spectroscopy (FT-IR) results showed that the AMS was much smoother than the nacreous inner shell in all the three species and the AMS had minor different compositions from the nacreous shell layer. SDS-PAGE (sodium dodecyl-sulfate polyacrylamide gel electophoresis) study of the proteins isolated from the interface indicated that there was a 70 kDa protein which seemed to be specifically located to the highly organized columnar AMS structure in Mytilus coruscus. Further analysis of this protein showed it contained high level of Asx (Asp+Asn), Glx (Glu+Gln) and Gly. The special structure and composition of the AMS might play important roles in the stability, adhesion and function at this stress distribution site. |
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