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从贻贝中鉴定出一种具有 vWA 结构域的新型壳基质蛋白。

Characterization of a novel shell matrix protein with vWA domain from Mytilus coruscus.

机构信息

Laboratory of Marine Biology Protein Engineering, Marine Science and Technical College, Zhejiang Ocean University , Zhoushan City, Zhejiang, China.

出版信息

Biosci Biotechnol Biochem. 2020 Aug;84(8):1629-1644. doi: 10.1080/09168451.2020.1756735. Epub 2020 Apr 21.

DOI:10.1080/09168451.2020.1756735
PMID:32314940
Abstract

Mollusk shell is a product of biomineralization with excellent mechanical properties, and the shell matrix proteins (SMPs) have important functions in shell formation. A vWA domain-containing protein (VDCP) was identified from the shell of as a novel shell matrix protein. The VDCP gene is expressed at a high level in specific locations in the mantle and adductor muscle. Recombinant VDCP (rVDCP) showed abilities to alter the morphology of both calcite and aragonite, induce the polymorph change of calcite, bind calcite, and decrease the crystallization rate of calcite. In addition, immunohistochemistry analyses revealed the specific location of VDCP in the mantle, the adductor muscle, and the myostracum layer of the shell. Furthermore, a pull-down analysis revealed eight protein interaction partners of VDCP in shell matrices and provided a possible protein-protein interaction network of VDCP in the shell.

摘要

软体动物贝壳是生物矿化作用的产物,具有优异的机械性能,贝壳基质蛋白 (SMPs) 在贝壳形成中具有重要功能。从 的贝壳中鉴定出一种含有 vWA 结构域的蛋白 (VDCP),它是一种新型的贝壳基质蛋白。VDCP 基因在套膜和闭壳肌的特定位置高表达。重组 VDCP(rVDCP)表现出改变方解石和文石形态、诱导方解石多晶型转变、结合方解石以及降低方解石结晶速率的能力。此外,免疫组织化学分析显示 VDCP 特异性存在于套膜、闭壳肌和贝壳的肌鞘层中。此外,下拉分析揭示了壳基质中 VDCP 的八个蛋白相互作用伙伴,并提供了 VDCP 在贝壳中的可能的蛋白-蛋白相互作用网络。

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FEBS Open Bio. 2020 Oct;10(10):2216-2234. doi: 10.1002/2211-5463.12972. Epub 2020 Sep 21.