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解析海胆可逆黏附背后的分子机制:一种定量蛋白质组学方法。

Deciphering the molecular mechanisms underlying sea urchin reversible adhesion: A quantitative proteomics approach.

作者信息

Lebesgue Nicolas, da Costa Gonçalo, Ribeiro Raquel Mesquita, Ribeiro-Silva Cristina, Martins Gabriel G, Matranga Valeria, Scholten Arjen, Cordeiro Carlos, Heck Albert J R, Santos Romana

机构信息

Netherlands Proteomics Center, Padualaan 8, 3584, CH, Utrecht, Netherlands; Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute of Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584, CH, Utrecht, Netherlands.

Centro de Química e Bioquímica, Departamento de Química e Bioquímica, Faculdade de Ciências da Universidade de Lisboa, Campo Grande, Campo Grande, 1749-016, Lisboa, Portugal; Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade de Lisboa, 1749-016, Lisboa, Portugal; Laboratório de FTICR e espectrometria de massa estrutural, Faculdade de Ciências, Universidade de Lisboa, 1749-016, Lisboa, Portugal.

出版信息

J Proteomics. 2016 Apr 14;138:61-71. doi: 10.1016/j.jprot.2016.02.026. Epub 2016 Feb 27.

Abstract

UNLABELLED

Marine bioadhesives have unmatched performances in wet environments, being an inspiration for biomedical applications. In sea urchins specialized adhesive organs, tube feet, mediate reversible adhesion, being composed by a disc, producing adhesive and de-adhesive secretions, and a motile stem. After tube foot detachment, the secreted adhesive remains bound to the substratum as a footprint. Sea urchin adhesive is composed by proteins and sugars, but so far only one protein, Nectin, was shown to be over-expressed as a transcript in tube feet discs, suggesting its involvement in sea urchin adhesion. Here we use high-resolution quantitative mass-spectrometry to perform the first study combining the analysis of the differential proteome of an adhesive organ, with the proteome of its secreted adhesive. This strategy allowed us to identify 163 highly over-expressed disc proteins, specifically involved in sea urchin reversible adhesion; to find that 70% of the secreted adhesive components fall within five protein groups, involved in exocytosis and microbial protection; and to provide evidences that Nectin is not only highly expressed in tube feet discs but is an actual component of the adhesive. These results give an unprecedented insight into the molecular mechanisms underlying sea urchin adhesion, and opening new doors to develop wet-reliable, reversible, and ecological biomimetic adhesives.

SIGNIFICANCE

Sea urchins attach strongly but in a reversible manner to substratum, being a valuable source of inspiration for industrial and biomedical applications. Yet, the molecular mechanisms governing reversible adhesion are still poorly studied delaying the engineering of biomimetic adhesives. We used the latest mass spectrometry techniques to analyze the differential proteome of an adhesive organ and the proteome of its secreted adhesive, allowing us to uncover the key players in sea urchin reversible adhesion. We demonstrate, that Nectin, a protein previously pointed out as potentially involved in sea urchin adhesion, is not only highly expressed in tube feet discs, but is a genuine component of the secreted adhesive.

摘要

未标注

海洋生物粘合剂在潮湿环境中具有无与伦比的性能,为生物医学应用提供了灵感。在海胆的特殊粘附器官——管足中,介导可逆粘附,管足由一个圆盘、产生粘附和脱粘分泌物的部分以及一个可移动的柄组成。管足脱落后,分泌的粘合剂会作为足迹留在基质上。海胆粘合剂由蛋白质和糖类组成,但到目前为止,只有一种蛋白质——NECTIN,在管足圆盘的转录本中被证明过度表达,表明它参与海胆的粘附。在这里,我们使用高分辨率定量质谱法进行了第一项研究,将粘附器官的差异蛋白质组分析与其分泌粘合剂的蛋白质组分析相结合。这种策略使我们能够鉴定出163种高度过度表达的圆盘蛋白,它们专门参与海胆的可逆粘附;发现70%的分泌粘合剂成分属于五个蛋白质组,参与胞吐作用和微生物保护;并提供证据表明NECTIN不仅在管足圆盘中高度表达,而且是粘合剂的实际成分。这些结果为海胆粘附的分子机制提供了前所未有的见解,并为开发可靠、可逆和生态的湿环境仿生粘合剂打开了新的大门。

意义

海胆能牢固但可逆地附着在基质上,是工业和生物医学应用的宝贵灵感来源。然而,控制可逆粘附的分子机制仍研究不足,延迟了仿生粘合剂的工程设计。我们使用最新的质谱技术分析了粘附器官的差异蛋白质组及其分泌粘合剂的蛋白质组,使我们能够揭示海胆可逆粘附的关键因素。我们证明,NECTIN这种先前被指出可能参与海胆粘附的蛋白质,不仅在管足圆盘中高度表达,而且是分泌粘合剂的真正成分。

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