Utilize este identificador para referenciar este registo: http://hdl.handle.net/10451/41086
Título: Deciphering the molecular mechanisms underlying sea urchin reversible adhesion: A quantitative proteomics approach
Autor: Lebesgue, Nicolas
da Costa, Gonçalo
Ribeiro, Raquel Mesquita
Ribeiro-Silva, Cristina
Martins, Gabriel G.
Matranga, Valeria
Scholten, Arjen
Cordeiro, Carlos
Heck, Albert J.R.
Almeida dos santos, Romana
Palavras-chave: Sea urchin
Paracentrotus lividus
Reversible adhesion
Tube foot adhesive protein
Quantitative proteomics
Data: 2016
Editora: Elsevier
Resumo: 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, themolecularmechanisms 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.
Peer review: yes
URI: http://hdl.handle.net/10451/41086
DOI: 10.1016/j.jprot.2016.02.026
ISSN: 1874-3919
Versão do Editor: https://www.sciencedirect.com/science/article/pii/S1874391916300495
Aparece nas colecções:MARE - Artigos em Revistas Internacionais

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