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

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dc.contributor.authorLebesgue, Nicolas
dc.contributor.authorda Costa, Gonçalo
dc.contributor.authorRibeiro, Raquel Mesquita
dc.contributor.authorRibeiro-Silva, Cristina
dc.contributor.authorMartins, Gabriel G.
dc.contributor.authorMatranga, Valeria
dc.contributor.authorScholten, Arjen
dc.contributor.authorCordeiro, Carlos
dc.contributor.authorHeck, Albert J.R.
dc.contributor.authorAlmeida dos santos, Romana
dc.date.accessioned2020-01-19T19:02:54Z
dc.date.available2020-01-19T19:02:54Z
dc.date.issued2016
dc.description.abstractMarine 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.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.doi10.1016/j.jprot.2016.02.026pt_PT
dc.identifier.issn1874-3919
dc.identifier.urihttp://hdl.handle.net/10451/41086
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherElsevierpt_PT
dc.relation.publisherversionhttps://www.sciencedirect.com/science/article/pii/S1874391916300495pt_PT
dc.subjectSea urchinpt_PT
dc.subjectParacentrotus lividuspt_PT
dc.subjectReversible adhesionpt_PT
dc.subjectTube foot adhesive proteinpt_PT
dc.subjectQuantitative proteomicspt_PT
dc.titleDeciphering the molecular mechanisms underlying sea urchin reversible adhesion: A quantitative proteomics approachpt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage71pt_PT
oaire.citation.startPage61pt_PT
oaire.citation.titleJournal of Proteomicspt_PT
oaire.citation.volume138pt_PT
person.familyNameLopes Almeida dos Santos
person.givenNameRomana
person.identifier.ciencia-idBD12-1D9C-3627
person.identifier.orcid0000-0001-7720-6806
rcaap.rightsrestrictedAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublicationd7b58331-4fdc-410b-878b-199a8f2975cb
relation.isAuthorOfPublication.latestForDiscoveryd7b58331-4fdc-410b-878b-199a8f2975cb

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