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. 2016 Apr 22:7:1497-505.
doi: 10.1016/j.dib.2016.04.002. eCollection 2016 Jun.

Proteomic dataset of the sea urchin Paracentrotus lividus adhesive organs and secreted adhesive

Nicolas Lebesgue  1 , Gonçalo da Costa  2 , Raquel Mesquita Ribeiro  3 , Cristina Ribeiro-Silva  3 , Gabriel G Martins  4 , Valeria Matranga  5 , Arjen Scholten  1 , Carlos Cordeiro  2 , Albert J R Heck  1 , Romana Santos  6
Affiliations

Proteomic dataset of the sea urchin Paracentrotus lividus adhesive organs and secreted adhesive

Nicolas Lebesgue et al. Data Brief. .

Abstract

Sea urchins have specialized adhesive organs called tube feet, which mediate strong but reversible adhesion. Tube feet are composed by a disc, producing adhesive and de-adhesive secretions for substratum attachment, and a stem for movement. After detachment the secreted adhesive remains bound to the substratum as a footprint. Recently, a label-free quantitative proteomic approach coupled with the latest mass-spectrometry technology was used to analyze the differential proteome of Paracentrotus lividus adhesive organ, comparing protein expression levels in the tube feet adhesive part (the disc) versus the non-adhesive part (the stem), and also to profile the proteome of the secreted adhesive (glue). This data article contains complementary figures and results related to the research article "Deciphering the molecular mechanisms underlying sea urchin reversible adhesion: a quantitative proteomics approach" (Lebesgue et al., 2016) [1]. Here we provide a dataset of 1384 non-redundant proteins, their fragmented peptides and expression levels, resultant from the analysis of the tube feet differential proteome. Of these, 163 highly over-expressed tube feet disc proteins (>3-fold), likely representing the most relevant proteins for sea urchin reversible adhesion, were further annotated in order to determine the potential functions. In addition, we provide a dataset of 611 non-redundant proteins identified in the secreted adhesive proteome, as well as their functional annotation and grouping in 5 major protein groups related with adhesive exocytosis, and microbial protection. This list was further analyzed to identify the most abundant protein groups and pinpoint putative adhesive proteins, such as Nectin, the most abundant adhesive protein in sea urchin glue. The obtained data uncover the key proteins involved in sea urchins reversible adhesion, representing a step forward to the development of new wet-effective bio-inspired adhesives.

Keywords: Adhesive; Paracentrotus lividus; Quantitative proteomics; Sea urchin; Secreted; Tube feet.

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Figures

Fig. 1
Fig. 1
Paracentrotus lividus tube feet disc (A) and stem (B) in-solution digest fractionation gradient by strong cation exchange.
Fig. 2
Fig. 2
Paracentrotus lividus tube feet disc (A) and stem (B) proteins dynamic range.
Fig. 3.
Fig. 3
Annotation distribution of the proteins identified in Paracentrotus lividus tube feet (A) and the proteins identified in secreted adhesive (B).
Fig. 4
Fig. 4
Gene Ontology distribution of the proteins identified in Paracentrotus lividus tube feet (A) and the proteins identified in secreted adhesive (B), grouped by biological process (BP), molecular function (MF) and cellular component (CC).
Fig. 5
Fig. 5
MS/MS spectra for the unique peptide IGIEDGR from the overexpressed Nectin-like variant W4Z4Y0 (A) and the unique peptide unique peptide QLHEVSGImSQGR from the overexpressed Nectin-like variant W4ZF96.
See this image and copyright information in PMC

References

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