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.
Highlights
Sea urchins have specialized adhesive organs called tube feet, which mediate strong but reversible adhesion
A label-free quantitative proteomic approach coupled with the latest mass-spectrometry technology
Lebesgue et al / Data in Brief 7 (2016) 1497–1505 was used to analyze the differential proteome of Paracentrotus lividus adhesive organ, comparing protein expression levels in the tube feet adhesive part versus the non-adhesive part, and to profile the proteome of the secreted adhesive
Summary
Biology Proteomics analysis of sea urchin adhesive organs and secreted adhesives. Figure, table Mass spectrometry, LC-MS/MS using a Orbitrap Q-exactive mass spectrometer (Thermo Scientific). To perform the differential proteome of the sea urchin Paracentrotus lividus adhesive organs, tube feet were dissected to separate discs (adhesive part) from stems (non-adhesive part). Both samples were in-solution digested with Lys-C and trypsin and. Present data can be further explored in other to find key functionalities in sea urchin adhesive proteins and by comparison with other marine adhesive proteins, significantly simplify the development of bio-inspired adhesives This dataset provides a comprehensive list of non-redundant proteins, their fragmented peptides and expression levels, resultant from the analysis of the tube feet differential proteome. This list was further analyzed to identify the most abundant protein groups and pinpoint putative adhesive proteins
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