Proteomic dataset of the sea urchin Paracentrotus lividus adhesive organs and secreted adhesive
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...
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Format: | Article |
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Elsevier
2016-06-01
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Series: | Data in Brief |
Online Access: | http://www.sciencedirect.com/science/article/pii/S2352340916302165 |
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Article |
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DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Nicolas Lebesgue Gonçalo da Costa Raquel Mesquita Ribeiro Cristina Ribeiro-Silva Gabriel G. Martins Valeria Matranga Arjen Scholten Carlos Cordeiro Albert J.R. Heck Romana Santos |
spellingShingle |
Nicolas Lebesgue Gonçalo da Costa Raquel Mesquita Ribeiro Cristina Ribeiro-Silva Gabriel G. Martins Valeria Matranga Arjen Scholten Carlos Cordeiro Albert J.R. Heck Romana Santos Proteomic dataset of the sea urchin Paracentrotus lividus adhesive organs and secreted adhesive Data in Brief |
author_facet |
Nicolas Lebesgue Gonçalo da Costa Raquel Mesquita Ribeiro Cristina Ribeiro-Silva Gabriel G. Martins Valeria Matranga Arjen Scholten Carlos Cordeiro Albert J.R. Heck Romana Santos |
author_sort |
Nicolas Lebesgue |
title |
Proteomic dataset of the sea urchin Paracentrotus lividus adhesive organs and secreted adhesive |
title_short |
Proteomic dataset of the sea urchin Paracentrotus lividus adhesive organs and secreted adhesive |
title_full |
Proteomic dataset of the sea urchin Paracentrotus lividus adhesive organs and secreted adhesive |
title_fullStr |
Proteomic dataset of the sea urchin Paracentrotus lividus adhesive organs and secreted adhesive |
title_full_unstemmed |
Proteomic dataset of the sea urchin Paracentrotus lividus adhesive organs and secreted adhesive |
title_sort |
proteomic dataset of the sea urchin paracentrotus lividus adhesive organs and secreted adhesive |
publisher |
Elsevier |
series |
Data in Brief |
issn |
2352-3409 |
publishDate |
2016-06-01 |
description |
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: Sea urchin, Paracentrotus lividus, Tube feet, Secreted, Adhesive, Quantitative proteomics |
url |
http://www.sciencedirect.com/science/article/pii/S2352340916302165 |
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doaj-e3c36aefc1a84f31ad120a77917128042020-11-25T02:40:01ZengElsevierData in Brief2352-34092016-06-01714971505Proteomic dataset of the sea urchin Paracentrotus lividus adhesive organs and secreted adhesiveNicolas Lebesgue0Gonçalo da Costa1Raquel Mesquita Ribeiro2Cristina Ribeiro-Silva3Gabriel G. Martins4Valeria Matranga5Arjen Scholten6Carlos Cordeiro7Albert J.R. Heck8Romana Santos9Netherlands Proteomics Center, Padualaan 8, 3584 CH Utrecht, The Netherlands; Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute of Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, The NetherlandsCentro de Química e Bioquímica, Departamento de Química e Bioquímica, Faculdade de Ciências da Universidade de Lisboa, 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, PortugalCentro de Química e Bioquímica, Departamento de Química e Bioquímica, Faculdade de Ciências da Universidade de Lisboa, Campo Grande, 1749-016 Lisboa, Portugal; Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade de Lisboa, 1749-016 Lisboa, PortugalCentro de Química e Bioquímica, Departamento de Química e Bioquímica, Faculdade de Ciências da Universidade de Lisboa, Campo Grande, 1749-016 Lisboa, Portugal; Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade de Lisboa, 1749-016 Lisboa, PortugalInstituto Gulbenkian de Ciência, R. da Quinta Grande 6, 2780-156 Oeiras, Portugal; Centro de Ecologia, Evolução e Alterações Ambientais, Faculdade de Ciências da Universidade de Lisboa, Campo Grande, 1749-016 Lisboa, PortugalConsiglio Nazionale delle Ricerche, Istituto di Biomedicina e Immunologia Molecolare, ‘Alberto Monroy’, Via Ugo La Malfa 153, 90146 Palermo, ItalyNetherlands Proteomics Center, Padualaan 8, 3584 CH Utrecht, The Netherlands; Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute of Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, The NetherlandsCentro de Química e Bioquímica, Departamento de Química e Bioquímica, Faculdade de Ciências da Universidade de Lisboa, 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, PortugalNetherlands Proteomics Center, Padualaan 8, 3584 CH Utrecht, The Netherlands; Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute of Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, The NetherlandsCentro de Química e Bioquímica, Departamento de Química e Bioquímica, Faculdade de Ciências da Universidade de Lisboa, Campo Grande, 1749-016 Lisboa, Portugal; MARE – Centro de Ciências do Mar e do Ambiente, Faculdade de Ciências da Universidade de Lisboa, Campo Grande, 1749-016 Lisboa, Portugal; Corresponding author at: MARE - Centro de Ciências do Mar e do Ambiente, Faculdade de Ciências da Universidade de Lisboa, Campo Grande, 1749-016 Lisboa, Portugal. Tel.: +351 21 750 0857; fax: +351 21 750 00 09.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: Sea urchin, Paracentrotus lividus, Tube feet, Secreted, Adhesive, Quantitative proteomicshttp://www.sciencedirect.com/science/article/pii/S2352340916302165 |