title: Cloning, Characterization, and Expression Levels of the Nectin Gene from the Tube Feet of the Sea Urchin Paracentrotus Lividus.
abstract: Marine bioadhesives perform in ways that manmade products simply cannot match, especially in wet environments. Despite their technological potential, bioadhesive molecular mechanisms are still largely understudied, and sea urchin adhesion is no exception. These animals inhabit wave-swept shores, relying on specialized adhesive organs, tube feet, composed by an adhesive disc and a motile stem. The disc encloses a duo-gland adhesive system, producing adhesive and deadhesive secretions for strong reversible substratum attachment. The disclosure of sea urchin Paracentrotus lividus tube foot disc proteome led to the identification of a secreted adhesion protein, Nectin, never before reported in adult adhesive organs but, that given its adhesive function in eggs/embryos, was pointed out as a putative substratum adhesive protein in adults. To further understand Nectin involvement in sea urchin adhesion, Nectin cDNA was amplified for the first time from P. lividus adhesive organs, showing that not only the known Nectin mRNA, called Nectin-1 (GenBank AJ578435), is expressed in the adults tube feet but also a new mRNA sequence, called Nectin-2 (GenBank KT351732), differing in 15 missense nucleotide substitutions. Nectin genomic DNA was also obtained for the first time, indicating that both Nectin-1 and Nectin-2 derive from a single gene. In addition, expression analysis showed that both Nectins are overexpressed in tube feet discs, its expression being significantly higher in tube feet discs from sea urchins just after collection from the field relative to sea urchin from aquarium. These data further advocate for Nectin involvement in sea urchin reversible adhesion, suggesting that its expression might be regulated according to the hydrodynamic conditions.
authors.affiliation: Centro de Biotecnologia dos Açores, Departamento de Biologia, Universidade dos Açores, 9501-801, Ponta Delgada, Açores, Portugal.|Structural and Cellular Microbiology Unit, Instituto de Tecnologia Química e Biológica, 2780-157, Oeiras, Portugal.
authors.forename: Duarte
authors.initials: D
authors.lastname: Toubarro
authors.affiliation: Centro de Biotecnologia dos Açores, Departamento de Biologia, Universidade dos Açores, 9501-801, Ponta Delgada, Açores, Portugal.
authors.forename: Analuce
authors.initials: A
authors.lastname: Gouveia
authors.affiliation: Centro 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.
authors.forename: Raquel Mesquita
authors.initials: RM
authors.lastname: Ribeiro
authors.affiliation: Centro de Biotecnologia dos Açores, Departamento de Biologia, Universidade dos Açores, 9501-801, Ponta Delgada, Açores, Portugal.
authors.forename: Nélson
authors.initials: N
authors.lastname: Simões
authors.affiliation: Centro 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, Portugal.
authors.forename: Gonçalo
authors.initials: G
authors.lastname: da Costa
authors.affiliation: Centro 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, Portugal.
authors.forename: Carlos
authors.initials: C
authors.lastname: Cordeiro
authors.affiliation: Centro de Química e Bioquímica, Faculdade de Ciências da Universidade de Lisboa, Campo Grande, 1749-016, Lisboa, Portugal. romana.santos@campus.ul.pt.|MARE-Centro de Ciências do Mar e do Ambiente, Faculdade de Ciências da Universidade de Lisboa, Campo Grande, 1749-016, Lisboa, Portugal. romana.santos@campus.ul.pt.
authors.forename: Romana
authors.initials: R
authors.lastname: Santos
mesh_terms: D000268:Adhesiveness; D000269:Adhesives / Q000737:chemistry; D017398:Alternative Splicing; D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000818:Animals; D015815:Cell Adhesion Molecules / Q000235:genetics* / Q000378:metabolism; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D040542:Mechanotransduction, Cellular / Q000235:genetics*; D000075983:Nectins; D009928:Organ Specificity; D047328:Paracentrotus / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D020033:Protein Isoforms / Q000235:genetics / Q000378:metabolism; D020543:Proteome / Q000235:genetics* / Q000378:metabolism; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D000269:Adhesives; D015815:Cell Adhesion Molecules; D018076:DNA, Complementary; D000075983:Nectins; D020033:Protein Isoforms; D020543:Proteome; D012333:RNA, Messenger; D011994:Recombinant Proteins
keywords: Marine adhesion; Nectin; Sea urchin; Substratum adhesive protein; Tube feet