First Insights into the Biochemistry of Tube Foot Adhesive from the Sea Urchin Paracentrotus lividus (Echinoidea, Echinodermata) |
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Authors: | R Santos G da Costa C Franco P Gomes-Alves P Flammang A V Coelho |
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Institution: | 1. Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal 2. Departamento de Genética, Instituto Nacional de Saúde Dr. Ricardo Jorge, Lisbon, Portugal 3. Laboratoire de Biologie Marine, Université de Mons-Hainaut, Mons, Belgium 4. Departamento de Química, Universidade de évora, évora, Portugal
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Abstract: | Sea urchins are common inhabitants of wave-swept shores. To withstand the action of waves, they rely on highly specialized
independent adhesive organs, the adoral tube feet. The latter are extremely well-designed for temporary adhesion being composed
by two functional subunits: (1) an apical disc that produces an adhesive secretion to fasten the sea urchin to the substratum,
as well as a deadhesive secretion to allow the animal to move and (2) a stem that bears the tensions placed on the animal
by hydrodynamism. Despite their technological potential for the development of new biomimetic underwater adhesives, very little
is known about the biochemical composition of sea urchin adhesives. A characterization of sea urchin adhesives is presented
using footprints. The latter contain inorganic residues (45.5%), proteins (6.4%), neutral sugars (1.2%), and lipids (2.5%).
Moreover, the amino acid composition of the soluble protein fraction revealed a bias toward six amino acids: glycine, alanine,
valine, serine, threonine, and asparagine/aspartic acid, which comprise 56.8% of the total residues. In addition, it also
presents higher levels of proline (6.8%) and half-cystine (2.6%) than average eukaryotic proteins. Footprint insolubility
was partially overcome using strong denaturing and reducing buffers, enabling the visualization of 13 proteins by sodium dodecyl
sulfate polyacrylamide gel electrophoresis. The conjugation of mass spectrometry with homology–database search allowed the
identification of six proteins: alpha and beta tubulin, actin, and histones H2B, H3, H2A, and H4, whose location and function
in the adhesive are discussed but require further investigation. For the remaining unidentified proteins, five de novo-generated
peptide sequences were found that were not present in the available protein databases, suggesting that they might be novel
or modified proteins. |
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