First Insights into the Biochemistry of Tube Foot Adhesive from the Sea Urchin Paracentrotus lividus (Echinoidea, Echinodermata)
- 17 February 2009
- journal article
- Published by Springer Science and Business Media LLC in Marine Biotechnology
- Vol. 11 (6), 686-698
- https://doi.org/10.1007/s10126-009-9182-5
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.Keywords
This publication has 47 references indexed in Scilit:
- Underwater Adhesive of Marine Organisms as the Vital Link Between Biological Science and Material ScienceMarine Biotechnology, 2008
- Understanding Marine Mussel AdhesionMarine Biotechnology, 2007
- The Genome of the Sea Urchin Strongylocentrotus purpuratusScience, 2006
- Beyond the walls of the nucleus: the role of histones in cellular signaling and innate immunityThis paper is one of a selection of papers published in this Special Issue, entitled 27th International West Coast Chromatin and Chromosome Conference, and has undergone the Journal's usual peer review process.Biochemistry and Cell Biology, 2006
- Antifouling diketopiperazines produced by a deep-sea bacterium,Streptomyces fungicidicusBiofouling, 2006
- Adhesion of echinoderm tube feet to rough surfacesJournal Of Experimental Biology, 2005
- The tube cement of Phragmatopoma californica: a solid foamJournal Of Experimental Biology, 2004
- Characterization of the Adhesive from Cuvierian Tubules of the Sea Cucumber Holothuria forskali (Echinodermata, Holothuroidea)Marine Biotechnology, 2003
- Barnacle cement proteins: importance of disulfide bonds in their insolubilityJournal of Biological Chemistry, 2000
- Cement Proteins of the Acorn-Barnacle, Megabalanus rosaThe Biological Bulletin, 1996