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dc.contributor.advisor Rittschof, Daniel en_US
dc.contributor.author Dickinson, GH
dc.contributor.author Vega, IE
dc.contributor.author Wahl, KJ
dc.contributor.author Orihuela, B
dc.contributor.author Beyley, V
dc.contributor.author Rodriguez, EN
dc.contributor.author Everett, RK
dc.contributor.author Bonaventura, J
dc.contributor.author Rittschof, D
dc.coverage.spatial England
dc.date.accessioned 2008-08-01T12:53:15Z
dc.date.issued 2009-11
dc.identifier http://www.ncbi.nlm.nih.gov/pubmed/19837892
dc.identifier 212/21/3499
dc.identifier.citation J Exp Biol, 2009, 212 (Pt 21), pp. 3499 - 3510
dc.identifier.uri http://hdl.handle.net/10161/653
dc.description Dissertation en_US
dc.description.abstract Enzymes and biochemical mechanisms essential to survival are under extreme selective pressure and are highly conserved through evolutionary time. We applied this evolutionary concept to barnacle cement polymerization, a process critical to barnacle fitness that involves aggregation and cross-linking of proteins. The biochemical mechanisms of cement polymerization remain largely unknown. We hypothesized that this process is biochemically similar to blood clotting, a critical physiological response that is also based on aggregation and cross-linking of proteins. Like key elements of vertebrate and invertebrate blood clotting, barnacle cement polymerization was shown to involve proteolytic activation of enzymes and structural precursors, transglutaminase cross-linking and assembly of fibrous proteins. Proteolytic activation of structural proteins maximizes the potential for bonding interactions with other proteins and with the surface. Transglutaminase cross-linking reinforces cement integrity. Remarkably, epitopes and sequences homologous to bovine trypsin and human transglutaminase were identified in barnacle cement with tandem mass spectrometry and/or western blotting. Akin to blood clotting, the peptides generated during proteolytic activation functioned as signal molecules, linking a molecular level event (protein aggregation) to a behavioral response (barnacle larval settlement). Our results draw attention to a highly conserved protein polymerization mechanism and shed light on a long-standing biochemical puzzle. We suggest that barnacle cement polymerization is a specialized form of wound healing. The polymerization mechanism common between barnacle cement and blood may be a theme for many marine animal glues.
dc.format.extent 3499 - 3510
dc.format.mimetype application/pdf
dc.language eng
dc.language.iso en_US
dc.relation.ispartof J Exp Biol
dc.relation.isversionof 10.1242/jeb.029884
dc.subject Amino Acid Sequence
dc.subject Animals
dc.subject Biological Evolution
dc.subject Calcium
dc.subject Cattle
dc.subject Humans
dc.subject Microscopy, Atomic Force
dc.subject Models, Biological
dc.subject Molecular Sequence Data
dc.subject Polymers
dc.subject Proteins
dc.subject Tandem Mass Spectrometry
dc.subject Thoracica
dc.subject Transglutaminases
dc.subject Trypsin
dc.title Barnacle cement: a polymerization model based on evolutionary concepts.
dc.type Journal Article
dc.department Ecology en_US
duke.embargo.months 12 en_US
dc.date.accessible 2009-08-02T05:00:04Z
pubs.author-url http://www.ncbi.nlm.nih.gov/pubmed/19837892
pubs.issue Pt 21
pubs.organisational-group /Duke
pubs.organisational-group /Duke/Institutes and Provost's Academic Units
pubs.organisational-group /Duke/Institutes and Provost's Academic Units/Initiatives
pubs.organisational-group /Duke/Institutes and Provost's Academic Units/Initiatives/Duke Science & Society
pubs.organisational-group /Duke/Nicholas School of the Environment
pubs.organisational-group /Duke/Nicholas School of the Environment/Marine Science and Conservation
pubs.organisational-group /Duke/Trinity College of Arts & Sciences
pubs.organisational-group /Duke/Trinity College of Arts & Sciences/Biology
pubs.publication-status Published
pubs.volume 212
dc.identifier.eissn 1477-9145

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