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Barnacle cement: a polymerization model based on evolutionary concepts.

Publication ,  Journal Article
Dickinson, GH; Vega, IE; Wahl, KJ; Orihuela, B; Beyley, V; Rodriguez, EN; Everett, RK; Bonaventura, J; Rittschof, D
Published in: The Journal of experimental biology
November 2009

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.

Duke Scholars

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Published In

The Journal of experimental biology

DOI

EISSN

1477-9145

ISSN

0022-0949

Publication Date

November 2009

Volume

212

Issue

Pt 21

Start / End Page

3499 / 3510

Related Subject Headings

  • Trypsin
  • Transglutaminases
  • Thoracica
  • Tandem Mass Spectrometry
  • Proteins
  • Polymers
  • Physiology
  • Molecular Sequence Data
  • Models, Biological
  • Microscopy, Atomic Force
 

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Dickinson, G. H., Vega, I. E., Wahl, K. J., Orihuela, B., Beyley, V., Rodriguez, E. N., … Rittschof, D. (2009). Barnacle cement: a polymerization model based on evolutionary concepts. The Journal of Experimental Biology, 212(Pt 21), 3499–3510. https://doi.org/10.1242/jeb.029884
Dickinson, Gary H., Irving E. Vega, Kathryn J. Wahl, Beatriz Orihuela, Veronica Beyley, Eva N. Rodriguez, Richard K. Everett, Joseph Bonaventura, and Daniel Rittschof. “Barnacle cement: a polymerization model based on evolutionary concepts.The Journal of Experimental Biology 212, no. Pt 21 (November 2009): 3499–3510. https://doi.org/10.1242/jeb.029884.
Dickinson GH, Vega IE, Wahl KJ, Orihuela B, Beyley V, Rodriguez EN, et al. Barnacle cement: a polymerization model based on evolutionary concepts. The Journal of experimental biology. 2009 Nov;212(Pt 21):3499–510.
Dickinson, Gary H., et al. “Barnacle cement: a polymerization model based on evolutionary concepts.The Journal of Experimental Biology, vol. 212, no. Pt 21, Nov. 2009, pp. 3499–510. Epmc, doi:10.1242/jeb.029884.
Dickinson GH, Vega IE, Wahl KJ, Orihuela B, Beyley V, Rodriguez EN, Everett RK, Bonaventura J, Rittschof D. Barnacle cement: a polymerization model based on evolutionary concepts. The Journal of experimental biology. 2009 Nov;212(Pt 21):3499–3510.
Journal cover image

Published In

The Journal of experimental biology

DOI

EISSN

1477-9145

ISSN

0022-0949

Publication Date

November 2009

Volume

212

Issue

Pt 21

Start / End Page

3499 / 3510

Related Subject Headings

  • Trypsin
  • Transglutaminases
  • Thoracica
  • Tandem Mass Spectrometry
  • Proteins
  • Polymers
  • Physiology
  • Molecular Sequence Data
  • Models, Biological
  • Microscopy, Atomic Force