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Proteomic analysis of the organic matrix of the abalone Haliotis asinina calcified shell

Identifieur interne : 006E97 ( Main/Exploration ); précédent : 006E96; suivant : 006E98

Proteomic analysis of the organic matrix of the abalone Haliotis asinina calcified shell

Auteurs : Benjamin Marie [France] ; Arul Marie [France] ; Daniel J. Jackson [Allemagne] ; Lionel Dubost [France] ; Bernard M. Degnan [Australie] ; Christian Milet [France] ; Frédéric Marin [France]

Source :

RBID : PMC:2989941

Abstract

Background

The formation of the molluscan shell is regulated to a large extent by a matrix of extracellular macromolecules that are secreted by the shell forming tissue, the mantle. This so called "calcifying matrix" is a complex mixture of proteins and glycoproteins that is assembled and occluded within the mineral phase during the calcification process. While the importance of the calcifying matrix to shell formation has long been appreciated, most of its protein components remain uncharacterised.

Results

Recent expressed sequence tag (EST) investigations of the mantle tissue from the tropical abalone (Haliotis asinina) provide an opportunity to further characterise the proteins in the shell by a proteomic approach. In this study, we have identified a total of 14 proteins from distinct calcified layers of the shell. Only two of these proteins have been previously characterised from abalone shells. Among the novel proteins are several glutamine- and methionine-rich motifs and hydrophobic glycine-, alanine- and acidic aspartate-rich domains. In addition, two of the new proteins contained Kunitz-like and WAP (whey acidic protein) protease inhibitor domains.

Conclusion

This is one of the first comprehensive proteomic study of a molluscan shell, and should provide a platform for further characterization of matrix protein functions and interactions.


Url:
DOI: 10.1186/1477-5956-8-54
PubMed: 21050442
PubMed Central: 2989941


Affiliations:


Links toward previous steps (curation, corpus...)


Le document en format XML

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<title>Background</title>
<p>The formation of the molluscan shell is regulated to a large extent by a matrix of extracellular macromolecules that are secreted by the shell forming tissue, the mantle. This so called "calcifying matrix" is a complex mixture of proteins and glycoproteins that is assembled and occluded within the mineral phase during the calcification process. While the importance of the calcifying matrix to shell formation has long been appreciated, most of its protein components remain uncharacterised.</p>
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<sec>
<title>Results</title>
<p>Recent expressed sequence tag (EST) investigations of the mantle tissue from the tropical abalone (
<italic>Haliotis asinina</italic>
) provide an opportunity to further characterise the proteins in the shell by a proteomic approach. In this study, we have identified a total of 14 proteins from distinct calcified layers of the shell. Only two of these proteins have been previously characterised from abalone shells. Among the novel proteins are several glutamine- and methionine-rich motifs and hydrophobic glycine-, alanine- and acidic aspartate-rich domains. In addition, two of the new proteins contained Kunitz-like and WAP (whey acidic protein) protease inhibitor domains.</p>
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<p>This is one of the first comprehensive proteomic study of a molluscan shell, and should provide a platform for further characterization of matrix protein functions and interactions.</p>
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