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

Marie, Benjamin, Marie, Arul, Jackson, Daniel J., Dubost, Lionel, Degnan, Bernard, Milet, Christian and Marin, Frédéric (2010) Proteomic analysis of the organic matrix of the abalone Haliotis asinina calcified shell. Proteome Science, 8 . doi:10.1186/1477-5956-8-54

Author Marie, Benjamin
Marie, Arul
Jackson, Daniel J.
Dubost, Lionel
Degnan, Bernard
Milet, Christian
Marin, Frédéric
Title Proteomic analysis of the organic matrix of the abalone Haliotis asinina calcified shell
Journal name Proteome Science   Check publisher's open access policy
ISSN 1477-5956
Publication date 2010-11-04
Sub-type Article (original research)
DOI 10.1186/1477-5956-8-54
Open Access Status DOI
Volume 8
Total pages 11
Editor Martin Latterich
Fred E. Indig
Place of publication London, United Kingdom
Publisher BioMed Central
Collection year 2011
Language eng
Formatted 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.
© 2010 Marie et al; licensee BioMed Central Ltd.

Keyword Molluscan shell
Calcifying matrix
Haliotis asinina
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2011 Collection
School of Biological Sciences Publications
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Created: Fri, 26 Nov 2010, 17:02:08 EST by Gail Walter on behalf of School of Biological Sciences