Proteomic analysis of the organic matrix of the abalone Haliotis asinina calcified shellReportar como inadecuado

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Proteome Science

, 8:54

First Online: 04 November 2010Received: 23 August 2010Accepted: 04 November 2010


BackgroundThe 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.

ResultsRecent 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.

ConclusionThis 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.

AbbreviationsAIMacid-insoluble matrix

ASMacid-soluble matrix

SEMscanning electron microscopy

WAPwhey acidic protein

Electronic supplementary materialThe online version of this article doi:10.1186-1477-5956-8-54 contains supplementary material, which is available to authorized users.

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Autor: Benjamin Marie - Arul Marie - Daniel J Jackson - Lionel Dubost - Bernard M Degnan - Christian Milet - Frédéric Marin


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