Proteomic analysis of the organic matrix of the abalone Haliotis asininacalcified shell

biomed - Jackson , Marie Benjamin , Marie Arul , Dubost Lionel , Degnan , Milet Christian , Marin , Marin Frédéric

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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.

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Publié par	biomed
Publié le	01 janvier 2010
Nombre de lectures	311
Langue	English
Poids de l'ouvrage	3 Mo

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Marieet al.Proteome Science2010,8:54 http://www.proteomesci.com/content/8/1/54

R E S E A R C HOpen Access Proteomic analysis of the organic matrix of the abaloneHaliotis asininacalcified shell 1* 23 24 5 Benjamin Marie, Arul Marie , Daniel J Jackson , Lionel Dubost , Bernard M Degnan , Christian Milet , 1* Frédéric Marin

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.

Background The calcified molluscan shell is an excellent model with which to study the process of biomineral formation. The wide morphological diversity of shellbearing molluscs (bivalves, gastropods, cephalopods, monoplacophorans and scaphopods) also extends to a tremendous diversity of shell microtextures. Despite this diversity, molluscan shells are produced by an evolutionarily homologous structure known as the mantle. The polymorph of CaCO3(primarily aragonite or calcite), along with all other nanoscale features of the biomineral, are thought to be determined and regulated by an extracellular‘cell free’matrix that is secreted by the mantle. This matrix is incorporated into and surrounds nascent CaCO3crys tals during shell growth. Even though it constitutes only a small part of the total shell weight (15%), this matrix is clearly essential for initiating biomineral formation

* Correspondence: benjamin.marie@ubourgogne.fr; frederic.marin@u bourgogne.fr 1 UMR 5561 CNRS, Biogéosciences, Université de Bourgogne, 21000 Dijon, France Full list of author information is available at the end of the article

and imparting critical physical properties to the shell such as fracture resistance. The biochemical characteris tics of the matrix, usually purified and studied following decalcification of the shell, indicate that it is comprised of a heterogenous set of macromolecules including chitin, hydrophobic‘framework’proteins and soluble proteins and glycoproteins [1]. However, relatively few matrix proteins have been identified and characterised from abalone shells, perhaps the beststudied gastropod biomineralisation system. To date these include Lustrin A [2], Perlucin [3], Perlustrin [4], AP7, AP24 [5], Perl wapin [6] and Perlinhibin [7]. Jackson et al. [810] employed a highthroughput EST sequencing strategies in order to identify gene products that may be directly involved in shell formation of the tropical abaloneHaliotis asinina. Hundreds of concep tually translated proteins putatively related to shell calci fication were identified using this approach, however none of these have been directly characterized from the shell. Furthermore, this approach cannot accurately dis criminate between proteins required for nonmineralising functions, and those directly involved in shell formation.

© 2010 Marie et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Proteomic analysis of the organic matrix of the abalone Haliotis asininacalcified shell

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