Proteomics Analysis of the Nacre Soluble and Insoluble Proteins from the Oyster Pinctada margaritifera |
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Authors: | Laurent Bédouet Arul Marie Lionel Dubost Jean Péduzzi Denis Duplat Sophie Berland Marion Puisségur Hélène Boulzaguet Marthe Rousseau Christian Milet Evelyne Lopez |
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Institution: | (1) Département des Milieux et Peuplements Aquatiques, UMR 5178, CNRS-MNHN Biologie des Organismes Marins et Ecosystèmes, ERT Valorisation de Molécules Bioactives d’Origine Marine, Muséum National d’Histoire Naturelle, Paris, F-75231, France;(2) Plate forme de spectrométrie de masse et de protéomique, Département RDDM, Muséum National d’Histoire Naturelle, Paris, F-75231, France;(3) Laboratoire de Chimie et Biochimie des Substances Naturelles, UMR 5154 CNRS, USM 502, Muséum National d’Histoire Naturelle, Paris, F-75231, France |
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Abstract: | Shell nacre is laid upon an organic cell-free matrix, part of which, paradoxically, is water soluble and displays biological
activities. Proteins in the native shell also constitute an insoluble network and offer a model for studying supramolecular
organization as a means of self-ordering. Consequently, difficulties are encountered in extraction and purification strategies
for protein characterization. In this work, water-soluble proteins and the insoluble conhiolin residue of the nacre of Pinctada margaritifera matrix were analyzed via a proteomics approach. Two sequences homologous to nacre matrix proteins of other Pinctada species were identified in the water-soluble extract. One of them is known as a fundamental component of the insoluble organic
matrix of nacre. In the conchiolin, the insoluble residue, four homologs of Pinctada nacre matrix proteins were found. Two of them were the same as the molecules characterized in the water-soluble extract.
Results established that soluble and insoluble proteins of the nacre organic matrix share constitutive material. Surprisingly,
a peptide in the conchiolin residue was found homologous to a prismatic matrix protein of Pinctada fucata, suggesting that prismatic and nacre matrices may share common proteins. The insoluble properties of shell matrix proteins
appear to arise from structural organization via multimerization. The oxidative activity, found in the water-soluble fraction
of the nacre matrix, is proposed as a leading process in the transformation of transient soluble proteins into the insoluble
network of conchiolin during nacre growth. |
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Keywords: | conchiolin MSI31 MSI60 MASCOT N14 nacre (mother of pearl) nacrein oxidation Pinctada proteomics |
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