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The structure of mollusc larval shells formed in the presence of the chitin synthase inhibitor Nikkomycin Z

BACKGROUND: Chitin self-assembly provides a dynamic extracellular biomineralization interface. The insoluble matrix of larval shells of the marine bivalve mollusc Mytilus galloprovincialis consists of chitinous material that is distributed and structured in relation to characteristic shell features....

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Detalles Bibliográficos
Autores principales: Schönitzer, Veronika, Weiss, Ingrid M
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2007
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2241824/
https://www.ncbi.nlm.nih.gov/pubmed/17986326
http://dx.doi.org/10.1186/1472-6807-7-71
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author Schönitzer, Veronika
Weiss, Ingrid M
author_facet Schönitzer, Veronika
Weiss, Ingrid M
author_sort Schönitzer, Veronika
collection PubMed
description BACKGROUND: Chitin self-assembly provides a dynamic extracellular biomineralization interface. The insoluble matrix of larval shells of the marine bivalve mollusc Mytilus galloprovincialis consists of chitinous material that is distributed and structured in relation to characteristic shell features. Mollusc shell chitin is synthesized via a complex transmembrane chitin synthase with an intracellular myosin motor domain. RESULTS: Enzymatic mollusc chitin synthesis was investigated in vivo by using the small-molecule drug NikkomycinZ, a structural analogue to the sugar donor substrate UDP-N-acetyl-D-glucosamine (UDP-GlcNAc). The impact on mollusc shell formation was analyzed by binocular microscopy, polarized light video microscopy in vivo, and scanning electron microscopy data obtained from shell material formed in the presence of NikkomycinZ. The partial inhibition of chitin synthesis in vivo during larval development by NikkomycinZ (5 μM – 10 μM) dramatically alters the structure and thus the functionality of the larval shell at various growth fronts, such as the bivalve hinge and the shell's edges. CONCLUSION: Provided that NikkomycinZ mainly affects chitin synthesis in molluscs, the presented data suggest that the mollusc chitin synthase fulfils an important enzymatic role in the coordinated formation of larval bivalve shells. It can be speculated that chitin synthesis bears the potential to contribute via signal transduction pathways to the implementation of hierarchical patterns into chitin mineral-composites such as prismatic, nacre, and crossed-lamellar shell types.
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spelling pubmed-22418242008-02-14 The structure of mollusc larval shells formed in the presence of the chitin synthase inhibitor Nikkomycin Z Schönitzer, Veronika Weiss, Ingrid M BMC Struct Biol Research Article BACKGROUND: Chitin self-assembly provides a dynamic extracellular biomineralization interface. The insoluble matrix of larval shells of the marine bivalve mollusc Mytilus galloprovincialis consists of chitinous material that is distributed and structured in relation to characteristic shell features. Mollusc shell chitin is synthesized via a complex transmembrane chitin synthase with an intracellular myosin motor domain. RESULTS: Enzymatic mollusc chitin synthesis was investigated in vivo by using the small-molecule drug NikkomycinZ, a structural analogue to the sugar donor substrate UDP-N-acetyl-D-glucosamine (UDP-GlcNAc). The impact on mollusc shell formation was analyzed by binocular microscopy, polarized light video microscopy in vivo, and scanning electron microscopy data obtained from shell material formed in the presence of NikkomycinZ. The partial inhibition of chitin synthesis in vivo during larval development by NikkomycinZ (5 μM – 10 μM) dramatically alters the structure and thus the functionality of the larval shell at various growth fronts, such as the bivalve hinge and the shell's edges. CONCLUSION: Provided that NikkomycinZ mainly affects chitin synthesis in molluscs, the presented data suggest that the mollusc chitin synthase fulfils an important enzymatic role in the coordinated formation of larval bivalve shells. It can be speculated that chitin synthesis bears the potential to contribute via signal transduction pathways to the implementation of hierarchical patterns into chitin mineral-composites such as prismatic, nacre, and crossed-lamellar shell types. BioMed Central 2007-11-06 /pmc/articles/PMC2241824/ /pubmed/17986326 http://dx.doi.org/10.1186/1472-6807-7-71 Text en Copyright © 2007 Schönitzer and Weiss; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 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.
spellingShingle Research Article
Schönitzer, Veronika
Weiss, Ingrid M
The structure of mollusc larval shells formed in the presence of the chitin synthase inhibitor Nikkomycin Z
title The structure of mollusc larval shells formed in the presence of the chitin synthase inhibitor Nikkomycin Z
title_full The structure of mollusc larval shells formed in the presence of the chitin synthase inhibitor Nikkomycin Z
title_fullStr The structure of mollusc larval shells formed in the presence of the chitin synthase inhibitor Nikkomycin Z
title_full_unstemmed The structure of mollusc larval shells formed in the presence of the chitin synthase inhibitor Nikkomycin Z
title_short The structure of mollusc larval shells formed in the presence of the chitin synthase inhibitor Nikkomycin Z
title_sort structure of mollusc larval shells formed in the presence of the chitin synthase inhibitor nikkomycin z
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2241824/
https://www.ncbi.nlm.nih.gov/pubmed/17986326
http://dx.doi.org/10.1186/1472-6807-7-71
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