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      Organic membranes determine the pattern of the columnar prismatic layer of mollusc shells

      , , ,
      Proceedings of the Royal Society B: Biological Sciences
      The Royal Society

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          Abstract

          <p class="first" id="d5899067e229">The degree to which biological control is exercised compared to physical control of the organization of biogenic materials is a central theme in biomineralization. We show that the outlines of biogenic calcite domains with organic membranes are always of simple geometries, while without they are much more complex. Moreover, the mineral prisms enclosed within the organic membranes are frequently polycrystalline. In the prismatic layer of the mollusc shell, organic membranes display a dynamics in accordance with the von Neumann–Mullins and Lewis Laws for two-dimensional foam, emulsion and grain growth. Taken together with the facts that we found instances in which the crystals do not obey such laws, and that the same organic membrane pattern can be found even without the mineral infilling, our work indicates that it is the membranes, not the mineral prisms, that control the pattern, and the mineral enclosed within the organic membranes passively adjusts to the dynamics dictated by the latter. </p>

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          Most cited references29

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          An Overview of Biomineralization Processes and the Problem of the Vital Effect

          L Weiner (2003)
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            Control of crystal phase switching and orientation by soluble mollusc-shell proteins

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              Molluscan shell proteins: primary structure, origin, and evolution.

              In the last few years, the field of molluscan biomineralization has known a tremendous mutation, regarding fundamental concepts on biomineralization regulation as well as regarding the methods of investigation. The most recent advances deal more particularly with the structure of shell biominerals at nanoscale and the identification of an increasing number of shell matrix protein components. Although the matrix is quantitatively a minor constituent in the shell of mollusks (less than 5% w/w), it is, however, the major component that controls different aspects of the shell formation processes: synthesis of transient amorphous minerals and evolution to crystalline phases, choice of the calcium carbonate polymorph (calcite vs aragonite), organization of crystallites in complex shell textures (microstructures). Until recently, the classical paradigm in molluscan shell biomineralization was to consider that the control of shell synthesis was performed primarily by two antagonistic mechanisms: crystal nucleation and growth inhibition. New concepts and emerging models try now to translate a more complex reality, which is remarkably illustrated by the wide variety of shell proteins, characterized since the mid-1990s, and described in this chapter. These proteins cover a broad spectrum of pI, from very acidic to very basic. The primary structure of a number of them is composed of different modules, suggesting that these proteins are multifunctional. Some of them exhibit enzymatic activities. Others may be involved in cell signaling. The oldness of shell proteins is discussed, in relation with the Cambrian appearance of the mollusks as a mineralizing phylum and with the Phanerozoic evolution of this group. Nowadays, the extracellular calcifying shell matrix appears as a whole integrated system, which regulates protein-mineral and protein-protein interactions as well as feedback interactions between the biominerals and the calcifying epithelium that synthesized them. Consequently, the molluscan shell matrix may be a source of bioactive molecules that would offer interesting perspectives in biomaterials and biomedical fields.
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                Author and article information

                Journal
                Proceedings of the Royal Society B: Biological Sciences
                Proc. R. Soc. B
                The Royal Society
                0962-8452
                1471-2954
                May 04 2016
                May 11 2016
                May 04 2016
                May 11 2016
                : 283
                : 1830
                : 20160032
                Article
                10.1098/rspb.2016.0032
                4874705
                27147096
                1c186a93-9dcf-40ea-b1d2-6812a49906b7
                © 2016
                History

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