Abstract
The adductor muscle scar (AMS) is the fixation point of adductor muscle to the shell. It is an important organicinorganic interface and stress distribution area. Despite recent advances, our understanding of the structure and composition of the AMS remain limited. Here, we report study on the AMS of three bivalves: Mytilus coruscus, Chlamys farreri and Ruditapes philippinarum. Results showed that there were significant differences among their AMS structures. Both M. coruscus and C. farreri were found to have a columnar layer above the nacreous platelet shell structure at the AMS and this layer was more organized in M. coruscus. There was no distinguishable twolayer structure in R. philippinarum. Atomic force microscopy (AFM) and Fourier transform infrared spectroscopy (FT-IR) results showed that the AMS was much smoother than the nacreous inner shell in all the three species and the AMS had minor different compositions from the nacreous shell layer. SDS-PAGE (sodium dodecyl-sulfate polyacrylamide gel electophoresis) study of the proteins isolated from the interface indicated that there was a 70 kDa protein which seemed to be specifically located to the highly organized columnar AMS structure in Mytilus coruscus. Further analysis of this protein showed it contained high level of Asx (Asp+Asn), Glx (Glu+Gln) and Gly. The special structure and composition of the AMS might play important roles in the stability, adhesion and function at this stress distribution site.
Similar content being viewed by others
References
Addadi L, Joester D, Nudelman F, et al. 2006. Mollusk shell formation: a source of new concepts for understanding biomineralization processes. Chemistry—A European Journal, 12(4): 980–987
Andersen F A, Brecevic L. 1991. Infrared spectra of amorphous and crystalline calcium carbonate. Acta Chemica Scandinavica, 45: 1018–1024
Balmain J, Hannoyer B, Lopez E. 1999. Fourier transform infrared spectroscopy (FTIR) and X-ray diffraction analyses of mineral and organic matrix during heating of mother of pearl (nacre) from the shell of the mollusc Pinctada maxima. Journal of Biomedical Materials Research, 48(5): 749–754
Belcher A M, Wu X H, Christensen R J, et al. 1996. Control of crystal phase switching and orientation by soluble mollusc-shell proteins. Nature, 381(6577): 56–58
Checa A. 2000. A new model for periostracum and shell formation in Unionidae (Bivalvia, Mollusca). Tissue and Cell, 32(5): 405–416
Cölfen H. 2010. Biomineralization: a crystal-clear view. Nature Materials, 9(12): 960–961
Currey J D. 1977. Mechanical properties of mother of pearl in tension. Proceedings of the Royal Society B: Biological Sciences, 196(1125): 443–463
Currey J D. 1999. The design of mineralised hard tissues for their mechanical functions. Journal of Experimental Biology, 202(23): 3285–3294
Feng Q, Li H B, Pu G, et al. 2000. Crystallographic alignment of calcite prisms in the oblique prismatic layer of Mytilus edulis shell. Journal of Materials Science, 35(13): 3337–3340
Furuhashi T, Schwarzinger C, Miksik I, et al. 2009. Molluscan shell evolution with review of shell calcification hypothesis. Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 154(3): 351–371
Kennedy V S, Newell R I, Eble A F. 1996. The Eastern Oyster: Crassostrea Virginica. Maryland: University of Maryland Sea Grant College
Kong Y, Jing G, Yan Z, et al. 2009). Cloning and characterization of Prisilkin–39, a novel matrix protein serving a dual role in the prismatic layer formation from the oyster Pinctada fucata. Journal of Biological Chemistry, 284(16): 10841–10854
Lee S W, Jang Y N, Kim J C. 2011. Characteristics of the Aragonitic layer in adult oyster shells, Crassostrea gigas: structural study of myostracum including the adductor muscle scar. Evidence- Based Complementary and Alternative Medicine, 2011: 742963
Lin A, Meyers M A. 2005. Growth and structure in abalone shell. Materials Science and Engineering: A, 390(1–2): 27–41
Lippmann F. 1973. Sedimentary Carbonate Minerals. Berlin Heidelberg: Springer
Lowenstam H A, Weiner S. 1989. On Biomineralization. Oxford: Oxford University Press
Marie B, Le Roy N, Zanella-Cléon I, et al. 2011. Molecular evolution of mollusc shell proteins: insights from proteomic analysis of the edible mussel Mytilus. Journal of Molecular Evolution, 72(5–6): 531–546
Mount A S, Wheeler A, Paradkar R P, et al. 2004. Hemocyte-mediated shell mineralization in the eastern oyster. Science, 304(5668): 297–300
Song Y, Lu Y, Ding H, et al. 2013. Structural characteristics at the adductor muscle and shell interface in Mussel. Applied Biochemistry and Biotechnology, 171(5): 1203–1211
Spann N, Harper E M, Aldridge D C. 2010. The unusual mineral vaterite in shells of the freshwater bivalve Corbicula fluminea from the UK. Naturwissenschaften, 97(8): 743–751
Suzuki M, Iwashima A, Tsutsui N, et al. 2011. Identification and characterisation of a calcium carbonate-binding protein, blue mussel shell protein (BMSP), from the nacreous layer. ChemBio-Chem, 12(16): 2478–2487
Suzuki M, Saruwatari K, Kogure T, et al. 2009. An acidic matrix protein, Pif, is a key macromolecule for nacre formation. Science, 325(5946): 1388–1390
Takeuchi T, Endo K. 2006. Biphasic and dually coordinated expression of the genes encoding major shell matrix proteins in the pearl oyster Pinctada fucata. Marine Biotechnology, 8(1): 52–61
Vagenas N V, Gatsouli A, Kontoyannis C G. 2003. Quantitative analysis of synthetic calcium carbonate polymorphs using FT-IR spectroscopy. Talanta, 59(4): 831–836
Wainwright S A. 1969. Stress and design in bivalved mollusc shell. Nature, 224(5221): 777–779
Wheeler A P, Rusenko K W, Swift D M, et al. 1988. Regulation of in vitro and in vivo CaCO3 crystallization by fractions of oyster shell organic matrix. Marine Biology, 98(1): 71–80
Yoon G L, Kim B T, Kim B O, et al. 2003. Chemical–mechanical characteristics of crushed oyster-shell. Waste Management, 23(9): 825–834
Author information
Authors and Affiliations
Corresponding author
Additional information
Foundation item: The Basic Scientific Fund for National Public Research Institutes of China under contract No. 2011T10; the National Natural Science Foundation of China—Shandong Joint Grant U1406402-5; Qingdao Talents Program under contract No. 13-CX-20; the National Natural Science Foundation of China under contract Nos 31100567, 41176061, 41521064, 41306074 and 31160098; the Taishan Scholar Program.
Rights and permissions
About this article
Cite this article
Zhu, Y., Sun, C., Song, Y. et al. The study of the adductor muscle-shell interface structure in three Mollusc species. Acta Oceanol. Sin. 35, 57–64 (2016). https://doi.org/10.1007/s13131-016-0878-x
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s13131-016-0878-x