The Korean Journal of Malacology (한국패류학회지)

The Malacological Society of Korea (한국패류학회)
권호 표지
DOI QR코드

DOI QR Code

Prismatic shell repairs by hemoctyes in the extrapallial fluid of the Pacific Oyster, Crassostrea gigas

  • Cho, Sang-Man (Department of Aquaculture and Aquatic Sciences, Kunsan National University) ;
  • Jeong, Woo-Geon (Department of Marine biology and Aquaculture & Institute of Marine Industrial Science, Gyeongsang National University)
  • Received : 2011.09.07
  • Accepted : 2011.09.26
  • Published : 2011.09.30
Download PDF
⟨ Previous Next ⟩

Abstract

To understand the role of hemocytes in the shell repair process, a hole was drilled in the right valves of the Pacific oyster, Crassostrea gigas, and the repair process was observed. Histological observations suggested that the exterior surface of the shell was repaired by aggregated hemocytes. The nuclei of the hemocytes were cleary stained in the regenerated shell while appearing fragmented after calcification at the $7^{th}$ day. Globular calcium granules were genegenerated from the hemocytic monolyer after 6 days of incubation which were morphologically and chemically identical with those from prismatic shell. Our finding suggested that the repaired prismatic shell was composed by aggregated hemocytes and that their endogenous calcium component might support the nucleation of calcium biomineralization during shell repair.

Keywords

References

  1. Cho, S.M., Lee, Y.M. and Jeong, W.G. (2011). Effect of Polycylclic Aromatic Hydrocarbon (PAH) on Shell Repair in the Pacific Oyster, Crassostrea gigas. The Korean Journal of Malacology, 27:35-42. https://doi.org/10.9710/kjm.2011.27.1.035
  2. Fleury, C., Marin, F., Marie, B., Luquet, G., Thomas, J., Josse, C., Serpentini, A. and Lebel, J.M. (2008) Shell repair process in the green ormer Haliotis turberculata: A histological and microstructural study. Tissue & Cell, 40(3):207-218. https://doi.org/10.1016/j.tice.2007.12.002
  3. Gotliv, B.A., Kessler, N., Sumeral, J.L., Morse, D.E., Tuross, N., Addadi, L. and Weiner, S. (2005) Asprich: A novel aspartic acid-rich protein family from the prismatic shell matrix of the bivalve Atrina rigida. Chembiochem., 6(2):304-314.
  4. Jodrey, L.H. (1953) Studies on shell formation III. Measurement of calcium deposition in shell and calcium turnover in mantle tissue using the mantle-shell preparation and $ Ca^{45}$. Biological Bulletin, 104:398-407. https://doi.org/10.2307/1538493
  5. Johnstone, M.B., Ellis, S. and Mount, A.S. (2008) Visualization of shell matrix proteins in hemocytes and tissue of the eastern oyster, Crassostrea virginica. Journal of Experimental Zoology, 310B:227-239.
  6. Kadar, E., Lobo-da-Cunha, A. and Azevedo, C. (2009) Mantle-to-shell $ CaCO_{3} $ transfer during shell repair at different hydrostatic pressures in the deep-sea vent mussel Bathymodiolus azoricus (Bivalvia: Mytilidae). Marine Biology, 156:959-967. https://doi.org/10.1007/s00227-009-1140-2
  7. Lowenstam, H.A. and Weiner, S. (1989) On biomineralization. Oxford University Press, Oxford, p. 336.
  8. Marin, F., Luquet, G., Marie, B. and Medakovic, D. (2008)Molluscan shell proteins: Primary structure, origin and evolution. Current Topics in Developmenal Biology, 80:209-276.
  9. Miyashita, T., Takagi, R., Okushima, M., Nakano, S., Miyamoto, H. and Nishikawa, E. (2000) Complementary DNA cloning and characterization of Pearlin, a new class of matrix protein in the nacreous layer of oyster pearls. Marine Biotechnology, 2:409-418.
  10. Mount, A.S., Wheeler, A.P., Paradkar, R.P. and Snider, D. (2004) Hemcoyte-mediated shell mineralization in the eastern oyster. Science, 304:297-300. https://doi.org/10.1126/science.1090506
  11. Simkiss, K. and Wilbur, K.M. (1989)Bomineralization, cell biology and mineral deposition. Academic Press, San Diego, p. 337.
  12. Thompson, J.B., Paloczi, G.T., Kindt, J.H., Michemfelder, M., Smith, B.L., Stucky, G., Morse, D.E. and Hansma, P.K. (2000) Direct observation of the transition from calcite to aragonite growth as induced by abalone shell proteins. Biophysical Journal, 79:3307-3312. https://doi.org/10.1016/S0006-3495(00)76562-3
  13. Wheeler, A.P. (1992) Mechanisms of Molluscan Shell Formation. In: Calcification in Biological systems. (ed by Bonucci), CRC Press, Boca Raton, pp. 179-216.
  14. Wilbur, K.M. and Jodrey, L.H. (1952)Studies on shell formation. I. Measurement of the rate of shell formation using $Ca^{45}$. Biological Bulletin, 103:269-276. https://doi.org/10.2307/1538451
  15. Wilbur, K.M. (1964) Shell formation and regeneration. In: Physiology of Mollusca Vol. 1. (ed by Willbur, K.M. and Yonge, C.M.), Academic Press. New York, pp. 243-282.
  16. Wilbur, K.M. and Bernhardt, A.M. (1984) Effects of amino acids, magnesium and molluscan extrapallial fluid on crystallization of calcium carbonate: In vitro experiments. Biological Bulletin, 166:251-259. https://doi.org/10.2307/1541446
  17. Zhang, C. and Zhang, R. (2006) Matrix proteins in the outer shells of mollusk. Marine Biotechnology, 8:572-586. https://doi.org/10.1007/s10126-005-6029-6

Cited by

  1. Comparative Study on Physicochemical Characteristics of Oyster Shells, Crassostrea gigas, Cultured in Various Waters in Korea vol.30, pp.2, 2014, https://doi.org/10.9710/kjm.2014.30.2.165
  2. vol.285, pp.1891, 2018, https://doi.org/10.1098/rspb.2018.1676
  3. vol.15, pp.145, 2018, https://doi.org/10.1098/rsif.2018.0299
  4. Recent Advances of Shell Matrix Proteins and Cellular Orchestration in Marine Molluscan Shell Biomineralization vol.6, pp.2296-7745, 2019, https://doi.org/10.3389/fmars.2019.00041
  5. Dominin and Segon Form Multiprotein Particles in the Plasma of Eastern Oysters ( Crassostrea virginica ) and Are Likely Involved in Shell Formation vol.10, pp.None, 2011, https://doi.org/10.3389/fphys.2019.00566
  6. Dilution of Seawater Affects the Ca 2 + Transport in the Outer Mantle Epithelium of Crassostrea gigas vol.11, pp.None, 2011, https://doi.org/10.3389/fphys.2020.00001
  7. Nacre morphology and chemical composition in Atlantic winged oyster Pteria colymbus (Röding, 1798) vol.9, pp.None, 2011, https://doi.org/10.7717/peerj.11527