scholarly journals The Inner-Shell Film: An Immediate Structure Participating in Pearl Oyster Shell Formation

ChemBioChem ◽  
2008 ◽  
Vol 9 (8) ◽  
pp. 1181-1181
Author(s):  
Zhenguang Yan ◽  
Zhuojun Ma ◽  
Guilan Zheng ◽  
Qiaoli Feng ◽  
Hongzhong Wang ◽  
...  
Keyword(s):  
Oyster Shell ◽  
Pearl Oyster ◽  
Shell Formation

The Inner-Shell Film: An Immediate Structure Participating in Pearl Oyster Shell Formation

ChemBioChem ◽  
2008 ◽  
Vol 9 (7) ◽  
pp. 1093-1099 ◽  
Author(s):  
Zhenguang Yan ◽  
Zhuojun Ma ◽  
Guilan Zheng ◽  
Qiaoli Feng ◽  
Hongzhong Wang ◽  
...  
Keyword(s):  
Oyster Shell ◽  
Pearl Oyster ◽  
Shell Formation

scholarly journals Molecular Cloning and Characterization of Full-Length cDNA of Calmodulin Gene from Pacific OysterCrassostrea gigas

2016 ◽  
Vol 2016 ◽  
pp. 1-7 ◽  
Author(s):  
Xing-Xia Li ◽  
Wen-Chao Yu ◽  
Zhong-Qiang Cai ◽  
Cheng He ◽  
Na Wei ◽  
...  
Keyword(s):  
Calcium Binding ◽  
Pacific Oyster ◽  
Pearl Oyster ◽  
Full Length ◽  
Pinctada Fucata ◽  
Whole Genome Sequence ◽  
Formation Mechanisms ◽  
Shell Formation ◽  
Full Length Cdna ◽  
Ef Hand

The shell of the pearl oyster (Pinctada fucata) mainly comprises aragonite whereas that of the Pacific oyster (Crassostrea gigas) is mainly calcite, thereby suggesting the different mechanisms of shell formation between above two mollusks. Calmodulin (CaM) is an important gene for regulating the uptake, transport, and secretion of calcium during the process of shell formation in pearl oyster. It is interesting to characterize the CaM in oysters, which could facilitate the understanding of the different shell formation mechanisms among mollusks. We cloned the full-length cDNA of Pacific oyster CaM (cgCaM) and found that the cgCaM ORF encoded a peptide of 113 amino acids containing three EF-hand calcium-binding domains, its expression level was highest in the mantle, hinting that the cgCaM gene is probably involved in shell formation of Pacific oyster, and the common ancestor of Gastropoda and Bivalvia may possess at least three CaM genes. We also found that the numbers of some EF hand family members in highly calcified species were higher than those in lowly calcified species and the numbers of these motifs in oyster genome were the highest among the mollusk species with whole genome sequence, further hinting the correlation between CaM and biomineralization.

The Akoya pearl oyster shell as an archival monitor of lead exposure

2006 ◽  
Vol 143 (1) ◽  
pp. 166-173 ◽  
Author(s):  
G.R. MacFarlane ◽  
S.J. Markich ◽  
K. Linz ◽  
S. Gifford ◽  
R.H. Dunstan ◽  
...  
Keyword(s):  
Lead Exposure ◽  
Oyster Shell ◽  
Pearl Oyster

scholarly journals Deep Sequencing of ESTs from Nacreous and Prismatic Layer Producing Tissues and a Screen for Novel Shell Formation-Related Genes in the Pearl Oyster

PLoS ONE ◽  
2011 ◽  
Vol 6 (6) ◽  
pp. e21238 ◽  
Author(s):  
Shigeharu Kinoshita ◽  
Ning Wang ◽  
Haruka Inoue ◽  
Kaoru Maeyama ◽  
Kikuhiko Okamoto ◽  
...  
Keyword(s):  
Deep Sequencing ◽  
Pearl Oyster ◽  
Shell Formation ◽  
Prismatic Layer

Crystallization of biogenic Ca-carbonate within organo-mineral micro-domains. Structure of the calcite prisms of the Pelecypod Pinctada margaritifera (Mollusca) at the submicron to nanometre ranges

2008 ◽  
Vol 72 (2) ◽  
pp. 617-626 ◽  
Author(s):  
A. Baronnet ◽  
J. P. Cuif ◽  
Y. Dauphin ◽  
B. Farre ◽  
J. Nouet
Keyword(s):  
Crystallization Front ◽  
Oyster Shell ◽  
Pearl Oyster ◽  
Pinctada Margaritifera ◽  
Force Microscopy ◽  
Atomic Force ◽  
Transmission Electron ◽  
Afm Analysis ◽  
Diffraction Patterns ◽  
Ca Carbonate

AbstractAtomic force microscopy (AFM) and transmission electron microscopy (TEM) were used to investigate the fine structure of the calcite prisms from the pearl-oyster shell Pinctada margaritifera. The AFM analysis shows that the prisms are made of densely packed circular micro-domains (in the 0.1 μm range) surrounded by a dense cortex. The TEM images and diffraction patterns allow the internal structure of the micro-domains to be described. Each of them is enriched in Ca-carbonate. Hosted in distinct regions of each prism, some are fully amorphous, and some others fully crystallized as subunits of a large calcite single crystal. At the border separating the two regions, micro-domains display a crystallized core and an amorphous rim. Such a border probably marks out an arrested crystallization front having propagated through a previously bio-controlled architecture of the piling of amorphous micro-domains. Compared to recent data concerning the stepping mode of growth of the calcite prisms and the resulting layered organization at the μm-scale, these results give unexpected views regarding the modalities of biocrystallization.

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