Cloning, Characterization and Expression Analysis of Calcium Channel β Subunit from Pearl Oyster(Pinctada fucata)(GENETICS, MOLECULAR BIOLOGY, AND GENE ENGINEERING)

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The absorption, transport and localization of calcium underlie the basis of biomineralization, and Ca^<2+> entry into epithelial cell is the primary step in shell formation. However, the related mechanism of Ca^<2+> transport is poorly documented at the gene or protein level. L-type voltage-de- pendent calcium channels may be involved in calcium transport for biomineralization in some marine invertebrates. In this study, a full-length cDNA of a voltage-dependent calcium channel p subunit from Pinctada fucata(PCaβ) was cloned, and its amino acid sequence was deduced. PCaβ shared 51%-67% apparently sequence identity with voltage-dependent calcium channel β subunits from other species. However, PCap was much shorter than other voltage-dependent calcium channel β subunits particularly at the carboxyl terminus, indicating that it is likely a truncated β subunit isoform. Semi-quantitative RT-PCR analysis showed that PCaβ was expressed in all the tested tissues and that it had a higher expression level in the gill tissue and hemolymph than in other tissues, suggesting that L-type voltage-dependent calcium channels are responsible for Ca^<2+> absorption in the gill and Ca^<2+> entry into hemocytes. In the mantle, PCaβ mRNA was predominantly expressed in the inner and middle folds of the mantle epithelium, suggesting that L-type voltage-dependent calcium channels are involved in Ca^<2+> absorption from the ambient medium in the mantle. All these results suggest that voltage-dependent calcium channels are involved in Ca^<2+> uptake and transport during oyster biomineralization.
社団法人日本生物工学会の論文
2007-07-25

Cloning, Characterization and Expression Analysis of Calcium Channel β Subunit from Pearl Oyster(Pinctada fucata)(GENETICS, MOLECULAR BIOLOGY, AND GENE ENGINEERING)

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