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Comp Biochem Physiol B Biochem Mol Biol. 2007 Feb;146(2):207-14. Epub 2006 Oct 27.

Tyrosinase localization in mollusc shells.

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Wakayama Prefecture Collaboration of Regional Entities for the Advancement of Technological Excellence, Japan Science and Technology Agency, 60 Ogura, Wakayama-Shi, Wakayama, Japan.


In molluscan shellfish, pigmentation is frequently observed in the calcified shell, but the molecular basis of this process is not understood. Here, we report two tyrosinase proteins (Pfty1 and Pfty2) found in the prismatic shell layer of the pearl oyster Pinctada fucata; this layer is recognized as the pigmented region in P. fucata. The protein sequences were deduced from the corresponding cDNAs and confirmed by MALDI-TOF/TOF analysis. The sequences suggest that both tyrosinases have two copper-binding sites in similar N-terminal domains that are homologous to tyrosinases of cephalopods and hemocyanins of gastropods. In turn, this suggests that bivalve tyrosinases are evolved from a common ancestral copper-binding protein in the mollusc. Pfty1 and Pfty2 were specifically expressed in the mantle, and their expression in the mantle is different from each other, suggesting that these tyrosinases have distinctive roles in melanogenesis in shells.

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