A novel calcium-binding peptide from the cuticle of the crayfish, Procambarus clarkii |
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Authors: | Inoue Hirotaka Ohira Tsuyoshi Ozaki Noriaki Nagasawa Hiromichi |
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Institution: | Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo, Tokyo 113-8657, Japan. aa27009@mail.ecc.u-tokyo.ac.jp |
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Abstract: | A novel peptide named calcification-associated peptide (CAP)-2 was isolated from the exoskeleton of the crayfish, Procambarus clarkii. CAP-2 consists of 65 amino acid residues and has a 44% sequence identity with CAP-1 characterized previously. It has a chitin-binding domain observed in many arthropod cuticle proteins. CAP-2 showed inhibitory activity on calcium carbonate precipitation and chitin-binding ability. A CAP-2 cDNA was cloned using RT-PCR and RACE and the open reading frame encoded a precursor peptide consisting of a signal peptide and CAP-2. RT-PCR revealed that CAP-2 mRNA was exclusively expressed in the epidermal tissue during the postmolt stage, the site and stage being associated with calcification. Calcium-binding assay using recombinant CAP-2 revealed that this peptide had affinity for calcium ions with a Kd value of about 1 mM. All these results suggest that CAP-2 serves as a nucleator or a regulator in the calcification of the exoskeleton. |
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Keywords: | Biomineralization Calcification Calcium binding Chitin Crayfish Cuticle peptide Exoskeleton Procambarus clarkii |
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