A novel calcium-binding peptide from the cuticle of the crayfish, Procambarus clarkii

被引：48

作者：

Inoue, H ^{[1
]}

Ohira, T

Ozaki, N

Nagasawa, H

机构：

[1] Univ Tokyo, Grad Sch Agr & Life Sci, Dept Appl Biol Chem, Bunkyo Ku, Tokyo 1138657, Japan

[2] Japan Sci & Technol Agcy, CREST, Kawaguchi, Saitama 3320012, Japan

[3] Univ Tokyo, Grad Sch Sci, Dept Earth & Planetary Sci, Bunkyo Ku, Tokyo 1130033, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2004年 / 318卷 / 03期

基金：

日本学术振兴会;

关键词：

biomineralization; calcification; calcium bindings; chitin; crayfish; cuticle peptide; exoskeleton; Procambarus clarkii;

D O I：

10.1016/j.bbrc.2004.04.075

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 K-d 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. (C) 2004 Elsevier Inc. All rights reserved.

引用

页码：649 / 654

页数：6

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