Faculty of Life Science and Biotechnology, Ningbo University, 818 Fenghua Road, Ningbo, Zhejiang Province 315211, PR China.
Fish Shellfish Immunol. 2011 Apr-May;30(4-5):1147-51. doi: 10.1016/j.fsi.2011.02.017. Epub 2011 Mar 6.
Ferritin, a major iron storage protein of most living organisms, plays a crucial role in iron metabolism. Here we reported the isolation and characterization of a cDNA of ferritin gene from Sinonovacula constricta (denoted as ScFER). The full-length cDNA of ScFER was of 996 bp, consisting of a 5'-UTR of 120 bp, a 3'-UTR of 360 bp, and a complete open reading frame of 516 bp encoding a polypeptide with 171 amino acid residues. The predicted molecular mass of deduced amino acid of ScFER was 19.76 kDa and the theoretical pI was 5.07. Quantitative real-time PCR was employed to analyze the expression profiles of ScFER mRNA in muscle, mantle and visceral mass after iron exposure. The peak expression level of ScFER in the three tissues was 1.79-fold, 1.31-fold and 3.51-fold increases in muscle, mantle and visceral mass, respectively. The polyclonal antibodies generated from the recombinant product of ScFER could be specifically identified not only the recombinant product, but also the native protein from muscle. All these results strongly suggested that ScFER was involved in the iron metabolism regulation in S. constricta.
铁蛋白是大多数生物的主要铁储存蛋白，在铁代谢中起着至关重要的作用。在这里，我们报道了来自锯缘青蟹（Sinonovacula constricta）的铁蛋白基因 cDNA 的分离和鉴定（表示为 ScFER）。ScFER 的全长 cDNA 为 996 bp，由 120 bp 的 5'-UTR、360 bp 的 3'-UTR 和编码 171 个氨基酸残基的完整开放阅读框组成。ScFER 推断的氨基酸的预测分子量为 19.76 kDa，理论等电点为 5.07。采用定量实时 PCR 分析了铁暴露后 ScFER mRNA 在肌肉、套膜和内脏组织中的表达谱。ScFER 在这三种组织中的表达水平峰值分别增加了 1.79 倍、1.31 倍和 3.51 倍。从 ScFER 的重组产物中产生的多克隆抗体不仅可以特异性识别重组产物，还可以特异性识别肌肉中的天然蛋白。所有这些结果强烈表明 ScFER 参与了锯缘青蟹的铁代谢调节。
