| XIE Jiasong,CAO Xiaohua,WU Liuji,LUO Ming,ZHU Zewen,HUANG Yanqing,WU Xinzhong. 2012. Molecular and functional characterization of ferritin in abalone Haliotis diversicolor supertexta. Acta Oceanologica Sinica, (3):87－97 |
| Molecular and functional characterization of ferritin in abalone Haliotis diversicolor supertexta |
| Molecular and functional characterization of ferritin in abalone Haliotis diversicolor supertexta |
| Received:January 25, 2011 Revised:November 28, 2011 |
| DOI：10.1007/s13131-012-0209-9 |
| Key words:Haliotis diversicolor supertexta ferritin respiratory burst oxidative damage immune response |
| 中文关键词: Haliotis diversicolor supertexta ferritin respiratory burst oxidative damage immune response |
| 基金项目:The National Natural Science Foundation of China under contract No. 30671619; the Natural Science Foundation of Zhejiang Province under contract No. Y307606. |
| Author Name | Affiliation | E-mail | | XIE Jiasong | Laboratory of Marine Life Science and Technology, College of Animal Sciences, Zhejiang University, Hangzhou 310058, China | | | CAO Xiaohua | Laboratory of Marine Life Science and Technology, College of Animal Sciences, Zhejiang University, Hangzhou 310058, China | | | WU Liuji | Laboratory of Marine Life Science and Technology, College of Animal Sciences, Zhejiang University, Hangzhou 310058, China | | | LUO Ming | Laboratory of Marine Life Science and Technology, College of Animal Sciences, Zhejiang University, Hangzhou 310058, China | | | ZHU Zewen | Laboratory of Marine Life Science and Technology, College of Animal Sciences, Zhejiang University, Hangzhou 310058, China | | | HUANG Yanqing | Laboratory of Marine Life Science and Technology, College of Animal Sciences, Zhejiang University, Hangzhou 310058, China | | | WU Xinzhong | Laboratory of Marine Life Science and Technology, College of Animal Sciences, Zhejiang University, Hangzhou 310058, China | wuxz@zju.edu.cn |
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| Abstract: |
| Ferritin is an iron storage protein that plays a key role in the processes of physiology and pathology. In the present study, the authors reported the ferritin gene from abalone Haliotis diversicolor supertexta, which we named hds-ferritin. The full-length of hds-ferritin cDNA consisted of 879 bp with an ORF encoding a 171 amino acids. Amino acid sequence analysis revealed that hds-ferritin shared highly homology with other species. Real time PCR and western blot analysis showed that hds-ferritin was distributed ubiquitously in abalone tissues and had the highest expression level in digestive glands, but its transcripts are not modified remarkably by the stimulation with LPS. The recombinant protein was successfully expressed in Escherichia coli BL21 (DE3), and the titre of anti-ferritin antibody was about 1:14 000. The effects of ROS and RNS on ferritin were analyzed in the present study. The results showed that H2O2 played an important role in decreasing hds-ferritin, however NO cation appeared to have a protecting effect on H2O2-medied reduction of hds-ferritin. |
| 中文摘要: |
| Ferritin is an iron storage protein that plays a key role in the processes of physiology and pathology. In the present study, the authors reported the ferritin gene from abalone Haliotis diversicolor supertexta, which we named hds-ferritin. The full-length of hds-ferritin cDNA consisted of 879 bp with an ORF encoding a 171 amino acids. Amino acid sequence analysis revealed that hds-ferritin shared highly homology with other species. Real time PCR and western blot analysis showed that hds-ferritin was distributed ubiquitously in abalone tissues and had the highest expression level in digestive glands, but its transcripts are not modified remarkably by the stimulation with LPS. The recombinant protein was successfully expressed in Escherichia coli BL21 (DE3), and the titre of anti-ferritin antibody was about 1:14 000. The effects of ROS and RNS on ferritin were analyzed in the present study. The results showed that H2O2 played an important role in decreasing hds-ferritin, however NO cation appeared to have a protecting effect on H2O2-medied reduction of hds-ferritin. |
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