Identification and molecular analysis of a ferritin subunit from red drum (Sciaenops ocellatus)
Ferritin is a conserved iron binding protein existing ubiquitously in prokaryotes and eukaryotes. In this study, the gene encoding a ferritin M subunit homologue (SoFer1) was cloned from red drum (Sciaenops ocellatus) and analyzed at expression and functional levels. The open reading frame of SoFer1...
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ftchinacasciocas:oai:ir.qdio.ac.cn:337002/32774 2023-05-15T18:06:01+02:00 Identification and molecular analysis of a ferritin subunit from red drum (Sciaenops ocellatus) Hu, Yong-hua Zheng, Wen-jiang Sun, Li 2010-04-01 http://ir.qdio.ac.cn/handle/337002/32774 https://doi.org/10.1016/j.fsi.2010.01.001 英语 eng FISH & SHELLFISH IMMUNOLOGY http://ir.qdio.ac.cn/handle/337002/32774 doi:10.1016/j.fsi.2010.01.001 Ferritin Immune Defence Iron Oxidative Stress Sciaenops Ocellatus Article 期刊论文 2010 ftchinacasciocas https://doi.org/10.1016/j.fsi.2010.01.001 2022-06-27T05:37:08Z Ferritin is a conserved iron binding protein existing ubiquitously in prokaryotes and eukaryotes. In this study, the gene encoding a ferritin M subunit homologue (SoFer1) was cloned from red drum (Sciaenops ocellatus) and analyzed at expression and functional levels. The open reading frame of SoFer1 is 531 bp and preceded by a 5'-untranslated region that contains a putative Iron Regulatory Element (IRE) preserved in many ferritins. The deduced amino acid sequence of SoFer1 possesses both the ferroxidase center of mammalian H ferritin and the iron nucleation site of mammalian L ferritin. Expression of SoFer1 was tissue specific and responded positively to experimental challenges with Gram-positive and Gram-negative fish pathogens. Treatment of red drum liver cells with iron, copper, and oxidant significantly upregulated the expression of SoFer1 in time-dependent manners. To further examine the potential role of SoFer1 in antioxidation, red drum liver cells transfected transiently with SoFer1 were prepared. Compared to control cells, SoFer1 transfectants exhibited reduced production of reactive oxygen species following H(2)O(2) challenge. Finally, to examine the iron binding potential of SoFer1. SoFer1 was expressed in and purified from Escherichia colt as a recombinant protein. Iron-chelating analysis showed that purified recombinant SoFer1 was capable of iron binding. Taken together, these results suggest that SoFer1 is likely to be a functional ferritin involved in iron sequestration, host immune defence against bacterial infection, and antioxidation. (C) 2010 Elsevier Ltd. All rights reserved. Article in Journal/Newspaper Red drum Sciaenops ocellatus Institute of Oceanology, Chinese Academy of Sciences: IOCAS-IR Fish & Shellfish Immunology 28 4 678 686 |
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Open Polar |
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Institute of Oceanology, Chinese Academy of Sciences: IOCAS-IR |
op_collection_id |
ftchinacasciocas |
language |
English |
topic |
Ferritin Immune Defence Iron Oxidative Stress Sciaenops Ocellatus |
spellingShingle |
Ferritin Immune Defence Iron Oxidative Stress Sciaenops Ocellatus Hu, Yong-hua Zheng, Wen-jiang Sun, Li Identification and molecular analysis of a ferritin subunit from red drum (Sciaenops ocellatus) |
topic_facet |
Ferritin Immune Defence Iron Oxidative Stress Sciaenops Ocellatus |
description |
Ferritin is a conserved iron binding protein existing ubiquitously in prokaryotes and eukaryotes. In this study, the gene encoding a ferritin M subunit homologue (SoFer1) was cloned from red drum (Sciaenops ocellatus) and analyzed at expression and functional levels. The open reading frame of SoFer1 is 531 bp and preceded by a 5'-untranslated region that contains a putative Iron Regulatory Element (IRE) preserved in many ferritins. The deduced amino acid sequence of SoFer1 possesses both the ferroxidase center of mammalian H ferritin and the iron nucleation site of mammalian L ferritin. Expression of SoFer1 was tissue specific and responded positively to experimental challenges with Gram-positive and Gram-negative fish pathogens. Treatment of red drum liver cells with iron, copper, and oxidant significantly upregulated the expression of SoFer1 in time-dependent manners. To further examine the potential role of SoFer1 in antioxidation, red drum liver cells transfected transiently with SoFer1 were prepared. Compared to control cells, SoFer1 transfectants exhibited reduced production of reactive oxygen species following H(2)O(2) challenge. Finally, to examine the iron binding potential of SoFer1. SoFer1 was expressed in and purified from Escherichia colt as a recombinant protein. Iron-chelating analysis showed that purified recombinant SoFer1 was capable of iron binding. Taken together, these results suggest that SoFer1 is likely to be a functional ferritin involved in iron sequestration, host immune defence against bacterial infection, and antioxidation. (C) 2010 Elsevier Ltd. All rights reserved. |
format |
Article in Journal/Newspaper |
author |
Hu, Yong-hua Zheng, Wen-jiang Sun, Li |
author_facet |
Hu, Yong-hua Zheng, Wen-jiang Sun, Li |
author_sort |
Hu, Yong-hua |
title |
Identification and molecular analysis of a ferritin subunit from red drum (Sciaenops ocellatus) |
title_short |
Identification and molecular analysis of a ferritin subunit from red drum (Sciaenops ocellatus) |
title_full |
Identification and molecular analysis of a ferritin subunit from red drum (Sciaenops ocellatus) |
title_fullStr |
Identification and molecular analysis of a ferritin subunit from red drum (Sciaenops ocellatus) |
title_full_unstemmed |
Identification and molecular analysis of a ferritin subunit from red drum (Sciaenops ocellatus) |
title_sort |
identification and molecular analysis of a ferritin subunit from red drum (sciaenops ocellatus) |
publishDate |
2010 |
url |
http://ir.qdio.ac.cn/handle/337002/32774 https://doi.org/10.1016/j.fsi.2010.01.001 |
genre |
Red drum Sciaenops ocellatus |
genre_facet |
Red drum Sciaenops ocellatus |
op_relation |
FISH & SHELLFISH IMMUNOLOGY http://ir.qdio.ac.cn/handle/337002/32774 doi:10.1016/j.fsi.2010.01.001 |
op_doi |
https://doi.org/10.1016/j.fsi.2010.01.001 |
container_title |
Fish & Shellfish Immunology |
container_volume |
28 |
container_issue |
4 |
container_start_page |
678 |
op_container_end_page |
686 |
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1766177577241673728 |