title: Iron-metabolic function and potential antibacterial role of Hepcidin and its correlated genes (Ferroportin 1 and Transferrin Receptor) in turbot (Scophthalmus maximus).
abstract: Antimicrobial peptide plays an important role in fish immunity. The small molecular antimicrobial peptide Hepcidin in turbot was studied and reported in this paper. The Ferroportin 1 (FPN1) and Transferrin Receptor (TFR) genes, which are related to Hepcidin, were cloned in turbot. The characteristics of Hepcidin and its related genes were studied, including an analysis of the expression patterns and cloning of the Hepcidin promoter, the relationship between Hepcidin and NF-κB and the regulation of iron-metabolism. The results showed that the promoter of SmHepcidin contains the binding sites of NF-κB, and NF-κB may directly or indirectly receive feedback signals from SmHepcidin. In the liver, spleen and kidney, in which there was an increased SmHepcidin expression level, SmFPN1 dramatically decreased and SmTFR was also either decreased or exhibited no obvious change after bacterial/viral infection and an injection of exogenous Hepcidin protein. RNAi experiments in turbot kidney cells confirmed the expression changes of these gene patterns. Furthermore, the administration of exogenous Hepcidin protein, which regulates the level of chelatable iron in cells, further confirmed the function of Hepcidin in iron metabolism. It is speculated that the rapidly increased expression of SmHepcidin may induce changes in the expression of related genes, and that the in vivo chelatable iron concentration which participates in the antibacterial process was also changed when exogenous pathogens are present in turbot. It is suggested that SmHepcidin plays a defensive role against pathogenic infection.
authors.affiliation: Yellow Sea Fisheries Research Institute, Chinese Academy of Fisheries Sciences, 106 Nanjing Road, Qingdao 266071, Shandong, China.
authors.forename: Chang-Geng
authors.initials: CG
authors.lastname: Yang
authors.forename: Shan-Shan
authors.initials: SS
authors.lastname: Liu
authors.forename: Bing
authors.initials: B
authors.lastname: Sun
authors.forename: Xian-Li
authors.initials: XL
authors.lastname: Wang
authors.forename: Na
authors.initials: N
authors.lastname: Wang
authors.forename: Song-Lin
authors.initials: SL
authors.lastname: Chen
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000235:genetics / Q000276:immunology* / Q000378:metabolism; D001483:Base Sequence; D027682:Cation Transport Proteins / Q000737:chemistry / Q000235:genetics / Q000276:immunology* / Q000378:metabolism; D003001:Cloning, Molecular; D005412:Flatfishes / Q000235:genetics / Q000276:immunology* / Q000378:metabolism; D020869:Gene Expression Profiling / Q000662:veterinary; D064451:Hepcidins; D007501:Iron / Q000378:metabolism*; D008969:Molecular Sequence Data; D009928:Organ Specificity; D010802:Phylogeny; D016133:Polymerase Chain Reaction / Q000662:veterinary; D011401:Promoter Regions, Genetic; D012333:RNA, Messenger / Q000032:analysis; D011990:Receptors, Transferrin / Q000737:chemistry / Q000235:genetics / Q000276:immunology* / Q000378:metabolism; D016415:Sequence Alignment / Q000662:veterinary; D014733:Vibrio / Q000502:physiology; D014735:Vibrio Infections / Q000276:immunology / Q000662:veterinary; D000098742:Ferroportin
chemical_list: D023181:Antimicrobial Cationic Peptides; D027682:Cation Transport Proteins; D064451:Hepcidins; D012333:RNA, Messenger; D011990:Receptors, Transferrin; D000098742:Ferroportin; D007501:Iron