Dual function of fish hepcidin: Response to experimental iron overload and bacterial infection in sea bass (Dicentrarchus labrax)
Autor: | Sandra Vázquez-Dorado, Pedro Rodrigues, Jonathan M. Wilson, João V. Neves |
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Rok vydání: | 2006 |
Předmět: |
inorganic chemicals
congenital hereditary and neonatal diseases and abnormalities Iron Overload Molecular Sequence Data Immunology Microbiology Fish Diseases Exon Hepcidins Hepcidin hemic and lymphatic diseases Gene expression medicine Animals Amino Acid Sequence Sea bass Gene Phylogeny Base Sequence biology Photobacterium Reverse Transcriptase Polymerase Chain Reaction Transferrin Intron nutritional and metabolic diseases Iron deficiency biology.organism_classification medicine.disease Hematocrit Liver Erythrocyte Count biology.protein Bass Dicentrarchus Gram-Negative Bacterial Infections Sequence Alignment Antimicrobial Cationic Peptides Developmental Biology |
Zdroj: | Developmental & Comparative Immunology. 30:1156-1167 |
ISSN: | 0145-305X |
DOI: | 10.1016/j.dci.2006.02.005 |
Popis: | The role of hepcidin in iron metabolism regulation and bacterial infection has been the focus of recent attention. However, in spite of the growing number of hepcidin genes known from different organisms, little is known about its putative dual function in fish. The aim of this study was to characterize the sea bass hepcidin gene and to study its role in iron metabolism and infection. The novel sea bass hepcidin gene was found to be organized into two introns and three exons with several copies present in the genome. The transcript showed a constitutive low basal expression being mainly expressed in liver and encoding a putative 85 residues long peptide. Fish were submitted either to iron status modulation or bacterial infection and the hepcidin transcript levels were analysed along with a number of other parameters. Liver hepcidin expression was found to increase in both the iron-overloaded and infected fish, while in the iron-deficient fish no alteration in expression levels was detected. These results point to the evolutionary conservation of hepcidin's dual functions. |
Databáze: | OpenAIRE |
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