title: Identification and analysis of a Scophthalmus maximus ferritin that is regulated at transcription level by oxidative stress and bacterial infection.
abstract: Ferritins are conserved iron storage proteins that exist in most living organisms and play an essential role in iron homeostasis. In this study, we reported the identification and analysis a ferritin M subunit, SmFerM, from turbot Scophthalmus maximus. The full length cDNA of SmFerM contains a 5'-untranslated region (UTR) of 232 bp, an open reading frame (ORF) of 531 bp, and a 3'-UTR of 196 bp. The ORF encodes a putative protein of 176 amino acids, which shares extensive sequence identities with the M ferritins of several fish species. In silico analysis identified in SmFerM both the ferroxidase center of mammalian H ferritins and the iron nucleation site of mammalian L ferritins. Quantitative real time reverse transcriptase-PCR analysis indicated that SmFerM expression was highest in muscle and lowest in heart and responded positively to experimental challenges with bacterial pathogens and poly(I:C). Exposure of cultured turbot hepatocytes to treatment of stress inducers (iron, copper, and H(2)O(2)) significantly upregulated the expression of SmFerM in a dose dependent manner. Iron chelating analysis showed that recombinant SmFerM purified from Escherichia coli exhibited apparent iron binding activity. These results suggest that SmFerM is a functional M ferritin and is likely to play a role in iron sequestration and protection against oxidative stress and microbial infection.
authors.affiliation: Institute of Oceanology, Chinese Academy of Sciences, Qingdao, PR China.
authors.forename: Wen-jiang
authors.initials: WJ
authors.lastname: Zheng
authors.forename: Yong-hua
authors.initials: YH
authors.lastname: Hu
authors.forename: Li
authors.initials: L
authors.lastname: Sun
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001424:Bacterial Infections / Q000378:metabolism / Q000662:veterinary; D001483:Base Sequence; D002478:Cells, Cultured; D003001:Cloning, Molecular; D003300:Copper / Q000633:toxicity; D005293:Ferritins / Q000235:genetics / Q000378:metabolism*; D005393:Fish Diseases / Q000378:metabolism / Q000382:microbiology; D029941:Fish Proteins / Q000235:genetics / Q000378:metabolism*; D005412:Flatfishes / Q000235:genetics / Q000378:metabolism* / Q000382:microbiology; D005786:Gene Expression Regulation; D006861:Hydrogen Peroxide / Q000633:toxicity; D007501:Iron / Q000378:metabolism / Q000633:toxicity; D008969:Molecular Sequence Data; D018384:Oxidative Stress; D014158:Transcription, Genetic
chemical_list: D029941:Fish Proteins; D003300:Copper; D005293:Ferritins; D006861:Hydrogen Peroxide; D007501:Iron