A teleostean counterpart of ferritin M subunit from rock bream (Oplegnathus fasciatus): an active constituent in iron chelation and DNA protection against oxidative damage, with a modulated expression upon pathogen stress.

作者: Don Anushka Sandaruwan Elvitigala , HKA Premachandra , Ilson Whang , Myung-Joo Oh , Sung-Ju Jung

DOI: 10.1016/J.FSI.2013.08.012

关键词:

摘要: Ferritins are biological iron chelators that can sequestrate excess to maintain homeostasis in the body. basically consist of 2 types subunits, designated as H and L. However, another new subunit, ferritin "M" which possesses characteristic features both L was recently identified lower vertebrates, mostly fish. In this study, a M-like subunit from rock bream (Oplegnathus fasciatus) (RbFerM) characterized at molecular level, its transcriptional profile analyzed healthy fish, well pathogen- mitogen-stimulated Furthermore, functional properties were evaluated using recombinant protein. The complete coding sequence RbFerM 528 bp length, encoding 176-amino acid peptide with calculated mass 20 kDa. silico analysis revealed it has similar mammalian Phylogenetic depicted higher evolutionary proximity fish counterparts. Quantitative real time polymerase chain reaction (PCR) detected ubiquitous selected tissues bream, more pronounced expression observed blood liver tissues. Significant inductions upon lipopolysaccharides (LPS), Edwardsiella tarda, Streptococcus iniae, irido virus (RBIV) exposures time-course immune-challenge experiments. purified protein demonstrated detectable chelating activity varied temperature. Moreover, rendered protection effect against (II) H2O2-mediated DNA damage.

参考文章(54)
Paolo SANTAMBROGIO, Sonia LEVI, Anna COZZI, Barbara CORSI, Paolo AROSIO, Evidence that the specificity of iron incorporation into homopolymers of human ferritin L- and H-chains is conferred by the nucleation and ferroxidase centres. Biochemical Journal. ,vol. 314, pp. 139- 144 ,(1996) , 10.1042/BJ3140139
Paolo Arosio, James W. Drysdale, Minoru Yokota, Structural and immunological relationships of isoferritins in normal and malignant cells. Cancer Research. ,vol. 36, pp. 1735- 1739 ,(1976)
S V Torti, E L Kwak, S C Miller, L L Miller, G M Ringold, K B Myambo, A P Young, F M Torti, The molecular cloning and characterization of murine ferritin heavy chain, a tumor necrosis factor-inducible gene. Journal of Biological Chemistry. ,vol. 263, pp. 12638- 12644 ,(1988) , 10.1016/S0021-9258(18)37801-3
Ilson Whang, Youngdeuk Lee, Hyowon Kim, Sung-Ju Jung, Myung-Joo Oh, Cheol Young Choi, Woo Song Lee, Se-Jae Kim, Jehee Lee, Characterization and expression analysis of the myeloid differentiation factor 88 (MyD88) in rock bream Oplegnathus fasciatus. Molecular Biology Reports. ,vol. 38, pp. 3911- 3920 ,(2011) , 10.1007/S11033-010-0507-2
Frank M. Torti, Suzy V. Torti, Regulation of ferritin genes and protein Blood. ,vol. 99, pp. 3505- 3516 ,(2002) , 10.1182/BLOOD.V99.10.3505
Xiao Zhang, Wei Wei, Haizhen Wu, Hongyan Xu, Kangmei Chang, Yuanxing Zhang, Gene cloning and characterization of ferritin H and M subunits from large yellow croaker (Pseudosciaena crocea). Fish & Shellfish Immunology. ,vol. 28, pp. 735- 742 ,(2010) , 10.1016/J.FSI.2009.11.027
Jean Pieters, Evasion of host cell defense mechanisms by pathogenic bacteria. Current Opinion in Immunology. ,vol. 13, pp. 37- 44 ,(2001) , 10.1016/S0952-7915(00)00179-5
Jung-Hoon Kang, Oxidative Damage of DNA Induced by Ferritin and Hydrogen Peroxide Bulletin of The Korean Chemical Society. ,vol. 31, pp. 2873- 2876 ,(2010) , 10.5012/BKCS.2010.31.10.2873
Soo Il Park, Disease control in Korean aquaculture. Fish Pathology. ,vol. 44, pp. 19- 23 ,(2009) , 10.3147/JSFP.44.19