engleski

Iron homeostasis in Mediterranean mussel Mytilus galloprovincialis (Lamarck, 1819)

Iron is required for normal cell growth and proliferation. However, excess iron is potentially harmful, as it can catalyse the formation of toxic reactive oxygen species via Fenton chemistry. Ferritin plays a central role in the maintenance of intracellular balance of iron (Fe2+/Fe3+). Ferritin is almost ubiquitous and largely conserved from bacteria to human, although the role in the regulation of iron trafficking varies in different organisms. The metal chelator, ferritin molecule is a protein shell composed of 24 protein chains arranged in 2, 3, 4 point symmetry, with the capacity to sequester up to 4500 atoms of iron in a ferrihydrite mineral core. In this study we characterize full length M. galloprovincialis ferritin cDNA and gene sequence. The ferritin cDNA transcript with the 5’ and 3’ untranslated regions is 791 bp long. The putative open reading frame (114-638 bp) encodes a polypeptide of 174 amino acids, with a theoretical pI/Mw 4.88/ 20.114 kDa and three conserved domains: ferroxidase diiron center, ferrihydrite nucleation center and iron ion channel. According to the bioinformatics analysis, this ferritin is likely to be a homolog of vertebrate H-ferritin. The ferritin expression is regulated at both transcriptional and translational levels. The iron levels in the cell regulate the ferritin translation, removing the interaction between iron regulatory protein (IRP) and iron response element (IRE ; 17-44 bp). In response to oxidative stress, the cells activate a defence strategy using ferritin to restrict the metal availability, so the ferritin as an anti/pro- oxidant agent in mussel M. galloprovincialis has a potential application as biomarker of oxidative stress.

Iron; Oxidative stres; Ferritin; Biomarker; Mytilus galloprovincialis

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