engleski

Ferritin - Iron storage protein in the Mediterranean mussel Mytilus galloprovincialis

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. For this reason, cells have evolved highly regulated mechanisms for controlling intracellular iron levels. Ferritin plays a central role in the maintenance of this delicate intracellular iron balance. This protein has the capacity to sequester up to 4500 atoms of iron in a ferrihydrite mineral core, and functions to store iron not required for immediate metabolic needs. The metal chelator, ferritin molecule is a protein shell composed of 24 protein chains arranged in 2, 3, 4 point symmetry. The M. galloprovincialis ferritin cDNA transcript with the 5’ and 3’ regulating/untranslated region, is 805 bp long. The putative open reading frame (110-631 bp) encodes a polypeptide of 174 amino acids, with a theoretical pI/Mw 4.96/ 20.126 kDa and three conserved domains: ferroxidase diiron center, ferrihydrite nucleation center and iron ion channel. The number of amino acid residues in vertebrate ferritin subunits is very close to those of M. galoprovincialis ferritin, generally in the range of 170–185 amino acids. Ferritin is almost ubiquitous and largely conserved from bacteria to human, although the role in the regulation of iron trafficking varies in different organisms. Ferritin is a protein able to store and transport not only iron, but also, though to a lesser extent, some other heavy metals, including cadmium, transuranic elements such as 238Pu, 241Am and participate in accumulation of the natural radionuclide 210Po in marine organisms.

Ferritin; iron storage proteins; reactive oxygen species; Mytilus galloprovincialis

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