Ferritins from the liver and spleen of the cold-adapted Antarctic teleosts Trematomus bernacchii and Trematomus newnesi have been isolated and characterized. Interestingly, only H- and M-chains are expressed and no L-chains. The H-chains contain the conserved ferroxidase center residues while M-chains harbor both the ferroxidase center and the micelle nucleation site ligands. Ferritins have an organ-specific subunit composition, they are: M homopolymers in spleen and H/M heteropolymers in liver. The M-chain homopolymer mineralizes iron at higher rate with respect to the H/M heteropolymer, which however is endowed with a lower activation energy for the iron incorporation process, indicative of a higher local flexibility. These findings and available literature data on ferritin expression in fish point to the role of tissue-specific expression of different chains in modulating the iron oxidation/mineralization process. © 2008 Elsevier Inc. All rights reserved.

The unusual co-assembly of H- and M-chains in the ferritin molecule from the Antarctic teleosts Trematomus bernacchii and Trematomus newnesi / Giorgi, Alessandra; Mignogna, Giuseppina; Giuliano, Bellapadrona; Gattoni, Maurizio; Chiaraluce, Roberta; Consalvi, Valerio; Chiancone, Emilia; Stefanini, Simonetta. - In: ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS. - ISSN 0003-9861. - STAMPA. - 478:1(2008), pp. 69-74. [10.1016/j.abb.2008.06.022]

The unusual co-assembly of H- and M-chains in the ferritin molecule from the Antarctic teleosts Trematomus bernacchii and Trematomus newnesi

GIORGI, ALESSANDRA;MIGNOGNA, Giuseppina;GATTONI, Maurizio;CHIARALUCE, Roberta;CONSALVI, Valerio;CHIANCONE, Emilia;STEFANINI, Simonetta
2008

Abstract

Ferritins from the liver and spleen of the cold-adapted Antarctic teleosts Trematomus bernacchii and Trematomus newnesi have been isolated and characterized. Interestingly, only H- and M-chains are expressed and no L-chains. The H-chains contain the conserved ferroxidase center residues while M-chains harbor both the ferroxidase center and the micelle nucleation site ligands. Ferritins have an organ-specific subunit composition, they are: M homopolymers in spleen and H/M heteropolymers in liver. The M-chain homopolymer mineralizes iron at higher rate with respect to the H/M heteropolymer, which however is endowed with a lower activation energy for the iron incorporation process, indicative of a higher local flexibility. These findings and available literature data on ferritin expression in fish point to the role of tissue-specific expression of different chains in modulating the iron oxidation/mineralization process. © 2008 Elsevier Inc. All rights reserved.
2008
antarctic fish ferritin; cold adaptation; heteropolymeric assembly; trematomus bernacchii; trematomus newnesi
01 Pubblicazione su rivista::01a Articolo in rivista
The unusual co-assembly of H- and M-chains in the ferritin molecule from the Antarctic teleosts Trematomus bernacchii and Trematomus newnesi / Giorgi, Alessandra; Mignogna, Giuseppina; Giuliano, Bellapadrona; Gattoni, Maurizio; Chiaraluce, Roberta; Consalvi, Valerio; Chiancone, Emilia; Stefanini, Simonetta. - In: ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS. - ISSN 0003-9861. - STAMPA. - 478:1(2008), pp. 69-74. [10.1016/j.abb.2008.06.022]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/225586
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