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

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-chai...

Full description

Bibliographic Details
Published in:Archives of Biochemistry and Biophysics
Main Authors: GIORGI, ALESSANDRA, MIGNOGNA, Giuseppina, GATTONI, Maurizio, CHIARALUCE, Roberta, CONSALVI, Valerio, CHIANCONE, Emilia, STEFANINI, Simonetta, Giuliano Bellapadrona
Other Authors: Giorgi, Alessandra, Mignogna, Giuseppina, Giuliano, Bellapadrona, Gattoni, Maurizio, Chiaraluce, Roberta, Consalvi, Valerio, Chiancone, Emilia, Stefanini, Simonetta
Format: Article in Journal/Newspaper
Language:English
Published: ELSEVIER SCIENCE INC, 360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USA 2008
Subjects:
antarctic fish ferritin
cold adaptation
heteropolymeric assembly
trematomus bernacchii
trematomus newnesi
Antarctic
The Antarctic
Fish Point
Antarc*
Online Access:http://hdl.handle.net/11573/225586
https://doi.org/10.1016/j.abb.2008.06.022
http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=000259419200009&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396a
http://www.scopus.com/inward/record.url?eid=2-s2.0-51249120084&partnerID=65&md5=c245a644947940cd9e465e328ff5d908
Description
Summary: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.

Similar Items