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...

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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:
Online Access:http://hdl.handle.net/11573/225586
https://doi.org/10.1016/j.abb.2008.06.022
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spelling ftunivromairis:oai:iris.uniroma1.it:11573/225586 2024-02-04T09:54:29+01:00 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 Giuliano Bellapadrona Giorgi, Alessandra Mignogna, Giuseppina Giuliano, Bellapadrona Gattoni, Maurizio Chiaraluce, Roberta Consalvi, Valerio Chiancone, Emilia Stefanini, Simonetta 2008 STAMPA 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 eng eng ELSEVIER SCIENCE INC, 360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USA info:eu-repo/semantics/altIdentifier/pmid/18625196 info:eu-repo/semantics/altIdentifier/wos/WOS:000259419200009 volume:478 issue:1 firstpage:69 lastpage:74 numberofpages:6 journal:ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS http://hdl.handle.net/11573/225586 doi:10.1016/j.abb.2008.06.022 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-51249120084 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 antarctic fish ferritin cold adaptation heteropolymeric assembly trematomus bernacchii trematomus newnesi info:eu-repo/semantics/article 2008 ftunivromairis https://doi.org/10.1016/j.abb.2008.06.022 2024-01-10T17:48:26Z 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. Article in Journal/Newspaper Antarc* Antarctic Sapienza Università di Roma: CINECA IRIS Antarctic The Antarctic Fish Point ENVELOPE(-56.465,-56.465,49.900,49.900) Archives of Biochemistry and Biophysics 478 1 69 74
institution Open Polar
collection Sapienza Università di Roma: CINECA IRIS
op_collection_id ftunivromairis
language English
topic antarctic fish ferritin
cold adaptation
heteropolymeric assembly
trematomus bernacchii
trematomus newnesi
spellingShingle antarctic fish ferritin
cold adaptation
heteropolymeric assembly
trematomus bernacchii
trematomus newnesi
GIORGI, ALESSANDRA
MIGNOGNA, Giuseppina
GATTONI, Maurizio
CHIARALUCE, Roberta
CONSALVI, Valerio
CHIANCONE, Emilia
STEFANINI, Simonetta
Giuliano Bellapadrona
The unusual co-assembly of H- and M-chains in the ferritin molecule from the Antarctic teleosts Trematomus bernacchii and Trematomus newnesi
topic_facet antarctic fish ferritin
cold adaptation
heteropolymeric assembly
trematomus bernacchii
trematomus newnesi
description 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.
author2 Giorgi, Alessandra
Mignogna, Giuseppina
Giuliano, Bellapadrona
Gattoni, Maurizio
Chiaraluce, Roberta
Consalvi, Valerio
Chiancone, Emilia
Stefanini, Simonetta
format Article in Journal/Newspaper
author GIORGI, ALESSANDRA
MIGNOGNA, Giuseppina
GATTONI, Maurizio
CHIARALUCE, Roberta
CONSALVI, Valerio
CHIANCONE, Emilia
STEFANINI, Simonetta
Giuliano Bellapadrona
author_facet GIORGI, ALESSANDRA
MIGNOGNA, Giuseppina
GATTONI, Maurizio
CHIARALUCE, Roberta
CONSALVI, Valerio
CHIANCONE, Emilia
STEFANINI, Simonetta
Giuliano Bellapadrona
author_sort GIORGI, ALESSANDRA
title The unusual co-assembly of H- and M-chains in the ferritin molecule from the Antarctic teleosts Trematomus bernacchii and Trematomus newnesi
title_short The unusual co-assembly of H- and M-chains in the ferritin molecule from the Antarctic teleosts Trematomus bernacchii and Trematomus newnesi
title_full The unusual co-assembly of H- and M-chains in the ferritin molecule from the Antarctic teleosts Trematomus bernacchii and Trematomus newnesi
title_fullStr The unusual co-assembly of H- and M-chains in the ferritin molecule from the Antarctic teleosts Trematomus bernacchii and Trematomus newnesi
title_full_unstemmed The unusual co-assembly of H- and M-chains in the ferritin molecule from the Antarctic teleosts Trematomus bernacchii and Trematomus newnesi
title_sort unusual co-assembly of h- and m-chains in the ferritin molecule from the antarctic teleosts trematomus bernacchii and trematomus newnesi
publisher ELSEVIER SCIENCE INC, 360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USA
publishDate 2008
url http://hdl.handle.net/11573/225586
https://doi.org/10.1016/j.abb.2008.06.022
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long_lat ENVELOPE(-56.465,-56.465,49.900,49.900)
geographic Antarctic
The Antarctic
Fish Point
geographic_facet Antarctic
The Antarctic
Fish Point
genre Antarc*
Antarctic
genre_facet Antarc*
Antarctic
op_relation info:eu-repo/semantics/altIdentifier/pmid/18625196
info:eu-repo/semantics/altIdentifier/wos/WOS:000259419200009
volume:478
issue:1
firstpage:69
lastpage:74
numberofpages:6
journal:ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
http://hdl.handle.net/11573/225586
doi:10.1016/j.abb.2008.06.022
info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-51249120084
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container_title Archives of Biochemistry and Biophysics
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