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...
Published in: | Archives of Biochemistry and Biophysics |
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Format: | Article in Journal/Newspaper |
Language: | English |
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ELSEVIER SCIENCE INC, 360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USA
2008
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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 |
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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 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 |
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 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 |
op_doi |
https://doi.org/10.1016/j.abb.2008.06.022 |
container_title |
Archives of Biochemistry and Biophysics |
container_volume |
478 |
container_issue |
1 |
container_start_page |
69 |
op_container_end_page |
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