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Originally published In Press as doi:10.1074/jbc.M105372200 on April 12, 2002

J. Biol. Chem., Vol. 277, Issue 25, 22430-22437, June 21, 2002
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Human Mitochondrial Ferritin Expressed in HeLa Cells Incorporates Iron and Affects Cellular Iron Metabolism*

Barbara CorsiDagger , Anna Cozzi§, Paolo ArosioDagger , Jim Drysdale, Paolo Santambrogio§, Alessandro Campanella§, Giorgio BiasiottoDagger , Alberto AlbertiniDagger , and Sonia Levi§||

From the Dagger  Section of Chemistry, Faculty of Medicine, University of Brescia, Brescia, 25100 Italy, § Department of Biological and Technological Research, Istituto di Ricovero e Cura a Carattere Scientifico (IRCCS) H. San Raffaele, Milano, 20132 Italy, and the  Department of Biochemistry, Tufts University School of Medicine, Boston, Massachusetts 02111

Mitochondrial ferritin (MtF) is a newly identified ferritin encoded by an intronless gene on chromosome 5q23.1. The mature recombinant MtF has a ferroxidase center and binds iron in vitro similarly to H-ferritin. To explore the structural and functional aspects of MtF, we expressed the following forms in HeLa cells: the MtF precursor (~28 kDa), a mutant MtF precursor with a mutated ferroxidase center, a truncated MtF lacking the ~6-kDa mitochondrial leader sequence, and a chimeric H-ferritin with this leader sequence. The experiments show that all constructs with the leader sequence were processed into ~22-kDa subunits that assembled into multimeric shells electrophoretically distinct from the cytosolic ferritins. Mature MtF was found in the matrix of mitochondria, where it is a homopolymer. The wild type MtF and the mitochondrially targeted H-ferritin both incorporated the 55Fe label in vivo. The mutant MtF with an inactivated ferroxidase center did not take up iron, nor did the truncated MtF expressed transiently in cytoplasm. Increased levels of MtF both in transient and in stable transfectants resulted in a greater retention of iron as MtF in mitochondria, a decrease in the levels of cytosolic ferritins, and up-regulation of transferrin receptor. Neither effect occurred with the mutant MtF with the inactivated ferroxidase center. Our results indicate that exogenous iron is as available to mitochondrial ferritin as it is to cytosolic ferritins and that the level of MtF expression may have profound consequences for cellular iron homeostasis.

* This work was partially supported by grants from the Italian Ministry of the University and Research (MIUR) and Cofin-2000, Cofin-2001 (to P. A.), by Consiglio Nazionale delle Ricerche Targeted Project in Biotechnology (to P. A.), by Telethon-Italy Grant GP0001Y01 (to S. L.), by Consiglio Nazionale delle Ricerche-Agenzia2000 (to S. L. and P. A.), and by a grant from the Tufts University School of Medicine (to J. D.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed: Protein Engineering Unit, Istituto di Ricovero e Cura a Carattere Scientifico (IRCCS) H. San Raffaele, Via Olgettina 58, 20132 Milano, Italy. Tel.: 39-02-2643-4755; Fax: 39-02-2643-4844; E-mail: levi.sonia@hsr.it.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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