JBC Invitrogen Ultrasensitive Cytokine Assays

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Originally published In Press as doi:10.1074/jbc.C100141200 on April 25, 2001

J. Biol. Chem., Vol. 276, Issue 27, 24437-24440, July 6, 2001
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ACCELERATED PUBLICATION
A Human Mitochondrial Ferritin Encoded by an Intronless Gene*

Sonia LeviDagger , Barbara Corsi§, Marta BosisioDagger , Rosangela Invernizzi, Armin Volz||, David Sanford**, Paolo Arosio§, and Jim Drysdale**Dagger Dagger

From the Dagger  Istituto Ricovera e Cura a Carattera Scientifico S. Raffaele Hospital, 20132 Milan, Italy, the § Faculty of Medicine, University of Brescia, 25100 Brescia, Italy, the  Department of Internal Medicine and Medical Therapy, University of Pavia, 27100 Italy, || Charité, Universitätsklinikum der Humboldt Universität, zu Berlin, Germany, and the ** Department of Biochemistry, Tufts University School of Medicine, Boston, Massachusetts 02111

Ferritin is a ubiquitous protein that plays a critical role in regulating intracellular iron homoeostasis by storing iron inside its multimeric shell. It also plays an important role in detoxifying potentially harmful free ferrous iron to the less soluble ferric iron by virtue of the ferroxidase activity of the H subunit. Although excess iron is stored primarily in cytoplasm, most of the metabolically active iron in cells is processed in mitochondria. Little is yet known of how these organelles regulate iron homeostasis and toxicity. Here we report an unusual intronless gene on chromosome 5q23.1 that encodes a 242-amino acid precursor of a ferritin H-like protein. This 30-kDa protein is targeted to mitochondria and processed to a 22-kDa subunit that assembles into typical ferritin shells and has ferroxidase activity. Immunohistochemical analysis showed that it accumulates in high amounts in iron-loaded mitochondria of erythroblasts of subjects with impaired heme synthesis. This new ferritin may play an important role in the regulation of mitochondrial iron homeostasis and heme synthesis.

* This work was partially supported by Italian Ministry of the University and Scientific and Technologic Research (MURST) Cofin-99 (to P. A.), by CNR, Targeted Project in Biotechnology (to P. A.), by Ricerca Finalizzata IRCCS 1998 (to S. L.), and by 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.

Dagger Dagger To whom correspondence should be addressed: Dept. of Biochemistry, Tufts University School of Medicine, 136 Harrison Ave., Boston, MA 02111. Tel.: 617-636-6855; Fax: 617-636-2409; E-mail: jim. drysdale{at}tufts.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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