Oxidation-induced ferritin turnover in microglial cells: role of proteasome

Mehlhase, Jana; Sandig, Grit; Pantopoulos, Kostas; Grune, Tilman

doi:10.1016/j.freeradbiomed.2004.10.025

Cited by 78 publications

(47 citation statements)

References 75 publications

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“…Moreover, oxidation of the protein part of ferritin results in its accelerated degradation, as reported by Mehlhase et al (27) for RAW264.7 macrophages exposed to peroxide. Here, unlike what we and others have reported, proteasomal degradation seems to be involved: treatment with MG132 (a proteasomal inhibitor, which however, can also inhibit lysosomal proteases; see Ref.…”

mentioning

confidence: 56%

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Release of iron from ferritin requires lysosomal activity

Kidane

Sauble

Linder

2006

American Journal of Physiology-Cell Physiology

239

195

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mentioning

confidence: 56%

“…the degradation of ferritin induced by peroxide (27). Other in vitro and in vivo observations confirmed involvement of the 20 S proteasome in degradation of oxidized proteins and ferritin (36,38), and that ubiquitination and ATP are not required.…”

mentioning

confidence: 62%

Release of iron from ferritin requires lysosomal activity

Kidane

Sauble

Linder

2006

American Journal of Physiology-Cell Physiology

239

195

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“…Various studies indicated that the formation of large iron-rich ferritin particles, as a result of an increase in intracellular iron, results in the protection of ferritin molecules against degradation (Iancu, 1982;Truty et al, 2001;Worwood, 1982) and that iron-depleted ferritin is easily degraded Wixom et al, 1980). The 20S proteasome enzymatic system is responsible for the degradation of damaged intracellular proteins and can recognize specifically, and degrade, oxidized proteins (Mehlhase et al, 2005;Rudeck et al, 2000). The ferritin protein shell is confronted by a multitude of possible oxidative stressors.…”

Section: The Degradation Of Ferritinmentioning

confidence: 99%

“…The oxidation of Fe 2+ by the ferroxidase centre of the H-subunit results in the production of H 2 O 2 which could oxidize the protein shell, and the surrounding Fe 2+ can promote oxygen radical production by Fenton type chemistry. Oxidation of ferritin results in the loss of ferritin function and targeting of ferritin to the proteasome degradation system of the cell (Mehlhase et al, 2005;Rudeck et al, 2000). Oxidation of ferritin can also result in aggregation of ferritin molecules.…”

Section: The Degradation Of Ferritinmentioning

confidence: 99%

“…The formation of haemosiderin in reticuolendothelial cells and other macrophage-like cells are influenced by inflammatory and infectious conditions. Macrophages subjected to increased oxidative stress also degrade ferritin faster (Mehlhase et al, 2005). It is therefore suggested that during inflammatory and infectious conditions the proportion of poorly accessible (non-chelatable) iron associated with ferritin similarly increases, suggesting a pathway from non-ferritin iron, to loosely associated ferritin iron, to a well-sequestered non-chelatable form existing as haemo-siderin (Fahmy & Young, 1993).…”

Section: The Reticulo-endothelial Cell and Haemosiderin Formationmentioning

confidence: 99%

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Ferritin and ferritin isoforms I: Structure–function relationships, synthesis, degradation and secretion

Koorts

Viljoen

2007

Archives of Physiology and Biochemistry

134

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Ferritin is the intracellular protein responsible for the sequestration, storage and release of iron. Ferritin can accumulate up to 4500 iron atoms as a ferrihydrite mineral in a protein shell and releases these iron atoms when there is an increase in the cell's need for bioavailable iron. The ferritin protein shell consists of 24 protein subunits of two types, the H-subunit and the L-subunit. These ferritin subunits perform different functions in the mineralization process of iron. The ferritin protein shell can exist as various combinations of these two subunit types, giving rise to heteropolymers or isoferritins. Isoferritins are functionally distinct and characteristic populations of isoferritins are found depending on the type of cell, the proliferation status of the cell and the presence of disease. The synthesis of ferritin is regulated both transcriptionally and translationally. Translation of ferritin subunit mRNA is increased or decreased, depending on the labile iron pool and is controlled by an ironresponsive element present in the 5'-untranslated region of the ferritin subunit mRNA. The transcription of the genes for the ferritin subunits is controlled by hormones and cytokines, which can result in a change in the pool of translatable mRNA. The levels of intracellular ferritin are determined by the balance between synthesis and degradation. Degradation of ferritin in the cytosol results in complete release of iron, while degradation in secondary lysosomes results in the formation of haemosiderin and protection against iron toxicity. The majority of ferritin is found in the cytosol. However, ferritin with slightly different properties can also be found in organelles such as nuclei and mitochondria. Most of the ferritin produced intracellularly is harnessed for the regulation of iron bioavailability; however, some of the ferritin is secreted and internalized by other cells. In addition to the regulation of iron bioavailability ferritin may contribute to the control of myelopoiesis and immunological responses.

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Degradation and Accumulation of Oxidized Proteins in Age‐Related Diseases

Voss

Grune

2006

Redox Proteomics

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Oxidation-induced ferritin turnover in microglial cells: role of proteasome

Cited by 78 publications

References 75 publications

Release of iron from ferritin requires lysosomal activity

Release of iron from ferritin requires lysosomal activity

Ferritin and ferritin isoforms I: Structure–function relationships, synthesis, degradation and secretion

Degradation and Accumulation of Oxidized Proteins in Age‐Related Diseases

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