Ferritin mitochondrial

Deferoxamine is isolated from Streptomycespilosus. It binds iron avidly but essential trace metals poorly. Furthermore, while competing for loosely bound iron in iron-carrying proteins (hemosiderin and ferritin), it fails to compete for biologically chelated iron, as in microsomal and mitochondrial cytochromes and hemoproteins. Consequently, it is the chelator of choice for iron poisoning (Chapters 33 and 59). Deferoxamine plus hemodialysis may also be useful in the treatment of aluminum toxicity in renal failure. Deferoxamine is poorly absorbed when administered orally and may increase iron absorption when given by this route. It should therefore be administered intramuscularly or, preferably, intravenously. It is believed to be metabolized, but the pathways are unknown. The iron-chelator complex is excreted in the urine, often turning the urine an orange-red color. 

Lovell MA, Robertson ID, Teesdale WJ, Campbell JL, Markesbery WR (1998) Copper, iron and zinc in Alzheimer s disease senile plaques. J Neurol Sci 158 47-52 Lu Z, Nie G, Li Y, Soe-Lin S, Tao Y, Cao Y, Zhang Z, Liu N, Ponka P, Zhao B (2009) Overexpression of Mitochondrial Ferritin Sensitizes Cells to Oxidative Stress Via an Iron-Mediated Mechanism. Antioxid Redox Signal 11(8) 1791-1803 Luchsinger JA, Tang MX, Shea S, Mayeux R (2003) Antioxidant vitamin intake and risk of Alzheimer disease. Arch Neurol 60 203-208... 

The shorter chains of the 82- to 86-residue cytochromes C550 (from Pseudomonas ), 6553, " and C555 (from Chlorohiumd ) as well as the longer 112-residue polypeptide of cytochrome C2 from Rhodospirillum rubrum have nearly the same folding pattern as that in mitochondrial cytochrome c. However, the 128-residue chain of the dimeric cytochrome c from Rhodospirillum molischianum forms an antiparallel four-helix bundle (Fig. 16-8). This is the same folding pattern present in the ferritin monomer (Fig. 16-3), hemerythrin (Fig. 2-22), and many other proteins including cytochrome 562 of E. coli ° Cytochrome/, which functions in photosynthetic electron transport, is also a c-type cytochrome but with a unique protein fold. ... 

Figure 8-2 Posttranscriptional regulation by IRE/IRP interactions. In iron-replete cells, IRPs do not bind to IREs. Iron starvation induces IRPs to bind to their ligands, resulting in stabilization of transferrin receptor mRNA and translational inhibition of the mRNAs encoding ferritin H- and L-chain), eALAS and mitochondrial aconitase.

Antibodies. — A new volume of Methods in Enzymology covers the preparation and use of affinity-labelled immunoglobulins. The specialized procedures required for the preparation of ferritin-antibody conjugates have been reviewed and the use of the conjugates for the localization of enzymes in mitochondrial membranes discussed. 

Crystal structures for a number of ferritins and bacterioferritins from different sources have become available, and have recently been reviewed [448], These structures include those for ferritins from horse spleen, bullfrog, the H subunit and the mitochondrial form from human, the L subunits from horse and mouse, as well as for bacterioferritin from E. coli, Rhodobacter capsulatus, and D. desulfuricans ATCC 27774 [433,447,449-462], In addition, the crystal structures of ferritins from the halophile Halobacterium salinarium, from S. solfataricus, from the hyperthermophilic archaeon Archaeoglobus fulgidus, and from Azotobacter vinelandii have recently been solved [463-467], Each ferritin subunit independent of source and type is folded into a characteristic four a-helix bundle (each helix 27 A long). 

Storage and recycling Ferritin (H, L and M) Heme oxygenase 1 (HO-1) Cytosolic and mitochondrial Fe storage protein Microsomal protein functioning in recycling Hb iron... 

The recent discovery of mitochondrial ferritin (MtFt) has contributed to our understanding of mitochondrial iron metabolism and sideroblastic anemia. 

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