Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P02794 (ferritin)
 17,525 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Ferritin is the major protein for iron storage and iron detoxification. Since non-ferrous metals, such as aluminum, beryllium and zinc, are bound both in vivo and in vitro, ferritin is implicated as a general metal ion donor and detoxicant. The role of ferritin in Al and Be toxicity is discussed. During iron release ferritin produces free radicals which are involved in phosphoprotein inactivation, lipid peroxidation and, possibly, the general aging process. Conversely, during iron loading oxidative energy in the form of electrons and protons is given off. The different subunit compositions of ferritin, termed isoferritins, are, at least in part, involved with the multifunctionality of this protein.
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PMID:Ferritin: an iron storage protein with diverse functions. 307 74

A single diethylstilbestrol (DES) injection (5 mg DES/100 g body wt) was administrated to several lots (three specimens each) of adult male quail (Coturnix coturnix japonica). The birds were sacrificed 24, 48, 72 and 96 hr after the DES injection. A significant increase in liver weight and a clear drop in the hemoglobin concentration were observed after 24 hr. Later, a progressive rise was observed in plasma iron, total iron binding capacity, plasma copper and the phosphoprotein (vitellogenin), which reached highest values after 96 hr. In the liver, the iron showed an initial increase (24 hr), due to a rise in non-ferritin iron followed by a progressive decrease. Ferritin iron increased slowly but was significantly higher after 96 hr. This experimental model on male quail suggests an estrogen response in birds that could be more general and uniform than in mammals.
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PMID:Iron mobilization in estrogenized male quail. 614 35

Phosvitin, a phosphoprotein known as an iron-carrier in egg yolk, binds almost all the yolk iron. In this study, we investigated the effect of phosvitin on Fe(II)-catalyzed hydroxyl radical ((.-)OH) formation from H(2)O(2) in the Fenton reaction system. Using electron spin resonance (ESR) with 5,5-dimethyl-1-pyrroline-N-oxide (DMPO) and deoxyribose degradation assays, we observed by both assays that phosvitin more effectively inhibited (.-)OH formation than iron-binding proteins such as ferritin and transferrin. The effectiveness of phosvitin was related to the iron concentration, indicating that phosvitin acts as an antioxidant by chelating iron ions. Phosvitin accelerates Fe(II) autoxidation and thus decreases the availability of Fe(II) for participation in the (.-)OH-generating Fenton reaction. Furthermore, using the plasmid DNA strand breakage assay, phosvitin protected DNA against oxidative damage induced by Fe(II) and H(2)O(2). These results provide insight into the mechanism of protection of the developing embryo against iron-dependent oxidative damage in ovo.
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PMID:Egg yolk phosvitin inhibits hydroxyl radical formation from the fenton reaction. 1521 98