Reactive oxygen species and iron—a dangerous partnership in inflammation

Local administration of transcription factor decoy oligonucleotides to nuclear factor-κB prevents carrageenin-induced inflammation in rat hind paw

“…The mechanism of NF-B activation may depend on the release of several mediators, including reactive oxygen species which appear to play a central role in the inflammatory response. 49 Recent study has shown that the removal of O − 2 , by recombinant human Cu/Zn superoxide dismutase coupled to polyethyleneglycol, significantly inhibited carrageenin-induced rat paw edema. 4 Such reactive oxygen species may act as intracellular second messengers via activation of the inactive cytoplasmic form of NF-B by the release of the inhibitory subunit I B␣.…”

Ferritina sérica e coronariopatia obstrutiva: correlação angiográfica

“…Most of this content, approximately 70% of it, is found in the heme compounds (markedly in hemoglobin and myoglobin). Around 30% remains as iron stores as ferritin and hemossiderin and only 0.1% or less is found in plasma, bound to the transport protein transferrin 1 …”

“…It is the fourth most abundant chemical element on Earth and the most abundant transition metal in living organisms. It is involved in oxygen transportation, transference of electrons, DNA synthesis, oxidation processes by oxygen and hydrogen peroxide (H 2 O 2 ) and in many others, keeping the normal structure and function of virtually all mammal cells 1 . The total body iron content is approximately 50 mg/kg of weight in normal adult men and 35 mg/kg of weight in women.…”

“…By regulating the "pool" of free intracellular iron, ferritin controls the generation of reactive-oxygen species catalyzed by iron, thus working as an anti-oxidant. On the other hand, Cairo et al 1 showed, in rats submitted to oxidative stress by the administration of phorone, a glutathione-depleting drug, that initially there is a decrease in the amount of ferritin, indicating that part of the iron participating in the free "pool" derives from ferritin itself, which under these circumstances works as a pro-oxidant. Actually, the initial degradation contributes to the expansion of free intracellular iron, which later activates multiple molecular mechanisms to reconstitute ferritin, therefore limiting the pro-oxidant effect.…”

“…There is, however, an association between the stored iron, intracellular, and the secreted one, in a way that the plasma ferritin concentration reflects the amount of ferritin inside the cell. It is estimated that 1 µg/l of serum ferritin is equivalent to approximately 10 mg of stored iron 1 .…”