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

Three of the most plausible biological theories of arsenic carcinogenesis are protein binding, oxidative stress and altered DNA methylation. This review presents the role of trivalent arsenicals binding to proteins in arsenic carcinogenesis. Using vacuum filtration based receptor dissociation binding techniques, the lifetimes of unidentate (<1s), bidentate (1-2min) and tridentate (1-2h) arsenite containing peptide binding complexes were estimated. According to our experimental data some of the protein targets to which arsenite may bind in vivo include tubulin, poly(ADP-ribose)polymerase (PARP-1), thioredoxin reductase, estrogen receptor-alpha, arsenic(+3)methyltransferase and Keap-1. Arsenite binding to tubulin can lead to several of the genetic effects observed after arsenic exposures (aneuploidy, polyploidy and mitotic arrests). Among many other possible arsenite binding sites are rat hemoglobin, the DNA repair enzyme xeroderma pigmentosum protein A (XPA), and other C2H2, C3H and C4 zinc finger proteins including members of the steroid receptor superfamily (e.g. glucocorticoid receptor). Macromolecules to which arsenite does not bind to include calf thymus DNA, mixed Type II-A histones and bovine H3/H4 histone. Although all six tested arsenicals released iron from ferritin, radioactive arsenite did not bind to the protein horse ferritin.
 ...
PMID:The role of protein binding of trivalent arsenicals in arsenic carcinogenesis and toxicity. 1816 70

In the nitrogen fixation process, iron plays a vital role by being part of many symbiotic proteins, such as nitrogenase and leghemoglobin, in an active symbiosis. Excess or insufficient iron in active nitrogen fixation negatively affects the entire process. In Lotus japonicus nodules, ferritin is expressed at the initial stages of nodule development and increases at the nodule senescence stage to mobilize iron release during that stage. In this study, we investigated the effects of overexpressing and suppressing ferritin on nitrogen fixation. Acetylene reduction activity revealed that nitrogen fixation is affected by the overexpression of ferritin at high iron concentrations, but at low iron concentrations, higher nitrogen fixation was observed in ferritin-suppressed plants. qRT-PCR data indicated that suppression of ferritin in nodules induces antioxidant genes, such as superoxide dismutase, dehydroascorbate reductase and ascorbate peroxidase, to detoxify reactive oxygen species. Our data suggest that suppressing ferritin in the nodules is effective for higher nitrogen fixation under iron deficient conditions. Overaccumulated ferritin in nodule is effective under the higher iron conditions, such as senescence state.
 ...
PMID:Effect of ferritin on nitrogen fixation in Lotus japonicus nodules under various iron concentrations. 3276 83