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)

1. The mechanism of the stimulation of ferritin synthesis by iron in vivo has been studied in rat liver. Ferritin synthesis and turnover was measured by [(14)C]leucine incorporation. 2. Actinomycin D had no inhibitory effect, after administration of iron, on [(14)C]leucine incorporation into ferritin but appeared to augment the effect of iron on ferritin synthesis. 3. Cycloheximide completely abolished the stimulation by iron of [(14)C]leucine into ferritin and was subsequently utilized to show that iron acts in vivo by translational induction of apoferritin synthesis, rather than by stabilization of apoferritin or its precursors. 4. This conclusion was confirmed by showing that 2 days after acute bleeding, when iron was in the process of being removed from hepatic ferritin stores, ferritin synthesis was decreased whereas breakdown rates were unchanged.
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PMID:Effect of actinomycin D, cycloheximide, and acute blood loss of ferritin synthesis in rat liver. 549 2

Neonatal (3 day old) rat oligodendrocytes grown in monolayer culture and exposed to increasingly hypoxic culture conditions showed increased Tran35S-label incorporation into a 22-kDa protein. Reoxygenation of cultures reversed the synthesis of the protein. Amino acid sequencing of a peptide derived from the purified protein revealed a 13 amino acid sequence with complete identity to a human heavy chain subunit of ferritin. This was confirmed by two-dimensional gel electrophoresis, immunoprecipitation, and western blot analysis with antiferritin antibody. In addition, hypoxia was able to induce the synthesis of ferritin in a cell line derived from human oligodendroglioma cells but not in astrocytes or neurons. Actinomycin D (1-15 micrograms/ml) treatment did not block the hypoxic induction of ferritin synthesis, whereas cycloheximide (1 microM) gave complete inhibition. Northern blot analysis showed that ferritin mRNA levels remained unchanged in both control and hypoxic oligodendrocytes and human oligodendroglioma cells, suggesting that the synthesis of ferritin was translationally rather than transcriptionally regulated by hypoxia. In neither oligodendrocytes nor the oligodendroglioma was there any cross-reaction with an antibody to alpha B-crystallin, the 22-kDa protein induced in astrocytes by various types of stress, further suggesting the specificity of hypoxic induction of ferritin in oligodendrocytes.
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PMID:Hypoxia specifically and reversibly induces the synthesis of ferritin in oligodendrocytes and human oligodendrogliomas. 793 1

Ferritin is an ubiquitous protein that has been shown to regulate cell differentiation in several experimental systems. In this study we have investigated the expression of ferritin genes encoding the heavy (H) and light (L) chains in t'B U937 cell line, induced to differentiate to macrophage-like cells by 12-O-tetradecanoylphorbol-13-acetate (TPA), retinoic acid (RA) or 1-beta-D-arabinofuranosylcytosine (Ara-C). An increase in the level of H ferritin mRNA was detected in U937 cells that had been incubated with Ara-C. Treatment of U937 cells with Actinomycin D suggested that the H ferritin mRNA increase was mediated by post-transcriptional mechanisms. The L ferritin mRNA level increased only following stimulation of U937 cells with RA. Immunophenotypic and cytochemical analyses showed that Ara-C was the strongest inducer of the macrophagic differentiation of U937 cells. These results suggest that the increase of H ferritin mRNA expression may represent a sensitive marker of myeloid cells differentiating along the monocyte-macrophage lineage.
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PMID:H and L ferritin gene expression in U937 cells induced to macrophage differentiation. 816 26

Ferritin synthesis is known to be regulated translationally by specific mRNA-protein interactions between an iron-responsive element (IRE) localized in the 5' untranslated region of ferritin mRNA and IRE-binding protein (IRE-BP). Binding of IRE-BP to IRE depresses its translation. In the present study, we demonstrated that ferritin synthesis in macrophages is strongly induced under hypoxic conditions by diethylmaleate, a sulfhydryl-reactive agent. The induction by diethylmaleate decreased as the oxygen tension rose. O2- is involved in this oxygen effect, because the induction was prevented when O2(-)-generating agents were present. Actinomycin D did not inhibit the ferritin synthesis induced by diethylmaleate under hypoxi. These results suggest that O2- is involved in post-transcriptional regulation of ferritin synthesis.
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PMID:Regulation of ferritin synthesis in macrophages by oxygen and a sulfhydryl-reactive agent. 819 99