Biomaterial Database

Regulation of ferritin synthesis and iron regulatory protein 1 by oxygen in mouse peritoneal macrophages. 1998

K Kuriyama-Matsumura, and H Sato, and M Yamaguchi, and S Bannai

Department of Biochemistry, University of Tsukuba, Ibaraki, Japan.

Ferritin is an intracellular iron storage protein whose synthesis is regulated post-transcriptionally by a mechanism that involves binding of cytoplasmic iron regulatory protein (IRP) to iron-responsive element (IRE) in the 5' untranslated region of ferritin mRNA. In this study, we have shown that in mouse peritoneal macrophages, the synthesis of ferritin was enhanced and the IRE binding activity of IRP-1 was diminished when the oxygen tension was decreased. Iron is known to induce ferritin synthesis and even in the presence of a low concentration of iron, synthesis of ferritin was enhanced and the activity of IRP-1 was decreased under hypoxia. The enhanced synthesis of ferritin under hypoxia was abolished by the addition of O2(-)-generating agents but not H2O2. The decreased activity of IRP-1 under hypoxia was reversed by adding O2(-)-generating agents. These data suggest that O2- generated in the cell is involved in alterations of ferritin synthesis and the activity of IRP-1 by oxygen.

UI	MeSH Term	Description	Entries
D007506	Iron-Sulfur Proteins	A group of proteins possessing only the iron-sulfur complex as the prosthetic group. These proteins participate in all major pathways of electron transport: photosynthesis, respiration, hydroxylation and bacterial hydrogen and nitrogen fixation.	Iron-Sulfur Protein,Iron Sulfur Proteins,Iron Sulfur Protein,Protein, Iron-Sulfur,Proteins, Iron Sulfur,Proteins, Iron-Sulfur,Sulfur Proteins, Iron
D010100	Oxygen	An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration.	Dioxygen,Oxygen-16,Oxygen 16
D002478	Cells, Cultured	Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.	Cultured Cells,Cell, Cultured,Cultured Cell
D005293	Ferritins	Iron-containing proteins that are widely distributed in animals, plants, and microorganisms. Their major function is to store IRON in a nontoxic bioavailable form. Each ferritin molecule consists of ferric iron in a hollow protein shell (APOFERRITINS) made of 24 subunits of various sequences depending on the species and tissue types.	Basic Isoferritin,Ferritin,Isoferritin,Isoferritin, Basic
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D016601	RNA-Binding Proteins	Proteins that bind to RNA molecules. Included here are RIBONUCLEOPROTEINS and other proteins whose function is to bind specifically to RNA.	Double-Stranded RNA-Binding Protein,Double-Stranded RNA-Binding Proteins,ds RNA-Binding Protein,RNA-Binding Protein,ds RNA-Binding Proteins,Double Stranded RNA Binding Protein,Double Stranded RNA Binding Proteins,Protein, Double-Stranded RNA-Binding,Protein, ds RNA-Binding,RNA Binding Protein,RNA Binding Proteins,RNA-Binding Protein, Double-Stranded,RNA-Binding Protein, ds,RNA-Binding Proteins, Double-Stranded,ds RNA Binding Protein
D017737	Macrophages, Peritoneal	Mononuclear phagocytes derived from bone marrow precursors but resident in the peritoneum.	Peritoneal Macrophages,Macrophage, Peritoneal,Peritoneal Macrophage
D051379	Mice	The common name for the genus Mus.	Mice, House,Mus,Mus musculus,Mice, Laboratory,Mouse,Mouse, House,Mouse, Laboratory,Mouse, Swiss,Mus domesticus,Mus musculus domesticus,Swiss Mice,House Mice,House Mouse,Laboratory Mice,Laboratory Mouse,Mice, Swiss,Swiss Mouse,domesticus, Mus musculus
D035925	Iron-Regulatory Proteins	Proteins that regulate cellular and organismal iron homeostasis. They play an important biological role by maintaining iron levels that are adequate for metabolic need, but below the toxicity threshold.	Iron Regulatory Factor,Iron Response Protein,IRE-BP,IRE-Binding Protein,Iron-Regulatory Protein,Iron-Response Proteins,Iron-Responsive Element Binding Proteins,Iron-Responsive Elements-Binding Protein,IRE Binding Protein,Iron Regulatory Protein,Iron Regulatory Proteins,Iron Response Proteins,Iron Responsive Element Binding Proteins,Iron Responsive Elements Binding Protein,Protein, Iron Response,Regulatory Factor, Iron,Response Protein, Iron
D035941	Iron Regulatory Protein 1	A multifunctional iron-sulfur protein that is both an iron regulatory protein and cytoplasmic form of aconitate hydratase. It binds to iron regulatory elements found on mRNAs involved in iron metabolism and regulates their translation. Its RNA binding ability and its aconitate hydrolase activity are dependent upon availability of IRON.	ACO1 Protein,Aconitase 1, Soluble,Ferritin Repressor Protein,IRE-BP1,IRP-1 Protein,IRP1 Protein,IRE BP1,IRP 1 Protein,Repressor Protein, Ferritin,Soluble Aconitase 1