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)

The rate of iron release from thioglycollate-elicited mouse peritoneal macrophages pulsed with 59Fe-labelled transferrin-antitransferrin immune complexes was lower than that from resident or Corynebacterium parvum-activated macrophages. Anaerobic conditions increased the rate of iron release by thioglycollate-elicited macrophages but had no effect on resident or C. parvum-activated macrophages. Thioglycollate-elicited macrophages also contained less ferritin and were deficient in their ability to synthesis ferritin. Incubation of these cells in medium containing 100 microM iron caused some increase in ferritin synthesis, but the response to iron was much less pronounced than that by resident or C. parvum-activated macrophages. In the thioglycollate-elicited macrophages, relatively less iron was incorporated into ferritin, and more into other soluble macromolecules and insoluble haemosiderin-like compounds than in the other types of macrophages. It is proposed that thioglycollate-elicited macrophages tend to divert iron to a relatively inert intracellular pool, and that this could account for their reduced ability to release iron. Such a mechanism might help to explain the reduced release of iron by liver and spleen macrophages occurring during inflammation.
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PMID:The relationship between iron release, ferritin synthesis and intracellular iron distribution in mouse peritoneal macrophages. Evidence for a reduced level of metabolically available iron in elicited macrophages. 369 81

The reductive mobilisation of iron from ferritin, the principal protein of iron storage, was studied. The kinetic characteristics of iron release by dithionite, thioglycollate, and dihydroriboflavin 5'-phosphate (FMNH2) were found to differ widely. The dependence on pH is most pronounced for the dithionite reduction which proceeds 100 times faster at pH 4 than at pH 7. The experimental data can be consistently explained in terms of specific interactions of products or educts with interfacial iron(III) hydroxide of the ferritin core. Surface complexes with the product sulfite are postulated in the dithionite reaction, and with the educt in the thioglycollate reaction. Iron(II) complexes with the radical anion FMN-. are suggested to be involved in the iron release by FMNH2. The mobilisation of iron by a series of thiols of different size and coordinative properties confirmed the importance of surface complex formation. No evidence was found for predominant effects of hindered shell penetration.
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PMID:Reductive mobilisation of ferritin iron. 404 77

Iron metabolism during inflammation was studied in normal and stimulated peritoneal mouse macrophages. A model was developed for detection of ferritin synthesis in these cells, and inflammatory stimulation was produced by i.p. injection of thioglycollate broth or i.m. injection of turpentine. The cells were adhered to culture discs and incubated at 37 degrees C with 59Fe-transferrin and 3H-leucine, and after washing the cell lysate was chromatographed. In the lysate from stimulated macrophages iron and tritium activity was found in a joint peak, and both were precipitated by a specific anti-mouse ferritin antibody. No significant peaks of radioactivity were found in lysates from normal cells. This showed that inflammatory RES cells have an increased ferritin synthesis. The uptake of 59Fe was investigated in a separate study and the stimulated macrophages were found to have a much higher iron uptake than normal macrophages.
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PMID:Increased ferritin synthesis and iron uptake in inflammatory mouse macrophages. 646 85

The cell surface of resident and thioglycolate-elicited mouse peritoneal macrophages was analysed using cell electrophoresis, ultrastructural cytochemistry and freeze-fracture. Both macrophages have a negative surface charge as evaluated by the binding of cationic particles (colloidal iron hydroxide and cationized ferritin) to the cell surface and determination of the cellular electrophoretic mobility (EPM). Elicited macrophages showed a more regular and intense binding of colloidal iron particles at pH 1.8 to their cell surfaces than resident macrophages. No differences were observed in the binding of cationized ferritin particles at pH 7.2 to the cell surface of resident and elicited macrophages. Both macrophages had the same mean EPM. Neuraminidase treatment of the cells did not interfere with the binding of cationic particles to the cell surface and with the EPM of the cells. With the freeze-fracture technique no special array of intramembranous particles was observed in the plasma membrane of the macrophages. Differences in the distribution of intramembranous particles in the P and E faces of the plasma membrane were observed between resident and elicited macrophages.
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PMID:Surface charge and ultrastructure of the cell surface of resident and thioglycolate-elicited mouse peritoneal macrophages. 665 67

A method of loading macrophages from normal and inflammatory mouse peritoneal exudates with 59Fe using 59Fe, 125I-transferrin-antitransferrin immune complexes is described and the subsequent release of iron and degraded transferrin to the incubation medium has been studied. Release of iron occurred more rapidly from resident macrophages than from thioglycollate broth-induced (stimulated) macrophages, but degradation of the 125I-transferrin in the immune complexes was faster in stimulated cells. A small percentage of the iron released was in the form of ferritin. Desferrioxamine (1 mM) increased the release of iron from both stimulated and resident macrophages, the effect being proportionally greater in the stimulated cells. Ascorbic acid (1 mM) had no effect on the release of iron, nor did the addition of apotransferrin (1 mg/ml) to the culture medium. These results support the concept of a blockade of iron release by reticuloendothelial cells in states of inflammation, and suggest that it may be a primary cause of the anaemia of chronic disease.
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PMID:Release of iron by resident and stimulated mouse peritoneal macrophages following ingestion and degradation of transferrin-antitransferrin immune complexes. 731 89