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Query: UNIPROT:P02794 (
ferritin
)
17,525
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
In vitro cultured myocardial cells from newborn rats were shown to be a good model system for the study of iron uptake and iron metabolism.
Ferric ammonium citrate
was readily taken up by cells, and about 50% of it was sequestered in
ferritin
. The rate of iron uptake and/or accumulation in the cells was proportional to its concentration in the medium at 30, 60, and 90 microM but was reduced at 180 microM. At 360 microM iron both the rate of uptake and the total iron taken up was less than at 90 microM iron. Electron-microscopic examination showed endocytotic vesicles and lysosomes containing iron-filled
ferritin
molecules, as well as normal morphology. In both control and experimental cultures there was an increase with time in the number of lysosomes; however, in the control cultures there were considerably fewer molecules of
ferritin
seen per lysosome than in experimentals. The number of
ferritin
molecules apparent in lysosomes increased with time and with increasing concentrations of iron in the medium.
...
PMID:Electron-microscopic and radioiron studies of iron uptake in newborn rat myocardial cells in vitro. 746 65
Ferritin is the major intracellular iron storage protein which has been shown to protect cells against oxidative damage. Recent reports that an inherited abnormality in human
ferritin
synthesis is associated with early bilateral cataracts underscore the importance of understanding
ferritin
synthesis and iron storage in lens epithelial cells. We previously demonstrated that ascorbic acid greatly increases de novo synthesis of
ferritin
in lens epithelial cells. The objectives of the present study were to determine: (1) the effects of ascorbic acid and ferric ammonium citrate on iron uptake by canine lens epithelial cells from iron bound to transferrin and from ferric chloride and (2) the incorporation of this element into
ferritin
. Iron uptake by lens epithelial cells from 59ferric chloride was 20 times higher than from 59iron-transferrin and iron deposition into
ferritin
was 8-fold higher when 59ferric chloride was the source. Ascorbic acid had a stimulatory effect on iron uptake from transferrin and on incorporation of this element into
ferritin
. The ascorbic acid-induced increase of iron uptake required de novo protein synthesis but not specifically de novo
ferritin
biosynthesis. Although
ferritin
is not directly involved in iron uptake, the level of
ferritin
protein could control the pool of intracellular iron. The present results indicate that iron homeostasis in lens epithelial cells is affected mainly by changes in
apoferritin
synthesis, which is greatly stimulated by ascorbic acid, rather than by altering the rate of protein degradation, which is very slow in these cells under all circumstances.
Ferric ammonium citrate
activates iron uptake from transferrin in a wide range of cell lines by generation of free radicals.
Ferric ammonium citrate
also increased iron uptake from Tf in lens epithelial cells.
Ferric ammonium citrate
treated cells incorporated 5 times more iron and deposited 2 times more iron into
ferritin
than control cells. Increased incorporation of iron into
ferritin
was due to ferric ammonium citrate-induced stimulation of de novo
ferritin
synthesis rather than an increased rate of iron deposition into pre-existing
ferritin
.
Ferric ammonium citrate
had a different effect on iron uptake from ferric chloride; total iron uptake was not significantly increased while deposition into
ferritin
was significantly decreased. These results demonstrate that iron homeostasis in lens epithelial cells is regulated by ascorbic acid and by changes in the rate of de novo
ferritin
synthesis. In addition, the differences in iron uptake from transferrin and ferric chloride and its subsequent incorporation into
ferritin
suggests that the mechanisms by which iron is incorporated into
ferritin
are source dependent.
...
PMID:The effect of ascorbic acid and ferric ammonium citrate on iron uptake and storage in lens epithelial cells. 965 1