The incorporation of 59Fe, [3H]leucine and [32P]inorganic phosphate in ferritin during the perfusion of isolated rat livers

Kreel, B.K. van; Pijnenburg, A.M.C.M.; Eijk, H.G. Van; Leijnse, B.

doi:10.1016/0304-4165(72)90213-9

Cited by 9 publications

(2 citation statements)

References 7 publications

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“…This observation, together with the finding that some 77 % of the P1 is lost from the iron micelles when they are separated from their protein shells by alkali treatment (Granick & Hahn, 1944), suggests that a considerable proportion of the P1 is bound loosely at surface sites and is not an intimate part of the atomic structure of the microcrystalline particles. This suggestion is supported by experiments by Van Kreel et al (1972), who showed that the specific radioactivities of Pi in ferritin molecules of different Fe contents, isolated from livers perfused Vol. 171 with media containing [32P]P, were constant and equal to the specific radioactivity of the P1 remaining in supernatants of liver homogenates.…”

mentioning

confidence: 63%

Incorporation and release of inorganic phosphate in horse spleen ferritin

Trefry¹,

Harrison²

1978

Biochemical Journal

129

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When ferritin is reconstituted from Fe and apoferritin in vitro in the presence of Pi, the product obtained differs both from native ferritin and from ferritin reconstituted in the absence of Pi. When the latter is incubated with Pi the product resembles native ferritin with respect both to the pattern of Pi incorporated per molecule or per Fe atom and to the ease of release of this Pi relative to Fe release. It is concluded that much of the Pi of native ferritin is adsorbed on surfaces of ferritin iron-core crystallites. The results also suggest that Pi is not present at the intracellular site of Fe incorporation into ferritin, but is added after Fe.

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mentioning

confidence: 63%

Incorporation and release of inorganic phosphate in horse spleen ferritin

Trefry¹,

Harrison²

1978

Biochemical Journal

129

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“…Whether parenchymal cells were incubated with ferric citrate or with iron transferrin, in both cases only 1-2% of the iron-59 taken up by the cells was found to be incorporated into haem. Probably a large part of the iron taken up is incorporated into ferritin [25], In figure 2 the results with Chinese hamster fibroblasts are shown. Iron uptake in creases linearly for at least 3 h, whereas human 125I-transferrin binding reaches an equilibrium within 30 min, in agreement with the results of M essmer [29].…”

Section: Functional Heterogeneity Of Iron-binding Sitesmentioning

confidence: 98%

Functional Heterogeneity of Transferrin-Bound Iron

Verhoef¹,

Kottenhagen²,

Mulder³

et al. 1978

Acta Haematol

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According to the hypothesis of Fletcher and Huehns, functional differences exist between both iron-binding sites of transferrin. The site designated A should mainly be involved in the delivery of iron to erythroid cells, whereas site B should donate its iron preferentially to cells involved in the absorption and storage of iron. In the present study this hypothesis could be confirmed by in vitro experiments with various cell types. Iron transferrin preincubated with rat bone marrow cells donates less iron to rat bone marrow cells, Chinese hamster fibroblasts, human fibroblasts and human lymphoblasts than freshly prepared iron transferrin equal in iron and transferrin concentration. Rat liver parenchymal cells, however, take up more iron from preincubated than from freshly prepared iron transferrin. Obviously, site A not only donates iron preferentially to erythroid cells but also to (rapidly) dividing nonerythroid cells in culture. From experiments with iron transferrin mixtures in which radioiron was present at low or high iron saturation, it could be concluded that rat bone marrow cells take up iron equally well from monoferric as from diferric transferrin. The observed functional heterogeneity could, therefore, not be ascribed to differences between monoferric and diferric transferrin.

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The Structure and Function of Ferritin

Hoare

et al. 1977

Novartis Foundation Symposia

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The incorporation of 59Fe, [3H]leucine and [32P]inorganic phosphate in ferritin during the perfusion of isolated rat livers

Cited by 9 publications

References 7 publications

Incorporation and release of inorganic phosphate in horse spleen ferritin

Incorporation and release of inorganic phosphate in horse spleen ferritin

Functional Heterogeneity of Transferrin-Bound Iron

The Structure and Function of Ferritin

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