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Binding and uptake of exogenous isoferritins by cultured human erythroid precursor cells
Author(s) -
MeyronHoltz E. G.,
Fibach E.,
Gelvan D.,
Konijn A. M.
Publication year - 1994
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1994.tb04797.x
Subject(s) - ferritin , internalization , biochemistry , cytosol , biology , cell culture , binding site , extracellular , plasma protein binding , enzyme , receptor , chemistry , microbiology and biotechnology , genetics
Summary. The interaction of extracellular human isoferritins with normal erythroid precursors developing in a two‐phase liquid culture was studied. Cells at the stage of polychromatic normoblasts exhibited substantial specific binding of radio‐iodinated placental isoferritins. Considerably more acidic isoferritin was bound than basic isoferritin. The binding of ferritin was significantly higher at 37°C than at 4°C. All of the 125 I‐acidic isoferritin bound at 4°C, but only part of that bound at 37°C, could be dislodged by the addition of a 500‐fold excess of non‐labelled acidic isoferritin. Acidic isoferritin displaced radio‐iodinated acidic isoferritin from the erythroid cells more efficiently than intermediate or basic isoferritins. Kinetic analysis suggests a dissociation constant ( K d ) of 3·9 × 10 ‐8 m for acidic ferritin and 3·7 × 10 ‐7 m for basic isoferritin. The average number of binding sites for acidic isoferritin was 1·3 × 10 5 per cell. The results point to specific binding and receptor‐mediated internalization for predominantly acidic isoferritin by developing human erythroid cells.