Ferritin expression in maturing normal human erythroid precursors.

We studied the expression of H- and L-ferritin subunits at sequential stages of maturation of normal human erythroid precursors. The erythroid cells developed in liquid culture and were purified immunomagnetically before analysis. It was found that the content of both ferritin subunits decreased exponentially with maturation: the decrease was rapid when cellular haemoglobin was low, and it slowed down when the haemoglobin was increased. This mode of decline was especially pronounced for the L-subunits. The H-/L-subunit ratio did not change significantly during the investigated period. The synthesis of both subunits was equal at each given developmental stage, and declined significantly with maturation. However, this decline was just slightly faster than that of total protein synthesis. The data indicated that the degradation of H- and L-ferritin also declined as maturation proceeded. No decrease was observed in mRNA levels of either ferritin subunit. Thus, the ferritin content and turnover were maximal at the beginning of haemoglobin accumulation and diminished later. As the rate of ferritin turnover determines the rate of incorporation and release of its iron, the results presented suggest that ferritin mediates cellular iron transport and donates iron for haem synthesis, mainly at the beginning of haemoglobin accumulation. The synthesis of both ferritin subunits is regulated during erythroid maturation at the post-transcriptional level.