Ferritin synthesis in differentiating Friend erythroleukemic cells.

We have investigated the regulation of ferritin synthesis during induction of Friend erythroleukemic cells by dimethyl sulfoxide. Northern blot analysis shows that mouse ferritin H and L mRNAs each contain approximately 1.1 kilobases. The levels of both mRNAs increase after addition of dimethyl sulfoxide in a biphasic manner. After a sharp rise in the first 6 h, the levels decline and then rise again over the next 90 h. These increases in mRNA levels reflect increased transcription of both mRNAs. Analysis of ferritin subunit synthesis surprisingly showed no corresponding increase in the rate of protein synthesis, suggesting that the additional mRNA was not in functional polysomes. These studies also indicated a novel processing of mouse ferritin H subunits. H subunits appear to be synthesized as a precursor of approximately 22,500. This form is not present in mature shells. Pulse-chase experiments indicated that the precursor is first processed to an intermediate form of 20,000 and then to the 18,000 component found in functional shells.