Specific binding of acidic isoferritins to erythroleukemia K562 cells.

An investigation of ferritin binding by human erythroleukemia K562 cells was prompted by recent studies suggesting that acidic isoferritins may act as regulators of granulopoiesis and hemopoiesis. Purified human heart and liver ferritins were labeled with iodine 125 and incubated with K562 cells at 37 degrees C. Specific uptake was calculated from the reduction in labeled ferritin binding in the presence of a 1000-fold excess of unlabeled ferritin. Specific uptake of 125I-labeled heart ferritin increased progressively, reaching a maximum after 2 to 3 hours' incubation, although nonspecific binding was too high to derive an affinity constant. There was no specific binding with 125I-labeled liver ferritin, and K562 cells bound neither 125I-labeled human serum albumin nor free 125I. Uptake of heart ferritin was negligible at 4 degrees C and was sharply reduced in the presence of 10% human plasma or fetal calf serum. There was no apparent relationship between the number of days of subculture and the level of uptake of acidic isoferritins by whole cells. These studies demonstrate a selective binding mechanism for acidic isoferritins on erythroleukemia cells and imply that these isoferritins have additional functions besides the storage of iron.