The role of ferritin in the intracellular distribution of gallium 67.
The binding of gallium 67 or iron 59 to ferritin in vitro was investigated using equilibrium dialysis. Gallium 67 did not bind to apo-ferritin until the protein was transformed into ferritin in the presence of iron citrate. Apotransferrin inhibited the binding of 67Ga to ferritin, especially in the presence of sodium bicarbonate and citrate, thus indicating that 67Ga has not gained access to ferritin from its complex with transferrin. Similar inhibition was observed for ferritin-59Fe. The release of 59Fe from its transferrin complex was enhanced by ATP, citrate, or ascorbic acid, while these reagents did not stimulate the dissociation of 67Ga from its transferrin complex. On the other hand, 67Ga injected intravenously in vivo was not found in the ferritin fractions of rat liver, kidney, and tumor. The difference between experimental results in vivo and in vitro supports the hypothesis that 67Ga in the cytoplasm is not labile enough to be bound to ferritin. We have indicated a significant role of ferritin in distinguishing between 67Ga and 59Fe in the cell, and provided some clues to interpret the chemical forms of 67Ga in the cytoplasm.
D000818:Animals; D001052:Apoferritins / Q000378:metabolism; D001059:Apoproteins; D002286:Carcinoma, Ehrlich Tumor / Q000378:metabolism; D003864:Depression, Chemical; D005260:Female; D005293:Ferritins / Q000378:metabolism*; D005710:Gallium Radioisotopes / Q000378:metabolism*; D007504:Iron Radioisotopes / Q000378:metabolism*; D051381:Rats; D014168:Transferrin / Q000494:pharmacology
D001059:Apoproteins; D005710:Gallium Radioisotopes; D007504:Iron Radioisotopes; D014168:Transferrin; C028284:apotransferrin; D005293:Ferritins; D001052:Apoferritins