Iron and transferrin distribution in reticulocytes incubated with heme synthesis inhibitors.
A high level of non-heme iron (either labelled or unlabelled) in mitochondria, ferritin and low-molecular-weight pool of reticulocytes was induced by preincubation with isonicotinic acid hydrazide or penicillamine together with either 59Fe- of 56Fe-labelled transferrin. Addition of apotransferrin during reincubation of 59Fe-labelled reticulocytes was accompanied by the transfer of 59Fe from low-molecular-weight pool to transferrin, which was found in the reticulocyte cytosol both free and bound to a carrier. Similarly, when cells were reincubated with 125I-labelled transferrin, more 125I-labelled radioactivity was found, in both free and carrier-bound transferrin peaks, in reticulocytes with a high level of low-molecular-weight cold iron than in control ones. These results suggest that transferrin enters reticulocytes and takes up iron from low-molecular-weight pool.
D000818:Animals; D006418:Heme / Q000096:biosynthesis; D007501:Iron / Q000097:blood*; D007538:Isoniazid / Q000494:pharmacology*; D007700:Kinetics; D010396:Penicillamine / Q000494:pharmacology*; D011817:Rabbits; D012156:Reticulocytes / Q000187:drug effects / Q000378:metabolism*; D014168:Transferrin / Q000378:metabolism*
D014168:Transferrin; D006418:Heme; D007501:Iron; D010396:Penicillamine; D007538:Isoniazid