Premium
Iron bound to low MW ligands: Interactions with mitochondria and cytosolic proteins
Author(s) -
Zhan Hui,
Gupta Raj K.,
Weaver Janet,
Pollack Simeon
Publication year - 1990
Publication title -
european journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.904
H-Index - 84
eISSN - 1600-0609
pISSN - 0902-4441
DOI - 10.1111/j.1600-0609.1990.tb00363.x
Subject(s) - cytosol , mitochondrion , biochemistry , chemistry , intracellular , ferritin , cellular compartment , cell , biophysics , enzyme , biology
The iron in the low MW pool of the cell is the precursor of iron in haem and is bound primarily to ATP. This precursor‐product relationship suggested that reticulocytes might accumulate ATP‐iron if their haem synthesis were blocked. However reticulocytes, treated with succinyl‐acetone or rotenone and taking up iron from transferrin, accumulated iron in nonhaem cytosolic proteins and in mitochondria and not in the low MW pool. This was demonstrated by NMR and also by disrupting the cell with shear stress, separating the cytosol and pellet and fractionating the cytosol with ammonium sulfate. This constancy of the low MW iron pool in the face of blocked haem synthesis could not be explained by saturation of cytosolic ATP or by sluggish exchange of the low MW pool with other compartments. Rather, nonhaem cytosolic proteins and mitochondria appeared to have a higher affinity for iron and to exchange it rapidly with that in the low MW pool.