Regulation of iron metabolism by oxalomalate

It has been investigatedin vitro the effect of oxalomalate (OMA) on the ferritin mRNA binding capacity of the bifunctional protein aconitase/IRP-1 contained in lysates of confluent cultures of 3T3-L1 fibroblasts. After short time of incubation with OMA at 37 °C, the gel mobility-shift analysis showed that the binding capacity of IRP-1 diminished and after 1 hour practically disappeared, indicating that the interaction of OMA with the aconitase counterpart reduced the aliquot of IRP-1 available to mRNA binding.