Oxalomalate, a competitive inhibitor of aconitase, modulates the RNA-binding activity of iron-regulatory proteins.

@article{Festa2000OxalomalateAC,
  title={Oxalomalate, a competitive inhibitor of aconitase, modulates the RNA-binding activity of iron-regulatory proteins.},
  author={Michela Festa and Alfredo Colonna and Concetta Pietropaolo and Alberto Ruffo},
  journal={The Biochemical journal},
  year={2000},
  volume={348 Pt 2},
  pages={315-20}
}
We investigated the effect of oxalomalate (OMA, alpha-hydroxy-beta-oxalosuccinic acid), a competitive inhibitor of aconitase, on the RNA-binding activity of the iron-regulatory proteins (IRP1 and IRP2) that control the post-transcriptional expression of various proteins involved in iron metabolism. The RNA-binding activity of IRP was evaluated by electrophoretic mobility-shift assay of cell lysates from 3T3-L1 mouse fibroblasts, SH-SY5Y human cells and mouse livers incubated in vitro with OMA… CONTINUE READING
9 Citations
30 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-9 of 9 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 30 references

Regulation of iron metabolism by oxalomalate

  • M. Festa, A. Colonna, C. Pietropaolo, A. Ruffo
  • Rend. Fis. Acc. Lincei s
  • 1999

Differential modulation of the RNA-binding proteins IRP-1 and IRP-2 in response to iron

  • L. C. hn
  • J. Biol
  • 1995

Iron regulates

  • B. Guo, J. D. Phillips, Y. Yu, E. A. Leibold
  • 1995

Similar Papers

Loading similar papers…