The iron-responsive element binding protein: A target for synaptic actions of nitric oxide

Samie R. Jaffrey, Noam A. Cohen, Tracey A. Rouault, Richard D. Klausner, Solomon H. Snyder

Research output: Contribution to journalArticle

Abstract

Molecular targets for the actions of nitric oxide (NO) have only been partially clarified. The dynamic properties of the iron-sulfur (Fe-S) cluster of the iron responsive-element binding protein (IRE-BP) suggested that it might serve as a target for NO produced in response to glutamatergic stimulation in neurons. In the present study, we demonstrate that N-methyl- D-aspartate, acting through NO, stimulates the RNA-binding function of the IRE-BP in brain slices while diminishing its aconitase activity. In addition, we demonstrate a selective localization of the IRE-BP in discrete neuronal structures, suggesting a potential role for this protein in the response of neurons to NO.

Original languageEnglish (US)
Pages (from-to)12994-12998
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume91
Issue number26
DOIs
StatePublished - Dec 20 1994

Keywords

  • GMP
  • N-methyl-D-aspartate
  • aconitase
  • ferritin
  • glutamate

ASJC Scopus subject areas

  • General

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