Open AccessThe iron-responsive element binding protein: a target for synaptic actions of nitric oxide.
Author(s) -
Samie R. Jaffrey,
Noam A. Cohen,
Tracey A. Rouault,
Richard D. Klausner,
Solomon H. Snyder
Publication year - 1994
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.91.26.12994
Subject(s) - aconitase , nitric oxide , glutamatergic , chemistry , biophysics , microbiology and biotechnology , biochemistry , stimulation , glutamate receptor , rna , neuroscience , biology , receptor , enzyme , organic chemistry , gene
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.