This study identifies the iron-responsive element binding protein (IRE-BP) as a molecular target for the synaptic actions of nitric oxide in neurons.
Provides molecular target for NO synaptic actions; leaves open in vivo validation and clinical relevance.
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.
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Jaffrey et al. (1994) studied this question.