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

doi:10.1073/pnas.91.26.12994

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

School of Medicine

Research output: Contribution to journal › Article › peer-review

66 Scopus citations

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 language	English (US)
Pages (from-to)	12994-12998
Number of pages	5
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	91
Issue number	26
DOIs	https://doi.org/10.1073/pnas.91.26.12994
State	Published - Dec 20 1994

Keywords

GMP
N-methyl-D-aspartate
aconitase
ferritin
glutamate

ASJC Scopus subject areas

General

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10.1073/pnas.91.26.12994

Cite this

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

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.",

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T2 - A target for synaptic actions of nitric oxide

AU - Jaffrey, Samie R.

AU - Cohen, Noam A.

AU - Rouault, Tracey A.

AU - Klausner, Richard D.

AU - Snyder, Solomon H.

PY - 1994/12/20

Y1 - 1994/12/20

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AB - 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.

KW - GMP

KW - N-methyl-D-aspartate

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KW - ferritin

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

Abstract

Keywords

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