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The Journal of Neuroscience, April 1, 1998, 18(7):2342-2349
Nitric Oxide Depresses GABAA Receptor Function via Coactivation of cGMP-Dependent Kinase and Phosphodiesterase
Eric M. Wexler1, 2, Patric K. Stanton2, 3, and Scott Nawy1, 2 Departments of 1 Ophthalmology and Visual Science, 2 Neuroscience, and 3 Neurology, Albert Einstein College of Medicine, Bronx, New York 10461
Nitric oxide (NO) is thought to play an essential role in neuronal processing, but the downstream mechanisms of its action remain unclear. We report here that NO analogs reduce GABA-gated currents in cultured retinal amacrine cells via two distinct, but convergent, cGMP-dependent pathways. Either extracellular application of the NO-mimetic S-nitroso-N-acetyl-penicillamine (SNAP) or intracellular perfusion with cGMP depressed GABA currents. This depression was partially blocked by a pseudosubstrate peptide inhibitor of cGMP-dependent protein kinase (PKG), suggesting both PKG-dependent and independent actions of cGMP. cAMP-dependent protein kinase (PKA) is known to enhance retinal GABA responses. 8-Bromoinosine 3',5'-cyclic monophosphate (8Br-cIMP), which activates a type of cGMP-stimulated phosphodiesterase that hydrolyzes cAMP, also significantly reduced GABA currents. 1-Methyl-3-isobutylxanthine (IBMX), a nonspecific phosphodiesterase (PDE) inhibitor, blocked both the action of 8Br-cIMP and the portion of SNAP-induced depression that was not blocked by PKG inhibition. Our results suggest that NO depresses retinal GABAA receptor function by simultaneously upregulating PKG and downregulating PKA.
Key words: retina; amacrine; culture; nitric oxide; guanylate cyclase; ODQ; SNAP; PKG inhibitory peptide
Copyright © 1998 Society for Neuroscience 0270-6474/98/1872342-08$05.00/0
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