Please use this identifier to cite or link to this item: https://doi.org/10.1152/jn.01185.2004
Title: Differential mechanisms underlying the modulation of delayed-rectifier K+ channel in mouse neocortical neurons by nitric oxide
Authors: Han, N.-L.R. 
Ye, J.-S. 
Yu, A.C.H.
Sheu, F.-S. 
Issue Date: Apr-2006
Citation: Han, N.-L.R., Ye, J.-S., Yu, A.C.H., Sheu, F.-S. (2006-04). Differential mechanisms underlying the modulation of delayed-rectifier K+ channel in mouse neocortical neurons by nitric oxide. Journal of Neurophysiology 95 (4) : 2167-2178. ScholarBank@NUS Repository. https://doi.org/10.1152/jn.01185.2004
Abstract: The modulatory effects of nitric oxide (NO) on voltage-dependent K+ channels are intricate. In our present study, the augmentation and reduction of K+ currents by NO donor S-nitro-N-acetylpenicillamine (SNAP) and pure dissolved NO was observed in dissociated neurons from mice neocortex with both whole cell and cell-attached patch clamp. By using a specific electrochemical sensor, the critical concentrations of NO that increased or reduced the channel activities were accurately quantified. Low concentrations of SNAP (20 μM) or NO solution (0.1 μM) enhanced whole cell delayed rectifier K+-current (IK) and left the fast inactivating A current (IA) unchanged. However, high concentrations of SNAP (100 μM) and NO (0.5 μM) reduced both IK and IA currents. In cell-attached experiments, a significant increase in channel open probability (NP0) was observed when using low concentrations of SNAP or NO. High concentrations of SNAP or NO dramatically decreased NP0. The increase in channel activities by low concentrations of SNAP was abolished in the presence of either inhibitors of soluble guaylate cyclase or inhibitors of cGMP-dependent protein kinase G, suggesting a link to the NO-cGMP signaling cascade. The reduction of channel activities by high concentrations of SNAP was reversed by the reducing agent dithiothreitol, implying a redox reaction mechanism. Thus both NO-cGMP signaling and a redox mechanism are involved in the modulation of IK channel activity for neuron excitability. Copyright © 2006 The American Physiological Society.
Source Title: Journal of Neurophysiology
URI: http://scholarbank.nus.edu.sg/handle/10635/115675
ISSN: 00223077
DOI: 10.1152/jn.01185.2004
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

25
checked on Aug 22, 2019

WEB OF SCIENCETM
Citations

26
checked on Aug 22, 2019

Page view(s)

49
checked on Aug 16, 2019

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.