A common inhibitory binding site for zinc and odorants at the voltage-gated K+ channel of rat olfactory receptor neurons

Seebungkert, B and Lynch, JW (2001) A common inhibitory binding site for zinc and odorants at the voltage-gated K+ channel of rat olfactory receptor neurons. European Journal of Neuroscience, 14 2: 353-362.


Author Seebungkert, B
Lynch, JW
Title A common inhibitory binding site for zinc and odorants at the voltage-gated K+ channel of rat olfactory receptor neurons
Journal name European Journal of Neuroscience   Check publisher's open access policy
Publication date 2001
Sub-type Article
DOI 10.1046/j.0953-816x.2001.01646.x
Volume number 14
Issue number 2
ISSN 0953-816X
Start page 353
End page 362
Total pages 10
Editor B.J. Everitt
Place of publication United Kingdom
Publisher Blackwell Science
Collection year 2001
Language eng
Subject C1
320600 Medical Physiology
780105 Biological sciences
Abstract This study compared the effects of zinc and odorants on the voltage-gated K+ channel of rat olfactory neurons. Zinc reduced current magnitude, depolarized the voltage activation curve and slowed activation kinetics without affecting inactivation or deactivation kinetics. Zinc inhibition was potentiated by the NO compound, S-nitroso-cysteine. The pH- and diethylpyrocarbonate-dependence of zinc inhibition suggested that zinc acted by binding to histidine residues. Cysteine residues were eliminated as contributing to the zinc-binding site. The odorants, acetophenone and amyl acetate, also reduced current magnitude, depolarized the voltage activation curve and selectively slowed activation kinetics. Furthermore, the diethylpyrocarbonate- and pH-dependence of odorant inhibition implied that the odorants also bind to histidine residues. Zinc inhibitory potency was dramatically diminished in the presence of odorants, implying competition for a common binding site. These observations indicate that the odorants and zinc share a common inhibitory binding site on the external surface of the voltage-gated K+ channel.
Keyword Neurosciences
Cysteine
Diethylpyrocarbonate
Histidine
Metal Binding Site
Nitric Oxide
Olfactory Transduction
Potassium Channels
Necturus-maculosus
Divalent-cations
Induced Response
Carbon-monoxide
Cells
Suppression
Modulation
Currents
Kinetics
Q-Index Code C1

Document type: Journal Article
Sub-type: Article
Collection: School of Biomedical Sciences Publications
 
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Created: Tue, 14 Aug 2007, 16:50:04 EST