scholarly journals Anomalous mole–fraction effects in recombinant and native cyclic nucleotide–gated channels in rat olfactory receptor neurons

2001 ◽  
Vol 268 (1474) ◽  
pp. 1395-1403 ◽  
Author(s):  
W. Qu ◽  
A. J. Moorhouse ◽  
A. M. Cunningham ◽  
P. H. Barry
Keyword(s):  
Mole Fraction ◽  
Cyclic Nucleotide ◽  
Olfactory Receptor ◽  
Olfactory Receptor Neurons ◽  
Cyclic Nucleotide Gated Channels ◽  
Receptor Neurons

Divalent cations block the cyclic nucleotide-gated channel of olfactory receptor neurons

1993 ◽  
Vol 69 (5) ◽  
pp. 1758-1768 ◽  
Author(s):  
F. Zufall ◽  
S. Firestein
Keyword(s):  
Cyclic Amp ◽  
Calcium Channels ◽  
Cyclic Nucleotide ◽  
Olfactory Receptor ◽  
Single Channel ◽  
Divalent Cations ◽  
Olfactory Receptor Neurons ◽  
Gated Channel ◽  
Receptor Neurons ◽  
Single Channel Currents

1. The effects of external divalent cations on odor-dependent, cyclic AMP-activated single-channel currents from olfactory receptor neurons of the tiger salamander (Ambystoma tigrinum) were studied in inside-out membrane patches taken from dendritic regions of freshly isolated sensory cells. 2. Channels were reversibly activated by 100 microM cyclic AMP. In the absence of divalent cations, the channel had a linear current-voltage relation giving a conductance of 45 pS. With increasing concentrations of either Ca2+ or Mg2+ in the external solution, the channel displayed a rapid flickering behavior. At higher concentrations of divalent cations, the transitions were too rapid to be fully resolved and appeared as a reduction in mean unitary single-channel current amplitude. 3. This effect was voltage dependent, and on analysis was shown to be due to an open channel block by divalent ions. In the case of Mg2+, the block increased steadily with hyperpolarization. In contrast, for Ca2+ the block first increased with hyperpolarization and then decreased with further hyperpolarization beyond -70 mV, providing evidence for Ca2+ permeation of this channel. 4. This block is similar to that seen in voltage-gated calcium channels. Additionally, the cyclic nucleotide-gated channel shows some pharmacological similarities with L-type calcium channels, including a novel block of the cyclic nucleotide channel by nifedipine (50 microM). 5. Our results indicate that the sensory generator current simultaneously depends on the presence of the second messenger and on the membrane potential of the olfactory neuron.

Both External and Internal Calcium Reduce the Sensitivity of the Olfactory Cyclic-Nucleotide-Gated Channel to cAMP

1999 ◽  
Vol 81 (6) ◽  
pp. 2675-2682 ◽  
Author(s):  
Steven J. Kleene
Keyword(s):  
Cyclic Nucleotide ◽  
Olfactory Receptor ◽  
Electrical Signal ◽  
Olfactory Receptor Neurons ◽  
Unexpected Result ◽  
Patch Clamp Recording ◽  
Ciliary Membrane ◽  
Gated Channel ◽  
Receptor Neurons ◽  
Internal Calcium

Both external and internal calcium reduce the sensitivity of the olfactory cyclic-nucleotide-gated channel to cAMP. In vertebrate olfaction, odorous stimuli are first transduced into an electrical signal in the cilia of olfactory receptor neurons. Many odorants cause an increase in ciliary cAMP, which gates cationic channels in the ciliary membrane. The resulting influx of Ca2+ and Na+ produces a depolarizing receptor current. Modulation of the cyclic-nucleotide-gated (CNG) channels is one mechanism of adjusting olfactory sensitivity. Modulation of these channels by divalent cations was studied by patch-clamp recording from single cilia of frog olfactory receptor neurons. In accord with previous reports, it was found that cytoplasmic Ca2+ above 1 μM made the channels less sensitive to cAMP. The effect of cytoplasmic Ca2+ was eliminated by holding the cilium in a divalent-free cytoplasmic solution and was restored by adding calmodulin (CaM). An unexpected result was that external Ca2+ could also greatly reduce the sensitivity of the channels to cAMP. This reduction was seen when external Ca2+ exceeded 30 μM and was not affected by the divalent-free solution, by CaM, or by Ca2+ buffering. The effects of cytoplasmic and external Ca2+ were additive. Thus the effects of cytoplasmic and external Ca2+ are apparently mediated by different mechanisms. There was no effect of CaM on a Ca2+-activated Cl− current that also contributes to the receptor current. Increases in Ca2+ concentration on either side of the ciliary membrane may influence olfactory adaptation.

scholarly journals 3-Phosphoinositides Modulate Cyclic Nucleotide Signaling in Olfactory Receptor Neurons

Neuron ◽  
2002 ◽  
Vol 33 (5) ◽  
pp. 731-739 ◽  
Author(s):  
Marc Spehr ◽  
Christian H. Wetzel ◽  
Hanns Hatt ◽  
Barry W. Ache
Keyword(s):  
Cyclic Nucleotide ◽  
Olfactory Receptor ◽  
Olfactory Receptor Neurons ◽  
Receptor Neurons ◽  
Nucleotide Signaling

Cyclic Nucleotide-Activated Currents in Cultured Olfactory Receptor Neurons of the Hawkmoth Manduca sexta

2008 ◽  
Vol 100 (5) ◽  
pp. 2866-2877 ◽  
Author(s):  
Steffi Krannich ◽  
Monika Stengl
Keyword(s):  
Manduca Sexta ◽  
Cyclic Nucleotide ◽  
Olfactory Receptor ◽  
Low Voltage ◽  
Cyclic Adenosine Monophosphate ◽  
Adenosine Monophosphate ◽  
Guanosine Monophosphate ◽  
Olfactory Receptor Neurons ◽  
Cation Channels ◽  
Receptor Neurons

Moth pheromones cause rises in intracellular Ca2+ concentrations that activate Ca2+-dependent cation channels in antennal olfactory receptor neurons. In addition, mechanisms of adaptation and sensitization depend on changes in cyclic nucleotide concentrations. Here, cyclic nucleotide-activated currents in cultured olfactory receptor neurons of the moth Manduca sexta are described, which share properties with currents through vertebrate cyclic nucleotide-gated channels. The cyclic nucleotide-activated currents of M. sexta carried Ca2+ and monovalent cations. They were directly activated by cyclic adenosine monophosphate (cAMP) and cyclic guanosine monophosphate (cGMP), modulated by Ca2+/calmodulin, and inhibited by lanthanum. M. sexta cyclic nucleotide-activated currents developed in an all-or-none manner, which suggests that the underlying channels are coupled and act coordinately. At least one cAMP- and two cGMP-activated nonselective cation currents could be distinguished. Compared with the cAMP-activated current, both cGMP-activated currents appeared to conduct more Ca2+ and showed a stronger down-regulation by Ca2+/calmodulin-dependent negative feedback. Furthermore, both cGMP-activated currents differed in their Ca2+-dependent inhibition. Thus M. sexta olfactory receptor neurons, like vertebrate sensory neurons, appear to express nonselective cyclic nucleotide-activated cation channels with different subunit compositions. Besides the nonselective cyclic nucleotide-activated cation currents, olfactory receptor neurons express a cAMP-dependent current. This current resembled a protein kinase-modulated low-voltage–activated Ca2+ current.

Sign in / Sign up

Export Citation Format

Share Document