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J Neurophysiol (May 1, 2003). 10.1152/jn.00707.2002
Submitted on Submitted 20 August 2002; accepted in final form 13 January 2003
1Howard Hughes Medical Institute, Roy J. and Lucille A. Carver College of Medicine, Departments of 2Internal Medicine, 3Physiology and Biophysics, and 4Psychiatry, University of Iowa; and 5Department of Veterans Affairs Medical Center, Iowa City, Iowa 52242
Xie, Jinghui,
Margaret
P. Price,
John A. Wemmie,
Candice C. Askwith, and
Michael J. Welsh.
ASIC3 and ASIC1 Mediate FMRFamide-Related Peptide Enhancement of
H+-Gated Currents in Cultured Dorsal Root Ganglion Neurons. J. Neurophysiol. 89: 2459-2465, 2003. The acid-sensing ion channels (ASICs) form cation channels that
are transiently activated by extracellular protons. They are expressed
in dorsal root ganglia (DRG) neurons and in the periphery where they
play a function in nociception and mechanosensation. Previous studies
showed that FMRFamide and related peptides potentiate H+-gated currents. To better understand this potentiation,
we examined the effect of FMRFamide-related peptides on DRG neurons
from wild-type mice and animals missing individual ASIC subunits. We
found that FMRFamide and FRRFamide potentiated H+-gated
currents of wild-type DRG in a dose-dependent manner. They increased
current amplitude and slowed desensitization following a proton
stimulus. Deletion of ASIC3 attenuated the response to FMRFamide-related peptides, whereas the loss of ASIC1 increased the
response. The loss of ASIC2 had no effect on FMRFamide-dependent enhancement of H+-gated currents. These data suggest that
FMRFamide-related peptides modulate DRG H+-gated currents
through an effect on both ASIC1 and ASIC3 and that ASIC3 plays the
major role. The recent discovery of RFamide-related peptides (RFRP) in
mammals suggested that they might also modulate H+-gated
current. We found that RFRP-1 slowed desensitization of H+-gated DRG currents, whereas RFRP-2 increased the peak
amplitude. COS-7 cells heterologously expressing ASIC1 or ASIC3 showed
similar effects. These results suggest that FMRFamide-related peptides, including the newly identified RFRPs, modulate H+-gated DRG
currents through ASIC1 and ASIC3. The presence of several ASIC
subunits, the diversity of FMRFamide-related peptides, and the distinct
effects on H+-gated currents suggest the possibility of
substantial complexity in modulation of current in DRG sensory neurons.
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