Selective modulation of heteromeric ASIC proton-gated channels by neuropeptide FF

Catarsi, Stefano; Babinski, K.; Séguéla, Philippe

doi:10.1016/s0028-3908(01)00107-1

Cited by 56 publications

(48 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, the peptides altered current generated by extracellular acidosis. The peptides slowed the desensitization rate following application of a low pH stimulus and in some cases they increased the peak current amplitude (Askwith et al 2000;Catarsi et al 2001). Consistent with these heterologous expression studies, FMRFamide also modulated endogenous H ϩ -gated currents in DRG neurons (Askwith et al 2000).…”

Section: Introductionsupporting

confidence: 66%

See 1 more Smart Citation

ASIC3 and ASIC1 Mediate FMRFamide-Related Peptide Enhancement of H⁺-Gated Currents in Cultured Dorsal Root Ganglion Neurons

Xie¹,

Price

Wemmie

et al. 2003

Journal of Neurophysiology

View full text Add to dashboard Cite

. ASIC3 and ASIC1 mediate FMRFamide-related peptide enhancement of H ϩ -gated currents in cultured dorsal root ganglion neurons. J Neurophysiol 89: 2459 -2465, 2003. First published January 22, 2003 10.1152/jn.00707.2002. 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 ϩ -gated currents. To better understand this potentiation, we examined the effect of FMRFamide-related peptides on DRG neurons from wildtype mice and animals missing individual ASIC subunits. We found that FMRFamide and FRRFamide potentiated H ϩ -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 ϩ -gated currents. These data suggest that FMRFamide-related peptides modulate DRG H ϩ -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 ϩ -gated current. We found that RFRP-1 slowed desensitization of H ϩ -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 ϩ -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 ϩ -gated currents suggest the possibility of substantial complexity in modulation of current in DRG sensory neurons.

show abstract

Section: Introductionsupporting

confidence: 66%

“…Interestingly, FMRFamide, NPFF, and the synthetic FRRFamide affected currents generated by heterologously expressed ASIC1 and ASIC3 channels (Askwith et al 2000;Catarsi et al 2001). None of these peptides activated ASIC channels on their own.…”

Section: Introductionmentioning

confidence: 96%

ASIC3 and ASIC1 Mediate FMRFamide-Related Peptide Enhancement of H⁺-Gated Currents in Cultured Dorsal Root Ganglion Neurons

Xie¹,

Price

Wemmie

et al. 2003

Journal of Neurophysiology

View full text Add to dashboard Cite

show abstract

“…As mentioned before, HyNaCs are indeed not activated by H + . However, ASICs are not activated by neuropeptides, but RFamide neuropeptides, including FMRFamide, can modulate the ASIC current (Askwith et al, 2000;Catarsi et al, 2001;Deval et al, 2003;Xie et al, 2003;Ostrovskaya et al, 2004;Chen et al, 2006;Sherwood and Askwith, 2008;Sherwood and Askwith, 2009). It is believed that neuropeptides directly bind to ASICs to modulate the H + -activated current.…”

Section: Relatives Of Ionotropic Rfamide Receptors In Bilateriamentioning

confidence: 99%

Peptide-gated ion channels and the simple nervous system of Hydra

Gründer

Assmann

2015

Journal of Experimental Biology

View full text Add to dashboard Cite

Neurons either use electrical or chemical synapses to communicate with each other. Transmitters at chemical synapses are either small molecules or neuropeptides. After binding to their receptors, transmitters elicit postsynaptic potentials, which can either be fast and transient or slow and longer lasting, depending on the type of receptor. Fast transient potentials are mediated by ionotropic receptors and slow long-lasting potentials by metabotropic receptors. Transmitters and receptors are well studied for animals with a complex nervous system such as vertebrates and insects, but much less is known for animals with a simple nervous system like Cnidaria. As cnidarians arose early in animal evolution, nervous systems might have first evolved within this group and the study of neurotransmission in cnidarians might reveal an ancient mechanism of neuronal communication. The simple nervous system of the cnidarian Hydra extensively uses neuropeptides and, recently, we cloned and functionally characterized an ion channel that is directly activated by neuropeptides of the Hydra nervous system. These results demonstrate the existence of peptide-gated ion channels in Hydra, suggesting they mediate fast transmission in its nervous system. As related channels are also present in the genomes of the cnidarian Nematostella, of placozoans and of ctenophores, it should be considered that the early nervous systems of cnidarians and ctenophores have co-opted neuropeptides for fast transmission at chemical synapses.

show abstract

“…Recent studies have demonstrated that the activities of ASICs can be modulated by various endogenous signaling molecules; for example, ASIC currents are potentiated by neurochemical components associated with tissue inflammation (Askwith et al, 2000;Catarsi et al, 2001;Mamet et al, 2002;Deval et al, 2003) and ischemia (Immke and McCleskey, 2001;Allen and Attwell, 2002). So far, the reported modulations by endogenous molecules almost exclusively enhance the activation of ASICs.…”

Section: Introductionmentioning

confidence: 99%

Subunit-Dependent High-Affinity Zinc Inhibition of Acid-Sensing Ion Channels

et al. 2004

View full text Add to dashboard Cite

Selective modulation of heteromeric ASIC proton-gated channels by neuropeptide FF

Cited by 56 publications

References 40 publications

ASIC3 and ASIC1 Mediate FMRFamide-Related Peptide Enhancement of H⁺-Gated Currents in Cultured Dorsal Root Ganglion Neurons

ASIC3 and ASIC1 Mediate FMRFamide-Related Peptide Enhancement of H⁺-Gated Currents in Cultured Dorsal Root Ganglion Neurons

Peptide-gated ion channels and the simple nervous system of Hydra

Subunit-Dependent High-Affinity Zinc Inhibition of Acid-Sensing Ion Channels

Contact Info

Product

Resources

About

Selective modulation of heteromeric ASIC proton-gated channels by neuropeptide FF

Cited by 56 publications

References 40 publications

ASIC3 and ASIC1 Mediate FMRFamide-Related Peptide Enhancement of H+-Gated Currents in Cultured Dorsal Root Ganglion Neurons

ASIC3 and ASIC1 Mediate FMRFamide-Related Peptide Enhancement of H+-Gated Currents in Cultured Dorsal Root Ganglion Neurons

Peptide-gated ion channels and the simple nervous system of Hydra

Subunit-Dependent High-Affinity Zinc Inhibition of Acid-Sensing Ion Channels

Contact Info

Product

Resources

About

ASIC3 and ASIC1 Mediate FMRFamide-Related Peptide Enhancement of H⁺-Gated Currents in Cultured Dorsal Root Ganglion Neurons

ASIC3 and ASIC1 Mediate FMRFamide-Related Peptide Enhancement of H⁺-Gated Currents in Cultured Dorsal Root Ganglion Neurons