ArticlePflugers Archiv : European journal of physiology2015
Heterologous expression of NaV1.9 chimeras in various cell systems.
Article in Pflugers Archiv : European journal of physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 35 citations in OpenAlex.
- A robust expression system reveals distinct gating mechanisms and calmodulin regulation of NaScience advances · 2025Article
- Nociceptor sodium channels shape subthreshold phase, upstroke, and shoulder of action potentials.The Journal of general physiology · 2025Article
- Pharmacological activity and NMR solution structure of the leech peptide HSTX-I.Biochemical pharmacology · 2020Article
- Discovery of a selective, state-independent inhibitor of NaScientific reports · 2020Article
- Characterization of Synthetic Tf2 as a NaBiomedicines · 2020Article
- A 49-residue sequence motif in the C terminus of Nav1.9 regulates trafficking of the channel to the plasma membrane.The Journal of biological chemistry · 2020Article
- NaV1.6 and NaV1.7 channels are major endogenous voltage-gated sodium channels in ND7/23 cells.PloS one · 2019Article
- Voltage gated sodium channels as therapeutic targets for chronic pain.Journal of pain research · 2019Review
- Duplex signaling by CaM and Stac3 enhances CaThe Journal of general physiology · 2018Article
- Modulation of sodium channels as pharmacological tool for pain therapy-highlights and gaps.Naunyn-Schmiedeberg's archives of pharmacology · 2018Review
- A Chimeric NaV1.8 Channel Expression System Based on HEK293T Cell Line.Frontiers in pharmacology · 2018Article
- Breaking barriers to novel analgesic drug development.Nature reviews. Drug discovery · 2017Review
- Electrophysiological and Pharmacological Analyses of NaFrontiers in pharmacology · 2017Article
- Optical electrophysiology for probing function and pharmacology of voltage-gated ion channels.eLife · 2016Article
- Characterization of Endogenous Sodium Channels in the ND7-23 Neuroblastoma Cell Line: Implications for Use as a Heterologous Ion Channel Expression System Suitable for Automated Patch Clamp Screening.Assay and drug development technologies · 2016Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SCN11A encodes the voltage-gated sodium channel NaV1.9, which deviates most strongly from the other eight NaV channels expressed in mammals. It is characterized by resistance to the prototypic NaV channel blocker tetrodotoxin and exhibits slow activation and inactivation gating. Its expression in dorsal root ganglia neurons suggests a role in motor or pain signaling functions as also recently demonstrated by the occurrence of various mutations in human SCN11A leading to altered pain sensation syndromes. The systematic investigation of human NaV1.9, however, is severely hampered because of very poor heterologous expression in host cells. Using patch-clamp and two-electrode voltage-clamp methods, we show that this limitation is caused by the C-terminal structure of NaV1.9. A chimera of NaV1.9 harboring the C terminus of NaV1.4 yields functional expression not only in neuronal cells but also in non-excitable cells, such as HEK 293T or Xenopus oocytes. The major functional difference of the chimeric channel with respect to NaV1.9 is an accelerated activation and inactivation. Since the entire transmembrane domain is preserved, it is suited for studying pharmacological properties of the channel and the functional impact of disease-causing mutations. Moreover, we demonstrate how mutation S360Y makes NaV1.9 channels sensitive to tetrodotoxin and saxitoxin and that the unusual slow open-state inactivation of NaV1.9 is also mediated by the IFM (isoleucine-phenylalanine-methionine) inactivation motif located in the linker connecting domains III and IV.
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