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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Adams, D. J. Nevin, S. T. Yasuda, T. Knapp, O. Lawrence, N. Lewis, R. J. |
| Description | Author Affiliation: Knapp O ( Health Innovations Research Institute, RMIT University, Melbourne, Vic, Australia.) |
| Abstract | BACKGROUND AND PURPOSE: Voltage-gated sodium channels are expressed primarily in excitable cells and play a pivotal role in the initiation and propagation of action potentials. Nine subtypes of the pore-forming -subunit have been identified, each with a distinct tissue distribution, biophysical properties and sensitivity to tetrodotoxin (TTX). Na(v) 1.8, a TTX-resistant (TTX-R) subtype, is selectively expressed in sensory neurons and plays a pathophysiological role in neuropathic pain. In comparison with TTX-sensitive (TTX-S) Na(v) -subtypes in neurons, Na(v) 1.8 is most strongly inhibited by the µO-conotoxin MrVIB from Conus marmoreus. To determine which domain confers Na(v) 1.8 -subunit its biophysical properties and MrVIB binding, we constructed various chimeric channels incorporating sequence from Na(v) 1.8 and the TTX-S Na(v) 1.2 using a domain exchange strategy. EXPERIMENTAL APPROACH: Wild-type and chimeric Na(v) channels were expressed in Xenopus oocytes, and depolarization-activated Naâ º currents were recorded using the two-electrode voltage clamp technique. KEY RESULTS: MrVIB (1 µM) reduced Na(v) 1.2 current amplitude to 69 ± 12%, whereas Na(v) 1.8 current was reduced to 31 ± 3%, confirming that MrVIB has a binding preference for Na(v) 1.8. A similar reduction in Naâ º current amplitude was observed when MrVIB was applied to chimeras containing the region extending from S6 segment of domain I through the S5-S6 linker of domain II of Na(v) 1.8. In contrast, MrVIB had only a small effect on Naâ º current for chimeras containing the corresponding region of Na(v) 1.2. CONCLUSIONS AND IMPLICATIONS: Taken together, these results suggest that domain II of Na(v) 1.8 is an important determinant of MrVIB affinity, highlighting a region of the -subunit that may allow further nociceptor-specific ligand targeting. |
| ISSN | 00071188 |
| e-ISSN | 14765381 |
| Journal | British Journal of Pharmacology |
| Issue Number | 7 |
| Volume Number | 166 |
| Language | English |
| Publisher | Wiley Online Library(on behalf of The British Pharmacological Society) |
| Publisher Date | 2012-08-01 |
| Publisher Place | Great Britain (UK) |
| Access Restriction | Open |
| Subject Keyword | Conotoxins Pharmacology NAV1.2 Voltage-Gated Sodium Channel Physiology NAV1.8 Voltage-Gated Sodium Channel Animals Cells, Cultured Oocytes Protein Subunits Tetrodotoxin Xenopus Laevis Research Support, Non-U.S. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Pharmacology |
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