Therapeutic Concentrations of Local Anaesthetics Unveil the Potential Role of Sodium Channels in Neuropathic Pain

2008 ◽  
pp. 189-205 ◽  
Author(s):  
Gary R. Strichartz ◽  
Zhongren Zhou ◽  
Catherine Sinnott ◽  
Alla Khodorova
Keyword(s):  
Neuropathic Pain ◽  
Sodium Channels ◽  
Potential Role ◽  
Local Anaesthetics

Increase of interleukin-6 mRNA in the spinal cord following peripheral nerve injury in the rat: potential role of IL-6 in neuropathic pain

1998 ◽  
Vol 62 (2) ◽  
pp. 228-235 ◽  
Author(s):  
Janice L Arruda ◽  
Raymond W Colburn ◽  
Amy J Rickman ◽  
Maria D Rutkowski ◽  
Joyce A DeLeo
Keyword(s):  
Spinal Cord ◽  
Neuropathic Pain ◽  
Peripheral Nerve ◽  
Nerve Injury ◽  
Interleukin 6 ◽  
Peripheral Nerve Injury ◽  
Potential Role

scholarly journals Neuropathic Pain Develops Normally in Mice Lacking both Nav1.7 and Nav1.8

2005 ◽  
Vol 1 ◽  
pp. 1744-8069-1-24 ◽  
Author(s):  
Mohammed A Nassar ◽  
Alessandra Levato ◽  
L Caroline Stirling ◽  
John N Wood
Keyword(s):  
Neuropathic Pain ◽  
Sodium Channels ◽  
Sensory Neurons ◽  
Inflammatory Pain ◽  
Pain Thresholds ◽  
Voltage Gated ◽  
Voltage Gated Sodium Channels ◽  
Pain Symptoms ◽  
Α Subunits

Two voltage gated sodium channel α-subunits, Nav1.7 and Nav1.8, are expressed at high levels in nociceptor terminals and have been implicated in the development of inflammatory pain. Mis-expression of voltage-gated sodium channels by damaged sensory neurons has also been implicated in the development of neuropathic pain, but the role of Nav1.7 and Nav1.8 is uncertain. Here we show that deleting Nav1.7 has no effect on the development of neuropathic pain. Double knockouts of both Nav1.7 and Nav1.8 also develop normal levels of neuropathic pain, despite a lack of inflammatory pain symptoms and altered mechanical and thermal acute pain thresholds. These studies demonstrate that, in contrast to the highly significant role for Nav1.7 in determining inflammatory pain thresholds, the development of neuropathic pain does not require the presence of either Nav1.7 or Nav1.8 alone or in combination.

The role of sodium channels in neuropathic pain

2006 ◽  
Vol 17 (5) ◽  
pp. 571-581 ◽  
Author(s):  
Marc Rogers ◽  
Lam Tang ◽  
David J. Madge ◽  
Edward B. Stevens
Keyword(s):  
Neuropathic Pain ◽  
Sodium Channels

scholarly journals The Potential Role of Intrathecal Nefopam in the Management of Neuropathic Pain

2014 ◽  
Vol 27 (3) ◽  
pp. 301 ◽  
Author(s):  
Mohamed Amin Ghobadifar ◽  
Navid Kalani
Keyword(s):  
Neuropathic Pain ◽  
Potential Role

The potential role of nerve growth factor in cryoneurolysis-induced neuropathic pain in rats

Cryobiology ◽  
2012 ◽  
Vol 65 (2) ◽  
pp. 132-138 ◽  
Author(s):  
Hui Ju ◽  
Yi Feng ◽  
Zhifeng Gao ◽  
Ba-Xian Yang
Keyword(s):  
Neuropathic Pain ◽  
Nerve Growth Factor ◽  
Growth Factor ◽  
Potential Role ◽  
Nerve Growth

Potential role of allopregnanolone for a safe and effective therapy of neuropathic pain

2014 ◽  
Vol 113 ◽  
pp. 70-78 ◽  
Author(s):  
C. Patte-Mensah ◽  
L. Meyer ◽  
O. Taleb ◽  
A.G. Mensah-Nyagan
Keyword(s):  
Neuropathic Pain ◽  
Potential Role ◽  
Effective Therapy

scholarly journals Direct, gabapentin-insensitive interaction of a soluble form of the calcium channel subunit α2δ-1 with thrombospondin-4

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Ehab El-Awaad ◽  
Galyna Pryymachuk ◽  
Cora Fried ◽  
Jan Matthes ◽  
Jörg Isensee ◽  
...  
Keyword(s):  
Neuropathic Pain ◽  
Potential Role ◽  
Binding Assay ◽  
Molecular Level ◽  
Biochemical Properties ◽  
Matrix Proteins ◽  
Soluble Form ◽  
Voltage Gated Calcium Channels ◽  
Thrombospondin 4

Abstract The α2δ‐1 subunit of voltage-gated calcium channels binds to gabapentin and pregabalin, mediating the analgesic action of these drugs against neuropathic pain. Extracellular matrix proteins from the thrombospondin (TSP) family have been identified as ligands of α2δ‐1 in the CNS. This interaction was found to be crucial for excitatory synaptogenesis and neuronal sensitisation which in turn can be inhibited by gabapentin, suggesting a potential role in the pathogenesis of neuropathic pain. Here, we provide information on the biochemical properties of the direct TSP/α2δ-1 interaction using an ELISA-style ligand binding assay. Our data reveal that full-length pentameric TSP-4, but neither TSP-5/COMP of the pentamer-forming subgroup B nor TSP-2 of the trimer-forming subgroup A directly interact with a soluble variant of α2δ-1 (α2δ-1S). Interestingly, this interaction is not inhibited by gabapentin on a molecular level and is not detectable on the surface of HEK293-EBNA cells over-expressing α2δ‐1 protein. These results provide biochemical evidence that supports a specific role of TSP-4 among the TSPs in mediating the binding to neuronal α2δ‐1 and suggest that gabapentin does not directly target TSP/α2δ-1 interaction to alleviate neuropathic pain.

Potential role of nitric oxide synthase isoforms in pathophysiology of neuropathic pain

2014 ◽  
Vol 22 (5) ◽  
pp. 269-278 ◽  
Author(s):  
Abhilasha Ahlawat ◽  
Ajay Rana ◽  
Nidhi Goyal ◽  
Saurabh Sharma
Keyword(s):  
Nitric Oxide ◽  
Neuropathic Pain ◽  
Nitric Oxide Synthase ◽  
Potential Role ◽  
Oxide Synthase
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