Sigma‐1 receptor antagonist ( BD ‐1063) potentiates the antinociceptive effect of quercetin in neuropathic pain induced by chronic constriction injury

2020 ◽  
Author(s):  
Josué Vidal Espinosa‐Juárez ◽  
Osmar Antonio Jaramillo‐Morales ◽  
Myrna Déciga‐Campos ◽  
Luis Alfonso Moreno‐Rocha ◽  
Francisco Javier López‐Muñoz
Keyword(s):  
Neuropathic Pain ◽  
Receptor Antagonist ◽  
Chronic Constriction Injury ◽  
Antinociceptive Effect ◽  
Sigma 1 Receptor ◽  
Sigma 1

216 A NEW SELECTIVE SIGMA-1 RECEPTOR ANTAGONIST (S1RA) REDUCES NEUROPATHIC PAIN BEHAVIORS AND ACTIVITY-INDUCED SPINAL SENSITISATION

2010 ◽  
Vol 4 (S1) ◽  
pp. 63-63 ◽  
Author(s):  
D. Zamanillo ◽  
L. Romero ◽  
J. Burgueño ◽  
X. Nadal ◽  
A. Dordal ◽  
...  
Keyword(s):  
Neuropathic Pain ◽  
Receptor Antagonist ◽  
Sigma 1 Receptor ◽  
Pain Behaviors ◽  
Sigma 1

188 A NEW SELECTIVE SIGMA-1 RECEPTOR ANTAGONIST (S1RA) INHIBITS THE DEVELOPMENT AND EXPRESSION OF NEUROPATHIC PAIN INDUCED BY PACLITAXEL IN MICE

2010 ◽  
Vol 4 (S1) ◽  
pp. 56-56
Author(s):  
F.R. Nieto ◽  
C.M. Cendan ◽  
J.M. Entrena ◽  
D. Zamanillo ◽  
J.M. Vela ◽  
...  
Keyword(s):  
Neuropathic Pain ◽  
Receptor Antagonist ◽  
Sigma 1 Receptor ◽  
Sigma 1

scholarly journals The Antinociceptive Effect of Sigma-1 Receptor Antagonist, BD1047, in a Capsaicin Induced Headache Model in Rats

2009 ◽  
Vol 13 (6) ◽  
pp. 425 ◽  
Author(s):  
Young Bae Kwon ◽  
Young Chan Jeong ◽  
Jung Kee Kwon ◽  
Ji Seon Son ◽  
Kee Won Kim
Keyword(s):  
Receptor Antagonist ◽  
Antinociceptive Effect ◽  
Sigma 1 Receptor ◽  
Sigma 1

scholarly journals The selective sigma-1 receptor antagonist E-52862 attenuates neuropathic pain of different aetiology in rats

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Georgia Gris ◽  
Enrique Portillo-Salido ◽  
Bertrand Aubel ◽  
Yassine Darbaky ◽  
Kristof Deseure ◽  
...  
Keyword(s):  
Neuropathic Pain ◽  
Receptor Antagonist ◽  
Sigma 1 Receptor ◽  
Sigma 1

scholarly journals The σ1 Receptor and the HINT1 Protein Control α2δ1 Binding to Glutamate NMDA Receptors: Implications in Neuropathic Pain

Biomolecules ◽  
2021 ◽  
Vol 11 (11) ◽  
pp. 1681
Author(s):  
María Rodríguez-Muñoz ◽  
Elsa Cortés-Montero ◽  
Yara Onetti ◽  
Pilar Sánchez-Blázquez ◽  
Javier Garzón-Niño
Keyword(s):  
Neuropathic Pain ◽  
Sciatic Nerve ◽  
Mechanical Allodynia ◽  
Chronic Constriction Injury ◽  
Intracerebroventricular Injection ◽  
Sigma 1 Receptor ◽  
Targeted Deletion ◽  
Σ1 Receptor ◽  
Sigma 1 ◽  
Glutamate Nmda Receptors

Nerve injury produces neuropathic pain through the binding of α2δ1 proteins to glutamate N-methyl-D-aspartate receptors (NMDARs). Notably, mice with a targeted deletion of the sigma 1 receptor (σ1R) gene do not develop neuropathy, whereas mice lacking the histidine triad nucleotide-binding protein 1 (Hint1) gene exhibit exacerbated allodynia. σ1R antagonists more effectively diminish neuropathic pain of spinal origin when administered by intracerebroventricular injection than systemically. Thus, in mice subjected to unilateral sciatic nerve chronic constriction injury (CCI), we studied the participation of σ1Rs and HINT1 proteins in the formation of α2δ1-NMDAR complexes within the supraspinal periaqueductal gray (PAG). We found that δ1 peptides required σ1Rs in order to interact with the NMDAR NR1 variant that contains the cytosolic C1 segment. σ1R antagonists or low calcium levels provoke the dissociation of σ1R-NR1 C1 dimers, while they barely affect the integrity of δ1-σ1R-NR1 C1 trimers. However, HINT1 does remove δ1 peptides from the trimer, thereby facilitating the subsequent dissociation of σ1Rs from NMDARs. In σ1R-/- mice, CCI does not promote the formation of NMDAR-α2δ1 complexes and allodynia does not develop. The levels of α2δ1-σ1R-NMDAR complexes increase in HINT1-/- mice and after inducing CCI, degradation of α2δ1 proteins is observed. Notably, σ1R antagonists but not gabapentinoids alleviate neuropathic pain in these mice. During severe neuropathy, the metabolism of α2δ1 proteins may account for the failure of many patients to respond to gabapentinoids. Therefore, σ1Rs promote and HINT1 proteins hinder the formation α2δ1-NMDAR complexes in the PAG, and hence, the appearance of mechanical allodynia depends on the interplay between these proteins.

Sign in / Sign up

Export Citation Format

Share Document