Title : Acidification of rat TRPV1 alters the kinetics of capsaicin responses.

Pub. Date : 2005 Sep 28

PMID : 16191202






9 Functional Relationships(s)
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1 Acidification of rat TRPV1 alters the kinetics of capsaicin responses. Capsaicin transient receptor potential cation channel, subfamily V, member 1 Rattus norvegicus
2 TRPV1 (vanilloid receptor 1) receptors are activated by a variety of ligands such as capsaicin, as well as by acidic conditions and temperatures above 42 degrees C. These activators can enhance the potency of one another, shifting the activation curve for TRPV1 to the left. Capsaicin transient receptor potential cation channel, subfamily V, member 1 Rattus norvegicus
3 TRPV1 (vanilloid receptor 1) receptors are activated by a variety of ligands such as capsaicin, as well as by acidic conditions and temperatures above 42 degrees C. These activators can enhance the potency of one another, shifting the activation curve for TRPV1 to the left. Capsaicin transient receptor potential cation channel, subfamily V, member 1 Rattus norvegicus
4 TRPV1 (vanilloid receptor 1) receptors are activated by a variety of ligands such as capsaicin, as well as by acidic conditions and temperatures above 42 degrees C. These activators can enhance the potency of one another, shifting the activation curve for TRPV1 to the left. Capsaicin transient receptor potential cation channel, subfamily V, member 1 Rattus norvegicus
5 In this study, for example, we observed an approximately 10-fold shift in the capsaicin EC50 (640 nM to 45 nM) for rat TRPV1 receptors expressed in HEK-293 cells when the pH was lowered from 7.4 to 5.5. Capsaicin transient receptor potential cation channel, subfamily V, member 1 Rattus norvegicus
6 When TRPV1 was maximally activated by capsaicin and acidic pH, the apparent affinity of the novel and selective capsaicin-site competitive TRPV1 antagonist, A-425619, was reduced approximately 35 fold. Capsaicin transient receptor potential cation channel, subfamily V, member 1 Rattus norvegicus
7 When TRPV1 was maximally activated by capsaicin and acidic pH, the apparent affinity of the novel and selective capsaicin-site competitive TRPV1 antagonist, A-425619, was reduced approximately 35 fold. Capsaicin transient receptor potential cation channel, subfamily V, member 1 Rattus norvegicus
8 When TRPV1 was maximally activated by capsaicin and acidic pH, the apparent affinity of the novel and selective capsaicin-site competitive TRPV1 antagonist, A-425619, was reduced approximately 35 fold. Capsaicin transient receptor potential cation channel, subfamily V, member 1 Rattus norvegicus
9 When TRPV1 was maximally activated by capsaicin and acidic pH, the apparent affinity of the novel and selective capsaicin-site competitive TRPV1 antagonist, A-425619, was reduced approximately 35 fold. Capsaicin transient receptor potential cation channel, subfamily V, member 1 Rattus norvegicus