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TRPV1b overexpression negatively regulates TRPV1 responsiveness to capsaicin, heat and low pH in HEK293 cells.
J Neurochem. 2006 Nov; 99(4):1088-102.JN

Abstract

Transient receptor potential channel type V (TRPV) 1 is a non-selective cation channel that can be activated by capsaicin, endogenous vanilloids, heat and protons. The human TRPV1 splice variant, TRPV1b, lacking exon 7, was cloned from human dorsal root ganglia (DRG) RNA. The expression profile and relative abundance of TRPV1b and TRPV1 in 35 different human tissues were determined by quantitative RT-PCR using isoform-specific probes. TRPV1b was most abundant in fetal brain, adult cerebellum and DRG. Functional studies using electrophysiological techniques showed that recombinant TRPV1b was not activated by capsaicin (1 microM), protons (pH 5.0) or heat (50 degrees C). However, recombinant TRPV1b did form multimeric complexes and was detected on the plasma membrane of cells, demonstrating that the lack of channel function was not due to defects in complex formation or cell surface expression. These results demonstrate that exon 7, which encodes the third ankyrin domain and 44 amino acids thereafter, is required for normal channel function of human TRPV1. Moreover, when co-expressed with TRPV1, TRPV1b formed complexes with TRPV1, and inhibited TRPV1 channel function in response to capsaicin, acidic pH, heat and endogenous vanilloids, dose-dependently. Taken together, these data support the hypothesis that TRPV1b is a naturally existing inhibitory modulator of TRPV1.

Authors+Show Affiliations

Neuroscience Research, Global Pharmaceutical Research and Development, Abbott Laboratories, Abbott Park, Illinois 60064, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

17018028

Citation

Vos, Melissa H., et al. "TRPV1b Overexpression Negatively Regulates TRPV1 Responsiveness to Capsaicin, Heat and Low pH in HEK293 Cells." Journal of Neurochemistry, vol. 99, no. 4, 2006, pp. 1088-102.
Vos MH, Neelands TR, McDonald HA, et al. TRPV1b overexpression negatively regulates TRPV1 responsiveness to capsaicin, heat and low pH in HEK293 cells. J Neurochem. 2006;99(4):1088-102.
Vos, M. H., Neelands, T. R., McDonald, H. A., Choi, W., Kroeger, P. E., Puttfarcken, P. S., Faltynek, C. R., Moreland, R. B., & Han, P. (2006). TRPV1b overexpression negatively regulates TRPV1 responsiveness to capsaicin, heat and low pH in HEK293 cells. Journal of Neurochemistry, 99(4), 1088-102.
Vos MH, et al. TRPV1b Overexpression Negatively Regulates TRPV1 Responsiveness to Capsaicin, Heat and Low pH in HEK293 Cells. J Neurochem. 2006;99(4):1088-102. PubMed PMID: 17018028.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - TRPV1b overexpression negatively regulates TRPV1 responsiveness to capsaicin, heat and low pH in HEK293 cells. AU - Vos,Melissa H, AU - Neelands,Torben R, AU - McDonald,Heath A, AU - Choi,Won, AU - Kroeger,Paul E, AU - Puttfarcken,Pamela S, AU - Faltynek,Connie R, AU - Moreland,Robert B, AU - Han,Ping, PY - 2006/10/5/pubmed PY - 2007/1/11/medline PY - 2006/10/5/entrez SP - 1088 EP - 102 JF - Journal of neurochemistry JO - J. Neurochem. VL - 99 IS - 4 N2 - Transient receptor potential channel type V (TRPV) 1 is a non-selective cation channel that can be activated by capsaicin, endogenous vanilloids, heat and protons. The human TRPV1 splice variant, TRPV1b, lacking exon 7, was cloned from human dorsal root ganglia (DRG) RNA. The expression profile and relative abundance of TRPV1b and TRPV1 in 35 different human tissues were determined by quantitative RT-PCR using isoform-specific probes. TRPV1b was most abundant in fetal brain, adult cerebellum and DRG. Functional studies using electrophysiological techniques showed that recombinant TRPV1b was not activated by capsaicin (1 microM), protons (pH 5.0) or heat (50 degrees C). However, recombinant TRPV1b did form multimeric complexes and was detected on the plasma membrane of cells, demonstrating that the lack of channel function was not due to defects in complex formation or cell surface expression. These results demonstrate that exon 7, which encodes the third ankyrin domain and 44 amino acids thereafter, is required for normal channel function of human TRPV1. Moreover, when co-expressed with TRPV1, TRPV1b formed complexes with TRPV1, and inhibited TRPV1 channel function in response to capsaicin, acidic pH, heat and endogenous vanilloids, dose-dependently. Taken together, these data support the hypothesis that TRPV1b is a naturally existing inhibitory modulator of TRPV1. SN - 0022-3042 UR - https://www.unboundmedicine.com/medline/citation/17018028/TRPV1b_overexpression_negatively_regulates_TRPV1_responsiveness_to_capsaicin_heat_and_low_pH_in_HEK293_cells_ L2 - https://doi.org/10.1111/j.1471-4159.2006.04145.x DB - PRIME DP - Unbound Medicine ER -