Differences in sensitivity of vanilloid receptor 1 transfected to human embryonic kidney cells and capsaicin-activated channels in cultured rat dorsal root ganglion neurons to capsaicin receptor agonists

Jae Soo Shin, Myeong Hyeon Wang, Sun Wook Hwang, Hawon Cho, So Yeon Cho, Mi Jeong Kwon, Soon Youl Lee, Uhtaek Oh

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

Heterologously expressed vanilloid receptor 1 (VR1), a cloned cDNA encoding for capsaicin (CAP)-sensitive currents, resembles the native CAP channels in cultured sensory neurons in channel property. But, the pharmacological profile of VR1 to various CAP analogs is not known. The stable expression of VR1 in human embryonic kidney (HEK) cells was generated and confirmed by reverse transcription-polymerase chain reaction and Western blots. VR1 expressed in HEK cells retained single-channel properties similar to those of the native channels. When concentration-response relationships were compared, CAP and DA-5018·HCl, a synthetic analog of CAP, exhibited a greater potency in activating VR1 than the native channels in sensory neurons. In contrast, resiniferatoxin and its analog, phorbol 12-phenylacetate 13-acetate 20-homovanillate, was more potent in activating the CAP-activated channels in cultured sensory neurons than VR1. Thus, the difference in pharmacological profiles of VR1 and the native channels suggests the possible presence of subtypes of the CAP receptor or regulatory mechanisms associated with VR1.

Original languageEnglish
Pages (from-to)135-139
Number of pages5
JournalNeuroscience Letters
Volume299
Issue number1-2
DOIs
Publication statusPublished - 2001 Feb 16
Externally publishedYes

Fingerprint

TRPV Cation Channels
Capsaicin
Spinal Ganglia
Kidney
Neurons
Sensory Receptor Cells
Pharmacology
vanilloid receptor subtype 1
Reverse Transcription
Complementary DNA
Western Blotting
Polymerase Chain Reaction

Keywords

  • Capsaicin
  • Capsaicin receptor
  • DA-5018
  • Dorsal root ganglion
  • Pain
  • Phorbol 12-phenylacetate 13-acetate 20-homovanillate
  • Resiniferatoxin
  • Vanilloid receptor 1

ASJC Scopus subject areas

  • Neuroscience(all)

Cite this

Differences in sensitivity of vanilloid receptor 1 transfected to human embryonic kidney cells and capsaicin-activated channels in cultured rat dorsal root ganglion neurons to capsaicin receptor agonists. / Shin, Jae Soo; Wang, Myeong Hyeon; Hwang, Sun Wook; Cho, Hawon; Cho, So Yeon; Kwon, Mi Jeong; Lee, Soon Youl; Oh, Uhtaek.

In: Neuroscience Letters, Vol. 299, No. 1-2, 16.02.2001, p. 135-139.

Research output: Contribution to journalArticle

@article{30e384901ce141978523d913b7d81b63,
title = "Differences in sensitivity of vanilloid receptor 1 transfected to human embryonic kidney cells and capsaicin-activated channels in cultured rat dorsal root ganglion neurons to capsaicin receptor agonists",
abstract = "Heterologously expressed vanilloid receptor 1 (VR1), a cloned cDNA encoding for capsaicin (CAP)-sensitive currents, resembles the native CAP channels in cultured sensory neurons in channel property. But, the pharmacological profile of VR1 to various CAP analogs is not known. The stable expression of VR1 in human embryonic kidney (HEK) cells was generated and confirmed by reverse transcription-polymerase chain reaction and Western blots. VR1 expressed in HEK cells retained single-channel properties similar to those of the native channels. When concentration-response relationships were compared, CAP and DA-5018·HCl, a synthetic analog of CAP, exhibited a greater potency in activating VR1 than the native channels in sensory neurons. In contrast, resiniferatoxin and its analog, phorbol 12-phenylacetate 13-acetate 20-homovanillate, was more potent in activating the CAP-activated channels in cultured sensory neurons than VR1. Thus, the difference in pharmacological profiles of VR1 and the native channels suggests the possible presence of subtypes of the CAP receptor or regulatory mechanisms associated with VR1.",
keywords = "Capsaicin, Capsaicin receptor, DA-5018, Dorsal root ganglion, Pain, Phorbol 12-phenylacetate 13-acetate 20-homovanillate, Resiniferatoxin, Vanilloid receptor 1",
author = "Shin, {Jae Soo} and Wang, {Myeong Hyeon} and Hwang, {Sun Wook} and Hawon Cho and Cho, {So Yeon} and Kwon, {Mi Jeong} and Lee, {Soon Youl} and Uhtaek Oh",
year = "2001",
month = "2",
day = "16",
doi = "10.1016/S0304-3940(00)01777-8",
language = "English",
volume = "299",
pages = "135--139",
journal = "Neuroscience Letters",
issn = "0304-3940",
publisher = "Elsevier Ireland Ltd",
number = "1-2",

}

TY - JOUR

T1 - Differences in sensitivity of vanilloid receptor 1 transfected to human embryonic kidney cells and capsaicin-activated channels in cultured rat dorsal root ganglion neurons to capsaicin receptor agonists

AU - Shin, Jae Soo

AU - Wang, Myeong Hyeon

AU - Hwang, Sun Wook

AU - Cho, Hawon

AU - Cho, So Yeon

AU - Kwon, Mi Jeong

AU - Lee, Soon Youl

AU - Oh, Uhtaek

PY - 2001/2/16

Y1 - 2001/2/16

N2 - Heterologously expressed vanilloid receptor 1 (VR1), a cloned cDNA encoding for capsaicin (CAP)-sensitive currents, resembles the native CAP channels in cultured sensory neurons in channel property. But, the pharmacological profile of VR1 to various CAP analogs is not known. The stable expression of VR1 in human embryonic kidney (HEK) cells was generated and confirmed by reverse transcription-polymerase chain reaction and Western blots. VR1 expressed in HEK cells retained single-channel properties similar to those of the native channels. When concentration-response relationships were compared, CAP and DA-5018·HCl, a synthetic analog of CAP, exhibited a greater potency in activating VR1 than the native channels in sensory neurons. In contrast, resiniferatoxin and its analog, phorbol 12-phenylacetate 13-acetate 20-homovanillate, was more potent in activating the CAP-activated channels in cultured sensory neurons than VR1. Thus, the difference in pharmacological profiles of VR1 and the native channels suggests the possible presence of subtypes of the CAP receptor or regulatory mechanisms associated with VR1.

AB - Heterologously expressed vanilloid receptor 1 (VR1), a cloned cDNA encoding for capsaicin (CAP)-sensitive currents, resembles the native CAP channels in cultured sensory neurons in channel property. But, the pharmacological profile of VR1 to various CAP analogs is not known. The stable expression of VR1 in human embryonic kidney (HEK) cells was generated and confirmed by reverse transcription-polymerase chain reaction and Western blots. VR1 expressed in HEK cells retained single-channel properties similar to those of the native channels. When concentration-response relationships were compared, CAP and DA-5018·HCl, a synthetic analog of CAP, exhibited a greater potency in activating VR1 than the native channels in sensory neurons. In contrast, resiniferatoxin and its analog, phorbol 12-phenylacetate 13-acetate 20-homovanillate, was more potent in activating the CAP-activated channels in cultured sensory neurons than VR1. Thus, the difference in pharmacological profiles of VR1 and the native channels suggests the possible presence of subtypes of the CAP receptor or regulatory mechanisms associated with VR1.

KW - Capsaicin

KW - Capsaicin receptor

KW - DA-5018

KW - Dorsal root ganglion

KW - Pain

KW - Phorbol 12-phenylacetate 13-acetate 20-homovanillate

KW - Resiniferatoxin

KW - Vanilloid receptor 1

UR - http://www.scopus.com/inward/record.url?scp=0035895716&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035895716&partnerID=8YFLogxK

U2 - 10.1016/S0304-3940(00)01777-8

DO - 10.1016/S0304-3940(00)01777-8

M3 - Article

C2 - 11166956

AN - SCOPUS:0035895716

VL - 299

SP - 135

EP - 139

JO - Neuroscience Letters

JF - Neuroscience Letters

SN - 0304-3940

IS - 1-2

ER -