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  • 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.
    Author: Shin JS, Wang MH, Hwang SW, Cho H, Cho SY, Kwon MJ, Lee SY, Oh U.
    Journal: Neurosci Lett; 2001 Feb 16; 299(1-2):135-9. PubMed ID: 11166956.
    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.
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