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The Journal of Neuroscience, November 15, 2000, 20(22):8298-8304

Intracellular ATP Increases Capsaicin-Activated Channel Activity by Interacting with Nucleotide-Binding Domains

Jiyeon Kwak¹, Myeong Hyeon Wang¹, Sun Wook Hwang¹, Tae-Yoon Kim², Soon-Youl Lee¹, and Uhtaek Oh¹

¹ Sensory Research Group, Creative Research Initiatives, Seoul National University, College of Pharmacy, Kwanak, Shinlim San 56-1, Seoul 151-742, Korea, and ² Department of Immunology and Dermatology, College of Medicine, Catholic University, Seoul 137-040, Korea

Capsaicin (CAP)-activated ion channel plays a key role in generating nociceptive neural signals in sensory neurons. Here we present evidence that intracellular ATP upregulates the activity of capsaicin receptor channel. In inside-out membrane patches isolated from sensory neurons, application of CAP activated a nonselective cation channel (i_cap). Further addition of ATP to the bath caused a significant increase in i_cap, with a K_1/2 of 3.3 mM. Nonhydrolyzable analogs of ATP, adenylimidodiphosphate and adenosine 5'-O-(3-thio)-triphosphate, also increased i_cap. Neither Mg²⁺-free medium nor inhibitors of various kinases blocked the increase in i_cap induced by ATP. The enhancing effect of ATP was also observed in inside-out patches of oocytes expressing vanilloid receptor 1, a cloned capsaicin receptor. Single point mutations (D178N, K735R) within the putative Walker type nucleotide-binding domains abolished the effect of ATP. These results show that ATP increases i_cap in sensory neurons by direct interaction with the CAP channel without involvement of phosphorylation.

Key words: capsaicin receptor; VR1; ATP; allosteric regulation; nucleotide-binding motif; pain

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Copyright © 2000 Society for Neuroscience  0270-6474/00/20228298-07$05.00/0

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