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The Journal of Neurophysiology Vol. 88 No. 1 July 2002, pp. 544-548
Copyright ©2002 by the American Physiological Society
RAPID COMMUNICATION
1Department of Anesthesiology and Resuscitology, Nagoya City University Medical School, Nagoya 467-0001; 2Department of Neural Regulation, Research Institute of Environmental Medicine, Nagoya University, Nagoya 464-8601; and 3Department of Physiology, Mie University School of Medicine, Tsu 514-8507, Japan
Sugiura, Takeshi,
Makoto Tominaga,
Hirotada Katsuya, and
Kazue Mizumura.
Bradykinin Lowers the Threshold Temperature for Heat Activation
of Vanilloid Receptor 1. J. Neurophysiol. 88: 544-548, 2002. Bradykinin (BK) is an inflammatory
mediator that plays a pivotal role in pain and hyperalgesia to heat in
inflamed tissues by exciting nociceptors and sensitizing them to heat
through activation of protein kinase C (PKC). It has been suggested
that the capsaicin receptor (VR1), a nociceptor-specific cation channel
sensitive to noxious heat, protons, and capsaicin, is a channel that
is modified by BK in these effects. In this study, we
examined how BK modulates the activity of VR1. We measured VR1 currents
using the patch-clamp technique in human embryonic kidney-derived
(HEK293) cells expressing VR1 and B2 BK receptor. We found that BK
lowered the threshold temperature for activation of VR1 currents in HEK cells down to well below the physiological body temperature in a
concentration-dependent manner through PKC activation. We also demonstrated that in capsaicin-sensitive dorsal root ganglion (DRG)
neurons the activation threshold of heat-induced current, which is
considered to be VR-1 mediated, was lowered by BK and that this effect
was also mediated by PKC. These data further support the supposition
that modulation of VR1 is a mechanism for the BK-induced excitation of
nociceptors and their sensitization to heat.
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