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Expression of P2X5 receptors in the rat, cat, mouse and guinea pig dorsal root ganglion
Authors:Jun-Wei Zeng  Sai-Yu Cheng  Xiao-Hong Liu  Yan-Dong Zhao  Zhi Xiao  Geoffrey Burnstock  Huai-Zhen Ruan
Institution:1. Department of Neurobiology, Chongqing Key Laboratory of Neurobiology, Third Military Medical University, Chongqing, 400038, China
2. Department of Physiology, Zunyi Medical College, Zunyi, 563000, Guizhou province, China
3. Department of Neurology, Xin Qiao Hospital, Third Military Medical University, Chongqing, 400038, China
4. Autonomic Neuroscience Centre, University College Medical School, Royal Free Campus, Rowland Hill Street, London, NW3 2PF, UK
Abstract:P2X receptors are ATP-gated cationic channels composed of seven cloned subunits (P2X1 –7). P2X3 homomultimer and P2X2/3 heteromultimer receptors expressed by primary afferent dorsal root ganglion (DRG) neurons are involved in pain processing. The aim of the study was to investigate the expression of the P2X5 receptor subunit in DRG in different species including mouse, rat, cat and guinea pig. Immunohistochemistry showed that P2X5 receptors exhibited low levels of immunostaining in rat DRG, but high levels in mouse and guinea pig. Only a few neurons were immunoreactive for P2X5 receptors in cat. In mouse DRG, the P2X5 receptor was expressed largely by medium-diameter neurons (42.9 %), less in small (29.3 %) and large (27.8 %) neurons. In contrast, in the guinea pig DRG, P2X5 receptor expression was greatest in small-diameter (42.6 %), less in medium- (36.3 %) and large-diameter (21.1 %) neurons. Colocalization experiments revealed that, in mouse DRG, 65.5, 10.9 and 27.1 % of P2X5 receptors were immunoreactive for NF-200, CGRP and calbindin, while only a few P2X5-immunoreactive (IR) neurons were coexpressed with IB4 or with NOS. In guinea pig DRG, a total of 60.5 and 40.5 % of P2X5-IR neurons were coexpressed with IB4 or with CGRP, while 20.3 and 24.5 % of P2X5 receptors were coexpressed with NF-200 or with NOS. Only a few P2X5-IR neurons were coexpressed with calbindin in guinea pig DRG. It will be of great interest to clarify the relative physiological and pathophysiological roles of P2X5 receptors.
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