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      A P2X purinoceptor expressed by a subset of sensory neurons.

      Nature
      Amino Acid Sequence, Animals, Blotting, Northern, Cell Line, Cells, Cultured, Cloning, Molecular, Electrophysiology, In Situ Hybridization, Molecular Sequence Data, Neurons, Afferent, metabolism, Oocytes, PC12 Cells, Rats, Receptors, Purinergic P2, biosynthesis, genetics, Receptors, Purinergic P2X3, Sequence Homology, Amino Acid, Xenopus

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          Abstract

          ATP is known to depolarize sensory neurons, and may play a role in nociceptor activation when released from damaged tissue. Here we report the molecular cloning and characterization of a new member of the P2X receptor family, P2X3, expressed by these cells. The channel transcript was present in a subset of rat dorsal-root-ganglion sensory neurons, some of which express nociceptor-associated markers; it was absent in other tissues that were tested, including sympathetic, enteric and central nervous system neurons. Moreover, when expressed in Xenopus oocytes, the channel showed an ATP-dependent cation flux. P2X3 is the only ligand-gated channel known to be expressed exclusively by a subset of sensory neurons. The remarkable selectivity of expression of the channel coupled with its sensory neuron-like pharmacology suggests that this channel may transduce ATP-evoked nociceptor activation.

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