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Molecular Neurobiology Unit, Royal Free Hospital School of
Medicine, London, NW3 2PF, United Kingdom (J.S., E.A.B.), and
Glaxo
Institute of Applied Pharmacology (J.S., E.J.K., F.M.S., I.P.C.,
P.P.A.H.) and
Department of Pharmacology (F.M.S., R.M.-L.), University
of Cambridge, Cambridge CB2 1QJ, United Kingdom
cDNAs encoding three splice variants of the P2X2 receptor
were isolated from rat cerebellum. The first variant has a
serine/proline-rich segment deleted from the intracellularly located
carboxyl-terminal domain of the P2X2 subunit. The second
and third variants have the splice site in the second half of the
predicted first transmembrane domain. Either a 12-amino acid insertion
or a six-amino acid deletion occurs at this position. cRNAs for these
isoforms of the P2X2 subunit were injected into
Xenopus laevis oocytes and tested for function. ATP
evoked inward currents only with the splice variant [designated
P2X2(b)] having the 69-amino acid deletion. The potencies of various agonists at the homomeric P2X2(b) receptor were
not significantly different from those at the P2X2(a)
homomeric channel. However, the P2X2(b) receptor showed
significantly lower antagonist sensitivity. In contrast to the
nondesensitizing P2X2(a) receptor, prolonged application of
ATP produced a more rapid desensitization of the P2X2(b)
receptor. When the P2X2(a) and P2X2(b) receptor responses were recorded in transfected mammalian cells, this difference was again found. The change in desensitization may be determined by
proline/serine-rich segments and/or phosphorylation motifs that are
removed from the tail region in formation of the P2X2(b) subunit. In situ hybridization of the three newly
isolated isoforms of the P2X2 subunit was performed at the
macroscopic and cellular levels; transcripts for two of them
[P2X2(b) and p2x2(c)] but not the third
[p2x2(d)], which carries the 12-amino acid addition, were
present in many structures in the neonatal rat brain and on sensory and
sympathetic ganglia. mRNA for the p2x2(d) splice variant
was present only in the nodose ganglion, at a low level.
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