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Results for “Receptors, Purinergic P2X2”

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At least 19 recordsLinked to original sources

PubMed2006

Changes in the expression of P2X1 and P2X2 purinergic receptors in facial motoneurons after nerve lesions in rodents and correlation with motoneuron degeneration.

Involvement of P2X1 and P2X2 purinergic receptors in motoneuron response to injury was investigated with Western blotting and immunohistochemistry and correlated with motoneuron loss, Bcl-2 expression, nitric oxide synthase induction and glial activation. P2X1 was highly induced in rat facial motoneurons after nerve resection, which causes slowly occurring neurodegeneration. P2X1 induction was lower and less persistent after nerve crush, permissive for fiber regeneration. P2X2 expression was found in nuclei of rat facial motoneurons, with nuclear export in the cytoplasm after nerve resection. P2X1 induction in axotomized facial motoneurons was impaired in superoxide dismutase (SOD)1-G93A-mutant mice, a model of motoneuron disease. The data in rats point to a correlation of P2X1 induction with motoneuron degeneration, which also involves P2X2 intracellular changes, rather than with axon regeneration effort. The data in mice show that the SOD1 mutation interferes with injury-elicited P2X1 induction, suggesting alterations of ATP release from mutant motoneurons after damage.

Animals↗

PubMed2002

Cerebellar lesion up-regulates P2X1 and P2X2 purinergic receptors in precerebellar nuclei.

ATP released in the extracellular space by neuronal injury can influence neighboring neurons via activation of purinergic receptors. In vitro data suggest the involvement of ATP and purinergic receptors as trophic agents in different biological events such as neuritogenesis and cell survival. Recently, in vivo studies have demonstrated modifications in the glial expression of ionotropic purinergic receptors after CNS lesions. In the present study, we investigated the effects of CNS lesion on the neuronal expression of P2X(1) and P2X(2) receptor subunits by immunohistochemistry and western blotting techniques. In the precerebellar structures of normal animals the expression of P2X(1) and P2X(2) was lower than previously reported. P2X(1) immunostaining was confined only to fibers, while P2X(2) immunostaining demonstrated a neuronal expression. After unilateral cerebellar lesion (hemicerebellectomy) axotomized precerebellar neurons underwent marked cell loss; however, some precerebellar neurons did not degenerate. Seven to 35 days after hemicerebellectomy, a transient, time-dependent, marked increase in the number of immunopositive P2X(1) and P2X(2) neurons was observed in the precerebellar nuclei of the experimental side. An even distribution of immunopositive neurons was present in almost all precerebellar nuclei examined, except for the inferior olive. In this latter structure, differences in the distribution of immunopositive neurons were evident among the subnuclei. Up-regulation of immunoreactivity over relatively long time periods, distribution selectivity and absence of degenerating morphological features in immunopositive neurons suggest that purinergic receptors may have a role in mediating the survival of neuronal responses to axotomy. The present findings are the first report in the CNS of P2X(1) and P2X(2) receptor subunit involvement in neuronal reaction to axotomy. They provide in vivo evidence of a correlation between purinergic receptor subunit up-regulation and survival of injured neurons.

Animals↗

PubMed2005

ATP signaling is crucial for communication from taste buds to gustatory nerves.

Taste receptor cells detect chemicals in the oral cavity and transmit this information to taste nerves, but the neurotransmitter(s) have not been identified. We report that adenosine 5'-triphosphate (ATP) is the key neurotransmitter in this system. Genetic elimination of ionotropic purinergic receptors (P2X2 and P2X3) eliminates taste responses in the taste nerves, although the nerves remain responsive to touch, temperature, and menthol. Similarly, P2X-knockout mice show greatly reduced behavioral responses to sweeteners, glutamate, and bitter substances. Finally, stimulation of taste buds in vitro evokes release of ATP. Thus, ATP fulfils the criteria for a neurotransmitter linking taste buds to the nervous system.

Adenosine Triphosphate↗

PubMed2003

Intraganglionic laminar endings in the rat esophagus contain purinergic P2X2 and P2X3 receptor immunoreactivity.

Intraganglionic laminar endings (IGLEs) represent the most prominent vagal afferent terminal structures throughout the gastrointestinal tract. They are most prominent in the esophagus and stomach, but can be found down to the distal colon. Their role as mechanosensors as proposed on anatomical grounds was recently substantiated in elegant functional experiments. There is evidence that vagal mechanosensors in the esophagus and stomach respond to ATP. Thus, the present study aimed at detecting purinergic receptors on IGLEs. IGLEs in the rat esophagus were identified by immunohistochemistry for calretinin and sections were co-incubated with antibodies directed against P2X2 or P2X3 receptors. Also, double label immunocytochemistry for purinergic receptors and calcitonin gene-related peptide as a marker for spinal afferents was performed. Terminal nerve fibers immunoreactive for P2X2 and P2X3, respectively, were observed between outer and inner layers of the tunica muscularis, covering myenteric ganglia totally or partly. Both P2X2 and P2X3 receptor immunoreactivities were highly co-localized with calretinin positive IGLEs as shown by confocal laser scanning microscopy. Numerous calcitonin gene-related peptide immunostained fibers were found to closely approach and intermingle with P2X immunopositive IGLEs. However, there was never co-staining for either of the purinergic receptors and calcitonin gene-related peptide within the same fibers. P2X3 but not P2X2 immunoreactivity was also observed within nerve fiber arborizations in the mucosa of the pharynx. In the nodose ganglion, 8.9 +/- 1.1% of P2X2 and 7.2 +/- 1.3% of P2X3 immunopositive neurons, respectively, co-stained for calretinin. On the other hand, 63.4 +/- 4.6% and 60.1 +/- 5.3% of calretinin positive cell bodies contained P2X2 and P2X3 receptor immunoreactivity, respectively. These results indicate that IGLEs are equipped with both P2X2 and P2X3 receptors. Thus, they may act as chemosensors or their mechanosensory properties may be modulated by ATP. It is also suggested that spinal afferents innervating the esophagus are equipped with neither P2X2 nor P2X3 purinergic receptors.

Animals↗

PubMed2004

OFF-cholinergic-pathway-selective localization of P2X2 purinoceptors in the mouse retina.

It is known that, in the retina, extracellular adenosine triphosphate (ATP) inhibits acetylcholine (ACh) release from cholinergic neurons, but the types of purinoceptors on cholinergic neurons have not been examined. In the present work, we immunohistochemically examined the distribution of the purinoceptors P2X1, P2X2, P2X4, and P2X7 in relation to the cholinergic system of the retina in wild-type mice and transgenic mice expressing green fluorescent protein (GFP). Immunoreactivity for P2X2 was very strong in sublamina a of the inner plexiform layer but very weak in sublamina b of the inner plexiform layer of the retina. Immunoreactivity for P2X2 was colocalized with that for choline acetyltransferase (ChAT). When transgenic mice were treated with the immunotoxin-mediated cell-targeting technology to ablate cholinergic amacrine cells selectively, immunoreactivity for P2X2 and the signals for GFP disappeared in parallel and selectively in the OFF pathway. The distribution of immunoreactivity for P2X1, P2X4, and P2X7 differed from that of ChAT immunoreactivity. The selective distribution of P2X2 purinergic receptors in OFF-type cholinergic amacrine cells indicates that the P2X2 purinergic signaling systems in the ON and OFF pathways of the inner plexiform layer of the mouse retina are functionally different. The distribution of P2X2 purinoceptors may be responsible for the selective regulation of ACh release in the OFF pathway.

Acetylcholine↗

PubMed2000

Expression of purinergic P2X2 receptor-channels and their role in calcium signaling in pituitary cells.

Pituitary cells express purinergic receptor-channels (P2XR), the activation of which by ATP is associated with the facilitation of Ca2+ influx. Pharmacological, RT-PCR, and nucleotide sequence analyses confirm the presence of a wild type P2X2aR and a spliced isoform P2X2bR, which lacks a portion of carboxyl terminal amino acids. Wild type and spliced isoform receptors have a similar EC50 for ATP and time-course for activation, but the spliced isoform exhibits rapid and complete desensitization, whereas the wild type channel desensitizes slowly and incompletely. Deletion and insertion studies have revealed that a 6 residue sequence located in carboxyl tail (Arg371-Pro376) is required for sustained Ca2+ influx through wild type receptors. When co-expressed, the wild type and spliced channels form functional heteropolymeric channels. The patterns of Ca2+ signaling in the majority of pituitary cells expressing ATP-gated receptor-channels are highly comparable to those observed in cells co-transfected with P2X2aR and P2X2bR. ATP-induced [Ca2+]i response in pituitary cells is partially inhibited by nifedipine, a blocker of voltage-gated L-type Ca2+ channels, suggesting that P2X2R not only drive Ca2+ into the cell, but also activate voltage-gated Ca2+ entry. Our results indicate that ATP represents a paracrine and (or) autocrine factor in the regulation of Ca2+ signaling, and that its actions are mediated in part by heteropolymeric P2X2R.

Adenosine Triphosphate↗

PubMed2005

Visualization of the trimeric P2X2 receptor with a crown-capped extracellular domain.

The P2X2 purinergic receptor permeates cationic ions in response to stimulation by ATP and mediates fast synaptic transmission. Here, we purified the P2X2 receptor using baculovirus-Sf9 cell expression system and observed its structure using electron microscopy. The FLAG-tagged P2X2 receptor, which has intact ion channel function, was purified to be a single peak by affinity purification and gel filtration chromatography. It was confirmed to be a trimer by introducing cross-linking. Negatively stained P2X2 protein images were homogeneous and picked up by automated pick-up programs, aligned, and classified using the modified growing neural gas network method. Similarly oriented projections were averaged to decrease the signal-to-noise ratio. These images demonstrate an inverted three-sided pyramid with the dimensions of 215 A in height and 200 A in side length. It is composed of a high-density trunk and a stain-permeable swollen extracellular domain of a crown-shaped structure. The internal cavities and constituent segments were clearly demonstrated in both the raw images and the averaged images. The threefold symmetrical top view demonstrates the first visual evidence of the trimeric composition of the P2X receptor family.

Animals↗

PubMed2004

P2X2 and P2Y1 immunofluorescence in rat neostriatal medium-spiny projection neurones and cholinergic interneurones is not linked to respective purinergic receptor function.

1. The presence of ionotropic P2X receptors, targets of ATP in fast synaptic transmission, as well as metabotropic P2Y receptors, known to activate K(+) currents in cultured neostriatal neurones, was investigated in medium-spiny neurones and cholinergic interneurones contained in neostriatal brain slices from 5-26-day-old rats. 2. In these cells, adenosine-5'-triphosphate (ATP) (100-1000 microm), 2-methylthioadenosine-5'-triphosphate (2MeSATP), alpha,beta-methyleneadenosine-5'-triphosphate (alpha,betameATP, 30-300 microm, each) and adenosine-5'-O-(3-thiotriphosphate (ATPgammaS) (100 microm) failed to evoke P2X receptor currents even when 8-cyclopentyl-1,3-dipropylxanthine (DPCPX, 0.1 microm), apyrase (10 U ml(-1)) or intracellular Cs(+) was used to prevent occluding effects of the ATP breakdown product adenosine, desensitisation of P2X receptors by endogenous ATP and an interference with the activation of K(+) channels, respectively. P2X receptor agonists were also ineffective in outside-out patches withdrawn from the brain slice tissue. Muscimol (10 microm) evoked GABA(A) receptor-mediated currents under all these conditions. 3. When used as a control, locus coeruleus neurones responded with P2X receptor-mediated currents to ATP (300 microm), 2MeSATP and alpha,betameATP (100 microm, each). 4. ATP and adenosine-5'-diphosphate (ADP) (100 microm, each) did not activate K(+) currents in the neostriatal neurones. 5. Despite the observed lack of function, P2X(2) and P2Y(1) immunofluorescence was found in roughly 50% of the medium-spiny neurones and cholinergic interneurones. 6. A role of ATP in synaptic transmission to striatal medium-spiny neurones and cholinergic interneurones appears unlikely, however, the otherwise silent P2X and P2Y receptors may gain functionality under certain yet unknown conditions.

Adenosine Triphosphate↗

PubMed2004

Detecting ATP release by a biosensor method.

Cells release adenosine 5'-triphosphate (ATP) into the extracellular space in response to various stimuli. This released ATP plays an important physiological role in cell-to-cell signal transduction. The bulk ATP concentration can be detected using a conventional luciferin-luciferase assay. However, the ATP concentration in the vicinity of the cell surface is often different from the bulk concentration because of its rapid degradation by ecto-ATPases and because of delayed diffusion due to unstirred layer effects. Here, we describe a simple biosensor method to measure the local ATP concentration on the cell surface in real time. The method is based on the ATP-dependent opening of ligand-gated cation channels of purinergic P2X receptors expressed in undifferentiated pheochromocytoma (PC12) cells or in human embryonic kidney 293 (HEK293) cells stably transfected with recombinant P2X2 purinergic receptors. Under the whole-cell configuration of patch-clamp, a sensor PC12 cell or HEK293 is positioned within the proximity of a target cell, and the P2X-mediated currents induced by ATP released from a given site on the target cell surface is measured. The ATP release is quantified by a calibration procedure utilizing local puff applications of ATP at preset concentrations.

Adenosine Triphosphate↗

PubMed2000

The purinergic calcium channels P2X1,2,5,7 are down-regulated while P2X3,4,6 are up-regulated during apoptosis in the ageing rat prostate.

Subtype-specific antibodies were used to measure purinergic (P2X) receptor expression in the rat prostate. In mature Wistar rats, apoptosis and expression of P2X1, P2X2, P2X5 and P2X7 subtypes were all significantly decreased compared with the levels found in immature rat prostates. Accompanying this age-related reduction in purinergic calcium channel expression was a reduction in epithelial and stromal calcium as well as the calcium-regulating hormone stanniocalcin. In contrast, expression of P2X3, P2X4 and P2X6 increased with age. These results suggest that distinct changes in P2X subtype expression accompany apoptosis in the rat prostate.

Aging↗

PubMed2005

ATP and purinergic receptor-dependent membrane traffic in bladder umbrella cells.

The umbrella cells that line the bladder are mechanosensitive, and bladder filling increases the apical surface area of these cells; however, the upstream signals that regulate this process are unknown. Increased pressure stimulated ATP release from the isolated uroepithelium of rabbit bladders, which was blocked by inhibitors of vesicular transport, connexin hemichannels, ABC protein family members, and nucleoside transporters. Pressure-induced increases in membrane capacitance (a measure of apical plasma membrane surface area where 1 microF approximately equals 1 cm2) were inhibited by the serosal, but not mucosal, addition of apyrase or the purinergic receptor antagonist PPADS. Upon addition of purinergic receptor agonists, increased capacitance was observed even in the absence of pressure. Moreover, knockout mice lacking expression of P2X2 and/or P2X3 receptors failed to show increases in apical surface area when exposed to hydrostatic pressure. Treatments that prevented release of Ca2+ from intracellular stores or activation of PKA blocked ATPgammaS-stimulated changes in capacitance. These results indicate that increased hydrostatic pressure stimulates release of ATP from the uroepithelium and that upon binding to P2X and possibly P2Y receptors on the umbrella cell, downstream Ca2+ and PKA second messenger cascades may act to stimulate membrane insertion at the apical pole of these cells.

Adenosine Triphosphate↗

PubMed2002

Interstitial cells of Cajal and purinergic signalling.

Interstitial cells of Cajal (ICC) in the guinea pig intestine, identified by the tyrosine kinase receptor, c-Kit, have been shown with immunohistochemistry to express nucleotide P2X2 and P2X5 receptors. P2X5 receptors have also been demonstrated on interstitial cells in the mouse ileum. It is speculated that release of ATP from enteric nerves, enteric glial cells or from contracting smooth muscle may provide a feedback mechanism for pacemaker activity in the intestine.

Animals↗

PubMed2004

Selective modulation of ligand-gated P2X purinoceptor channels by acute hypoxia is mediated by reactive oxygen species.

Purinergic excitatory synapses use ATP to mediate fast synaptic transmission via activation of P2X receptor cation channels, and this response can be altered by acute hypoxia. This study examined the effect of acute hypoxia on cloned homo- and heteromeric P2X2 and P2X3 receptors expressed in human embryonic kidney 293 cells. In cells expressing homomeric P2X2 receptors, perfusion of 5 microM ATP (EC25) induced an inward whole-cell current that showed little desensitization during repeated exposures under continuously normoxic conditions. Exposure to a hypoxic ATP solution (pO2, 25-40 mm Hg) significantly reduced the whole-cell current to 49% of normoxic control. This hypoxic inhibition of P2X2-mediated inward current was maintained across all potentials when a voltage-step protocol was applied. In contrast, currents mediated by homomeric P2X3 receptors or heteromeric P2X(2/3) receptors were insensitive to an acute hypoxic challenge. One mechanism whereby hypoxia may modulate P2X2 channels is via the production of reactive oxygen species (ROS). H2O2 (1.8 mM) reversibly reduced homomeric P2X2 whole-cell currents to 38% of control. Furthermore, H2O2 attenuated the effect of hypoxia on homomeric P2X2 whole-cell currents. Inhibitors of the mitochondrial electron transport chain that reduce (rotenone and myxothiazol) or increase (antimycin A) the production of ROS altered the magnitude of P2X2-mediated currents. In summary, this is the first report indicating that acute hypoxia is able to regulate the activity of any ligand-gated ion channel. Furthermore, our data show that acute hypoxia selectively modulates the P2X2 receptor and that the response of P2X2 receptor subunits to hypoxia is mediated through the mitochondrial production of ROS.

Adenosine Triphosphate↗

PubMed2005

Possible role of 5'-adenosine triphosphate in synchronization of Ca2+ oscillations in primate luteinizing hormone-releasing hormone neurons.

LHRH neurons derived from the olfactory placode region of monkey embryos exhibit spontaneous intracellular Ca2+ ([Ca2+]i) oscillations that synchronize among LHRH neurons and nonneuronal cells at a frequency similar to pulsatile LHRH release. To understand the mechanism of intercellular communication between LHRH neurons and nonneuronal cells, which leads to synchronization, we examined the possible role of ATP. 1) ATP, not ADP or AMP, stimulated both LHRH release and [Ca2+]i concentration, whereas the ATP-induced [Ca2+]i response was abolished by infusion of apyrase, which hydrolyzes ATP; 2) the ATP-induced [Ca2+]i response occurred in normal (but not low) extracellular Ca2+ and was blocked by the voltage-dependent L-type Ca2+ channel blocker, nifedipine; 3) pharmacological experiments with purinergic receptor agonists and antagonists indicated that the ATP-induced [Ca2+]i response in LHRH neurons was mediated through P2X, but not P2Y, receptors; 4) cloning and sequencing studies suggested that P2X2 and P2X4 transcripts were present in olfactory placode cultures; and 5) P2X2 receptors and P2X4 were expressed in LHRH neurons. The results suggest that ATP may play a role in intercellular communication when LHRH neurons synchronize, and raise the possibility that nonneuronal cells, such as glia, may be a crucial component of the in vivo LHRH neurosecretory system.

Adenosine Triphosphate↗

PubMed2000

Distributional changes of purinergic receptor subtypes (P2X 1-7) in uterine epithelial cells during early pregnancy.

Expression of each of the purinergic receptor subtypes (P2X7) was studied by immunohistochemical localization in the apical, lateral and basal plasma membranes of rat uterine epithelial cells during early pregnancy to the time of implantation on Day 6. Labelling for each P2X subtype was seen in the apical, lateral and basal compartments on Days 1 and 3, except for P2X2 which was only observed in the basement membrane. The P2X5 signal was similar in temporal and spatial expression to the other subtypes, but with a greatly reduced intensity. At the time of implantation on Day 6, this pattern altered dramatically. Apical expression markedly increased for most subtypes while the lateral and basal signals were markedly reduced. The exceptions to this pattern were P2X2, which displayed both a strong basal and apical label, and P2X4 which became de-expressed in all areas. We propose that the changing spatial and temporal expression of the P2X receptors is a significant factor in the regulation of events during early pregnancy. They are expressed in the same location as remodelling. apoptosis, and protein activation events prior to implantation on Day 6. These observations suggest an up-regulation of calcium-mediated events, including cytoskeletal alterations, a decrease in luminal pH and transmembrane molecule activation.

Animals↗

PubMed2002

Potentiation of inhibitory glycinergic neurotransmission by Zn2+: a synergistic interplay between presynaptic P2X2 and postsynaptic glycine receptors.

The divalent cation zinc is known to modulate chloride currents carried by native and recombinant mammalian glycine receptors (GlyRs). To unravel the effect of Zn2+ on glycinergic neurotransmission, inhibitory postsynaptic currents (IPSC) of rat spinal neurons grown in culture were analysed in the absence and presence of Zn2+. Low concentrations of Zn2+ (0.5 and 5 micro m) augmented the mean amplitude of miniature IPSCs by approximately 40% over values obtained in the absence of zinc, whereas higher concentrations of Zn2+ (50 micro m) significantly decreased mean amplitude values. Remarkably, low concentrations of Zn2+ also significantly increased the mean frequency of miniature IPSCs. This effect was blocked by the P2X receptor antagonists PPADS and suramin, indicating the presence of Zn2+-sensitive presynaptic P2X receptors on glycinergic terminals. Immunostaining with antibodies against different P2X receptor subtypes revealed that P2X2 receptors partially colocalize with the GlyR. Potentiating concentrations of Zn2+ also affected the kinetics of miniature and evoked IPSCs by significantly prolonging their decay time constants. Electrophysiological analysis of heterologously expressed glycine transporters (GlyT) revealed for GlyT2 zero, and for GlyT1 a modest (< 20%), reduction of glycine uptake in the presence of 5 micro m Zn2+, indicating that prolongation of glycinergic IPSCs by Zn2+ is not due to inhibition of glycine removal from the synaptic cleft. Together, these results suggest that Zn2+ is a potent modulator of glycinergic synaptic transmission which increases in a synergistic manner the agonist affinity of both presynaptic P2X2 receptors and postsynaptic GlyRs.

Adenosine Triphosphate↗

PubMed2006

Characterization of three types of ATP-activated current in relation to P2X subunits in rat trigeminal ganglion neurons.

In the present study, ATP-activated currents (I(ATP)s) recorded from rat trigeminal ganglion (TG) neurons using whole-cell patch clamp technique are classified into three types (F, I and S) based on the characteristics of their activation and desensitization. The time of rising phase (R(10-90)) of types F, I and S of I(ATP) is measured to be 33.6+/-4.5, 62.2+/-9.9 and 302.1+/-62.0 ms respectively, and positively correlated to cell size. The time of decaying phases (D(10-90)) of types F and S is 399.4+/-58.2 and >1500 ms, respectively. The dose-response curves for the three types of I(ATP) show that their EC(50) values are close (3.44 x 10(-5), 4.89 x 10(-5) and 4.14 x 10(-5) M for types F, I and S respectively, P>0.05). Their reversal potentials are basically the same, varying from +4 to +10 mV. In addition, using whole-cell patch clamp technique in combination with single cell immunohistochemical staining for P2X receptor subunits, our results suggest that the type distinction of ATP-activated current was associated with cell size and P2X receptor subunits: small-sized cells with type F of I(ATP) express only P2X1 and/or P2X3 subunits, while cells with types S and I of I(ATP) express P2X2 or P2X4 in addition to P2X1 and P2X3.

Adenosine Triphosphate↗

PubMed2005

P2X2 and P2X3 receptor expression in postnatal and adult rat urinary bladder and lumbosacral spinal cord.

P2X receptors mediate the effects of ATP in micturition and nociception. During postnatal maturation, a spinobulbospinal reflex and voluntary voiding replace primitive voiding reflexes. This may involve changes in neuroactive compounds and receptors in bladder reflex pathways. We examined P2X2 and P2X3 receptors in bladder and spinal cord from postnatal (P0-P36, indicating number of days) and adult Wistar rats. Western blot of whole bladders for P2X2 and P2X3 expression was performed. Immunostaining for P2X2 and P2X3 receptors in urothelium and detrusor smooth muscle whole mounts and spinal cord sections was examined. Western blot demonstrated an age-dependent decrease (R(2) = 0.96, P </= 0.005) in P2X2 receptor expression in bladder, whereas P2X3 receptor expression in bladder peaked (P </= 0.005) during P14-P21. P2X2-immunoreactivity (IR) was present in urothelial cells, suburothelial plexus, detrusor smooth muscle, and serosa at birth, with staining in urothelial cells and serosa being most predominant. With increasing postnatal age, the intensity of P2X2-IR decreased in urothelial cells but increased in suburothelial plexus. P2X3-IR increased in urothelial cells and suburothelial plexus with postnatal age, whereas staining in detrusor and serosa remained relatively constant. At birth, P2X3-IR was present in the dorsal horn, lateral collateral pathway, and dorsal commissure. With increasing age, P2X3-IR was restricted to superficial dorsal horn and lateral collateral pathway. P2X2-IR was present in ependyme cells (S-100-IR) of the central canal as early as P2. These studies demonstrate plastic expression of P2X2 and P2X3 receptors in bladder and spinal cord during early postnatal development at times coincident with appearance of mature voiding patterns.

Aging↗