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The antagonist trinitrophenyl-ATP reveals co-existence of distinct P2X receptor channels in rat nodose neurones.
J Physiol 1998; 509 (Pt 2):411-7JP

Abstract

1. Whole-cell recordings were made from rat nodose ganglion neurones in culture and from human embryonic kidney (HEK293) cells stably transfected to express P2X2, P2X3 or both receptor subunits. We examined the blocking actions of 2',3'-O-trinitrophenyl-ATP (TNP-ATP) on currents evoked by the agonists ATP and alpha, beta-methylene ATP. 2. In cells expressing only P2X2 or P2X3 receptor subunits, the inhibition by TNP-ATP was fitted by a single binding site model with half-maximal concentrations of about 3 microM and 3 nM, respectively. In cells expressing both P2X2 and P2X3 receptor subunits, currents showed little or no desensitization, thus excluding contributions from homomeric P2X3 receptors. When alpha,beta-methylene ATP was the agonist (activating heteromeric P2X2/3 receptors), the inhibition by TNP-ATP conformed to a single binding site (half-maximal concentration about 3 nM). When ATP (30 microM) was the agonist, activating both heteromeric P2X2/3 as well as homomeric P2X2 receptors, the inhibition curve was biphasic (half-maximal concentrations about 3 nM and 3 microM); the proportion of high affinity sites in all six cells tested was about 40 %. 3. In nodose ganglion neurones, the inhibition by TNP-ATP of currents evoked by ATP (30 microM) was also clearly biphasic. In this case, individual neurones showed more variability in the proportion of high and low affinity sites for TNP-ATP. 4. We conclude that more than one form of multimeric P2X receptor channels are functionally expressed on the cell bodies of individual nodose ganglion neurones. On the basis of sensitivity to TNP-ATP, and other properties, one of these may correspond to the homomeric P2X2 receptor and the other(s) to heteromeric P2X2/3 receptors.

Authors+Show Affiliations

Geneva Biomedical Research Institute, GlaxoWellcome Research and Development, 14 chemin des Aulx, Plan-les-0uates, Geneva 1228, Switzerland.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

9575290

Citation

Thomas, S, et al. "The Antagonist trinitrophenyl-ATP Reveals Co-existence of Distinct P2X Receptor Channels in Rat Nodose Neurones." The Journal of Physiology, vol. 509 (Pt 2), 1998, pp. 411-7.
Thomas S, Virginio C, North RA, et al. The antagonist trinitrophenyl-ATP reveals co-existence of distinct P2X receptor channels in rat nodose neurones. J Physiol (Lond). 1998;509 (Pt 2):411-7.
Thomas, S., Virginio, C., North, R. A., & Surprenant, A. (1998). The antagonist trinitrophenyl-ATP reveals co-existence of distinct P2X receptor channels in rat nodose neurones. The Journal of Physiology, 509 (Pt 2), pp. 411-7.
Thomas S, et al. The Antagonist trinitrophenyl-ATP Reveals Co-existence of Distinct P2X Receptor Channels in Rat Nodose Neurones. J Physiol (Lond). 1998 Jun 1;509 (Pt 2):411-7. PubMed PMID: 9575290.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The antagonist trinitrophenyl-ATP reveals co-existence of distinct P2X receptor channels in rat nodose neurones. AU - Thomas,S, AU - Virginio,C, AU - North,R A, AU - Surprenant,A, PY - 1998/5/12/pubmed PY - 1998/5/12/medline PY - 1998/5/12/entrez SP - 411 EP - 7 JF - The Journal of physiology JO - J. Physiol. (Lond.) VL - 509 (Pt 2) N2 - 1. Whole-cell recordings were made from rat nodose ganglion neurones in culture and from human embryonic kidney (HEK293) cells stably transfected to express P2X2, P2X3 or both receptor subunits. We examined the blocking actions of 2',3'-O-trinitrophenyl-ATP (TNP-ATP) on currents evoked by the agonists ATP and alpha, beta-methylene ATP. 2. In cells expressing only P2X2 or P2X3 receptor subunits, the inhibition by TNP-ATP was fitted by a single binding site model with half-maximal concentrations of about 3 microM and 3 nM, respectively. In cells expressing both P2X2 and P2X3 receptor subunits, currents showed little or no desensitization, thus excluding contributions from homomeric P2X3 receptors. When alpha,beta-methylene ATP was the agonist (activating heteromeric P2X2/3 receptors), the inhibition by TNP-ATP conformed to a single binding site (half-maximal concentration about 3 nM). When ATP (30 microM) was the agonist, activating both heteromeric P2X2/3 as well as homomeric P2X2 receptors, the inhibition curve was biphasic (half-maximal concentrations about 3 nM and 3 microM); the proportion of high affinity sites in all six cells tested was about 40 %. 3. In nodose ganglion neurones, the inhibition by TNP-ATP of currents evoked by ATP (30 microM) was also clearly biphasic. In this case, individual neurones showed more variability in the proportion of high and low affinity sites for TNP-ATP. 4. We conclude that more than one form of multimeric P2X receptor channels are functionally expressed on the cell bodies of individual nodose ganglion neurones. On the basis of sensitivity to TNP-ATP, and other properties, one of these may correspond to the homomeric P2X2 receptor and the other(s) to heteromeric P2X2/3 receptors. SN - 0022-3751 UR - https://www.unboundmedicine.com/medline/citation/9575290/The_antagonist_trinitrophenyl_ATP_reveals_co_existence_of_distinct_P2X_receptor_channels_in_rat_nodose_neurones_ L2 - https://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0022-3751&date=1998&volume=509&spage=411 DB - PRIME DP - Unbound Medicine ER -