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P2X receptors are simple polypeptide channels that mediate fast purinergic depolarizations in both nerve and muscle. Although the depolarization results mainly from the influx of Na(+), these channels also conduct a significant Ca(2+) current that is large enough to evoke transmitter release from presynaptic neurons. We sought to determine the molecular(More)
P2X receptors are a distinct family of ligand-gated ion channels activated by extracellular ATP. Each of the seven identified subunit proteins (P2X1 through P2X7) has been reported to form functional homo-oligomeric channels when expressed in heterologous systems. Functional studies of native receptors, together with patterns of subunit gene expression,(More)
P2X receptors are a family of ATP-gated ion channels thought to have intracellular N and C termini and two transmembrane segments separating a large extracellular domain. We examined the involvement of the second putative transmembrane domain (TM2) of the P2X2 subunit in ion conduction, using the substituted cysteine accessibility method (SCAM). This method(More)
P2X receptors are a family of ion channels gated by extracellular ATP. Each member of the family can form functional homomeric channels, but only P2X2 and P2X3 have been shown to combine to form a unique heteromeric channel. Data from in situ hybridization studies suggest that P2X1 and P2X5 may also co-assemble. In this study, we tested this hypothesis by(More)
Kainic acid is a potent neurotoxin for certain neurons. Its neurotoxicity is thought to be mediated by an excitatory amino-acid-gated ion channel (ionotropic receptor) possessing nanomolar affinity for kainate. Here we describe a new member of the rat excitatory amino-acid receptor gene family, KA-1, that has a 30% sequence similarity with the previously(More)
We present the cloning of 10 N-methyl-D-aspartate (NMDA) receptor subunits from the zebrafish. These subunits fall into five subtypes, each containing two paralogous genes. Thus, we report two NMDAR1 genes (NR1.1 and NR1.2), and eight NMDAR2 genes, designated NR2A.1 and NR2A.2, NR2B.1 and NR2B.2, NR2C.1 and NR2C.2, and NR2D.1 and NR2D.2. The predicted(More)
P2X receptors are ATP-gated ion channels found in a variety of tissues and cell types. Seven different subunits (P2X(1)-P2X(7)) have been molecularly cloned and are known to form homomeric, and in some cases heteromeric, channel complexes. However, the molecular determinants leading to the assembly of subunits into P2X receptors are unknown. To address this(More)
ATP opens ionotropic P2X channels through a process that is poorly understood. We made an array of mutant rat P2X2 channels containing unique alanine substitutions in the transmembrane segments with the goal of identifying possible secondary structure and mapping gating domains in the pore. Alteration of channel function was measured as a change in ATP(More)
Multiple subtypes of alpha adrenergic receptors with CNS expression (alpha 1A, alpha 1B, alpha 2A and alpha 2C) have been identified through pharmacological and molecular biological means. To characterize the localization of these subtypes and attempt to correlate subtype expression with physiological significance, the expression of the mRNAs encoding the(More)
We describe a P2X subunit cloned from the zebrafish (Danio rerio) that is an orthologue of the mammalian P2X(3) subunit. Like the mammalian P2X(3), this receptor desensitizes rapidly in the presence of agonist. However, it differs in that alphabeta-meATP is a much less potent agonist than ATP and the antagonist TNP-ATP is not active at low nanomolar(More)