ライフサイエンスコーパス: P2X(2) receptor

1 s little to the permeation properties of the P2X2 receptor.

2 ionally interacting purinergic receptor: the P2X2 receptor.

3 -1.5) but was significantly higher (2.5) for P2X2 receptors.

4 neurons are likely to express predominantly P2X2 receptors.

5 X1 subunits to the equivalent amino acids on P2X2 receptors.

6 t EPAC is an important regulator of P2X1 and P2X2 receptors.

7 epend on the intracellular C terminus of the P2X2 receptors.

8 sstalk occurs between alpha6beta4 nAChRs and P2X2 receptors.

9 l openings that were never seen in wild-type P2X2 receptors.

10 e key components of the zinc binding site in P2X2 receptors.

11 els incorporating the properties of P2X1 and P2X2 receptors.

12 dines in the extracellular domain of the rat P2X(2) receptor.

13 gical profile is consistent with that of the P2X(2) receptor.

14 uence ion conduction through the pore of the P2X(2) receptor.

15 ance by a mutational analysis of recombinant P2X(2) receptors.

16 f whether both cell types contain functional P2X(2) receptors.

17 h half-maximal concentrations of 5 mM at the P2X2 receptor, 89 mM at the P2X3 receptor and 15 mM at b

18 ion, calcium permeability, and dye uptake as P2X2 receptors activated by ATP.

19 h frequent mating over days, suggesting that P2X2 receptor adds a selection advantage under these con

20 P2X2 receptors also functionally interact with alpha6bet

21 receptor function, we studied wild-type rat P2X(2) receptors and 10 mutant P2X(2) receptors, each co

22 ional green fluorescent protein (GFP)-tagged P2X(2) receptors and expressed them in embryonic hippoca

23 Zinc binds to rat P2X2 receptors and acts as an allosteric modulator, pote

24 cells stably transfected with either P2X1 or P2X2 receptors and by absorption controls with the cogna

25 he cranial neural crest and does not express P2X2 receptors and fails to respond to alpha,beta-methyl

26 a6beta4-containing (alpha6beta4*) nAChRs and P2X2 receptors and/or P2X3 receptors have not been fully

27 We conclude that P2X(2) receptors are trimers, whereas the P2X(6) recepto

28 ATP-gated P2X(2) receptors are widely expressed in neurons, but th

29 P2X2 receptors are ATP-gated ion channels widely express

30 sures of P2X receptor mobility and show that P2X2 receptors are mobile ATP sensors, sampling more of

31 el, since ATP currents evoked at recombinant P2X2 receptors are potentiated by lowering extracellular

32 surface, indicating that the nonglycosylated P2X2 receptors are retained inside the cell.

33 ATP-gated ionotropic P2X2 receptors are widely expressed in neurons.

34 uggest that the permeability sequence of the P2X(2) receptor arises in part from interactions of perm

35 taste neurons heterologously expressing rat P2X2 receptors as a screening platform.

36 X2 p.V60L abolishes two hallmark features of P2X(2) receptors: ATP-evoked inward current response and

37 ion by zinc, evidence for an in vivo role of P2X(2) receptors based on studies conducted on genetical

38 P2X(2) receptors bearing His(6) epitope tags were incuba

39 robe the location of this zinc binding site, P2X2 receptors bearing mutations of the histidines at po

40 of removing N-linked glycosylation from the P2X2 receptor by using two different approaches, tunicam

41 structurally homologous to the prototype rat P2X(2) receptor (called hP2X(2a)) and a variant containi

42 The slowly desensitizing P2X2 receptor can be activated by free ATP, but MgATP(2-

43 Activation of P2X2 receptor channels by extracellular ATP is thought t

44 essing either wild-type or functional mutant P2X2 receptors containing a cysteine substitution in or

45 P2X(2) receptor currents are potentiated by acidic pH an

46 at a significant component of TTS represents P2X2 receptor-dependent purinergic hearing adaptation th

47 However, P2X(2) receptors display permeability dynamics, which ar

48 an be quantified, and reveal the dynamics of P2X(2) receptor distribution on the seconds time scale.

49 ing commonly described as non-desensitizing, P2X2 receptors do desensitize or inactivate.

50 distances in the transmembrane domain of the P2X2 receptor during activation.

51 sequential expression of the P2X5, P2Y1, and P2X2 receptors during the process of muscle regeneration

52 wild-type rat P2X(2) receptors and 10 mutant P2X(2) receptors, each containing an alanine substituted

53 Similar results were obtained at P2X2 receptors even without previous agonist tethering:

54 , and to confirm its agonist activity on rat P2X2 receptors expressed in human cells.

55 Subsequent P2X2 receptor expression on newly formed myotubes showed

56 Both functional forms of the human P2X(2) receptors formed heteromeric channels with the hu

57 P2X(2) receptors from rats show potentiation when a subm

58 These data indicate that modulation of P2X2 receptor function, such as that evoked by acidifica

59 current is not detected in mice lacking the P2X2 receptor gene (P2rx2(-/-)).

60 is a noncompetitive antagonist at wild-type P2X2 receptors, had a pronounced agonist action at both

61 hough the electrophysiological properties of P2X2 receptors have been extensively studied, little is

62 Human P2X2 receptors (hP2X2) are strongly inhibited by zinc ov

63 nnels make no detectable contribution to the P2X(2) receptor I(2) state.

64 nant expression and functional gating of the P2X2 receptor in baker's yeast.

65 of the first transmembrane domain of the rat P2X2 receptor in cation permeability and flux.

66 In the present study, the distribution of P2X2 receptor in the rat hypothalamus was studied with i

67 spontaneous gating, and rectification of rat P2X2 receptor in which polar and charged residues of the

68 lamp recordings to track quantum dot-labeled P2X2 receptors in the dendrites of rat hippocampal neuro

69 to Cd(2+) at substituted cysteines in TM2 of P2X2 receptors in the open and closed states.

70 The propyl-MTS did not open P2X2 receptors in which the Val(48) side chain was remov

71 the unspliced, 472 amino acid isoform of the P2X2 receptor, inactivation required membrane disruption

72 Each subunit of a trimeric P2X2 receptor is composed of intracellular N and C termi

73 clude that the C-terminal splice site of the P2X2 receptor is located within a region that is critica

74 We find that plasma membrane P2X2 receptor lateral mobility in dendrites is heterogen

75 ers may be loss of function of the ATP-gated P2X(2) receptor (ligand-gated ion channel, purinergic re

76 drites of rat hippocampal neurons to explore P2X2 receptor mobility and its regulation.

77 dge, a comparison of the closed and open rat P2X2 receptor models revealed a significant rearrangemen

78 els likely activates the broadly distributed P2X2 receptors on epithelial cells lining the endolympha

79 annel pore and tested this as a reporter for P2X(2) receptor opening.

80 ults demonstrate that the loss of functional P2X2 receptors or distinct alterations of its functional

81 bout the plasma membrane lateral mobility of P2X2 receptors or whether receptor mobility is regulated

82 The P2X2 receptor (P2X2R) is a member of the ATP-gated ion c

83 The P2X2 receptor (P2X2R) is a slowly desensitizing adenosin

84 f ionic modulation that is characteristic of P2X2 receptors: potentiation by acidification and extrac

85 Cross-linking of the P2X(2) receptor produced higher order adducts, consisten

86 of the two transmembrane domains of the rat P2X2 receptor protein, and is likely to be close to the

87 or lowering the pH to 6.8, which potentiates P2X(2) receptor responses, did not alter the ATP-stimula

88 direct evidence that calcium influx through P2X2 receptors results in the activation of the MAP kina

89 inc over the range of 2-100 muM, whereas rat P2X2 receptors (rP2X2) are strongly potentiated over the

90 amino-terminal region with the corresponding P2X2 receptor section (P2X7-2Nbeta) gave responses that

91 Interpreted with a P2X2 receptor structural model of the closed state, our

92 gene structure and mRNA heterogeneity of the P2X(2) receptor subtype are evolutionarily conserved bet

93 Deletion mutants of the P2X(2) receptor subunit were expressed individually and

94 ere we describe null mutant mice lacking the P2X2 receptor subunit (P2X2-/-) and double mutant mice l

95 asparagine residues 182, 239, and 298 of the P2X2 receptor subunit by showing that the protein is gly

96 P2X2 receptor subunit immunoreactivity was detected in a

97 HEK-293 cells stably transfected with the P2X2 receptor subunit showed little or no response to AT

98 n mice null for the P2RX2 gene (encoding the P2X2 receptor subunit), sustained 85-dB noise failed to

99 of the VLM respiratory neurones express the P2X2 receptor subunit.

100 Coexpression of mutant and WT P2X(2) receptor subunits significantly reduced ATP-activ

101 he first transmembrane domains of ionotropic P2X(2) receptor subunits.

102 w that ATP-gated ion channels assembled from P2X2 receptor subunits in the cochlea are necessary for

103 rostral ventrolateral medulla (VLM) express P2X2 receptor subunits of the ATP-gated ion channel, sin

104 P2X2 receptor subunits of the ATP-gated ion channels are

105 introducing pairs of cysteines into the rat P2X2 receptor that might form disulfide bonds within or

106 We have engineered a P2X2 receptor that opens within milliseconds by irradiat

107 In rat P2X2 receptors, these intersect at Thr(339).

108 The response of P2X(2) receptors to submaximal concentrations of ATP is

109 We have used chimeras between human P2X1 and P2X2 receptors to address the contribution of the extrac

110 nnels that physically couple with purinergic P2X2 receptors to trigger a functional cross-inhibition

111 ment for P2X1 receptors but had no effect on P2X2 receptor trafficking.

112 ist potency and specificity profiles for rat P2X2 receptors; triphosphate-bearing analogues display b

113 As with a high degree of homology to the rat P2X(2) receptor were isolated from human pituitary and p

114 Wild type and 31 mutant P2X(2) receptors were expressed in HEK-293 cells and stu

115 Pharmacologically, these functional human P2X(2) receptors were virtually indistinguishable, with

116 Rat wild-type and mutant P2X2 receptors were expressed in Xenopus oocytes and cur

117 P2X2 receptors were forced into a prolonged desensitized

118 C regulate their parasensory cation flux via P2X(2) receptors, which would regulate the endolymphatic

119 P2RX2 encodes the P2X2 receptor, which is an adenosine triphosphate (ATP)

120 study, we used homology modeling of the rat P2X2 receptor with the zebrafish P2X4 X-ray template to