ライフサイエンスコーパス: P2X(2) receptor

1 ionally interacting purinergic receptor: the P2X2 receptor.

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

3 sstalk occurs between alpha6beta4 nAChRs and P2X2 receptors.

4 -1.5) but was significantly higher (2.5) for P2X2 receptors.

5 neurons are likely to express predominantly P2X2 receptors.

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

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

8 els incorporating the properties of P2X1 and P2X2 receptors.

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

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

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

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

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

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

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

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

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

18 P2X2 receptors also functionally interact with alpha6bet

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

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

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

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

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

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

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

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

27 P2X2 receptors are ATP-gated ion channels widely express

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

50 Subsequent P2X2 receptor expression on newly formed myotubes showed

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

87 P2X2 receptor subunit immunoreactivity was detected in a

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

107 P2X2 receptors were forced into a prolonged desensitized

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

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