Sensory presynaptic and widespread somatodendritic immunolocalization of central ionotropic P2X ATP receptors

Lê, Khanh-Tuoc; Villeneuve, Pierre; Ramjaun, Antoine R.; McPherson, Peter S.; Beaudet, Alain; Séguéla, Philippe

doi:10.1016/s0306-4522(97)00365-5

Cited by 145 publications

(57 citation statements)

References 34 publications

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“…Analysis of the subcellular localization of hP2X 5 R-FL in HEK-293 cells using confocal microscopy indicated a correct targeting of the subunit to the plasma membrane (Fig. 3), quantitatively similar to the surface distribution of the functional P2X receptors rat P2Xi-FL and rat P2X4-FL [14]. When expressed in Xenopus oocytes, homomeric hP2X 5 channels do not respond to extracellular ATP applied at concentrations up to 1 mM, However, the chimera h-rP2X 5 , made of the N-terminal domain of hP2X 5 linked to the C-terminal domain of rat P2X 5 , revealed the formation of cationic ATP-gated ion channels (Fig.…”

Section: Resultssupporting

confidence: 58%

“…Despite the fact that high levels of expression of P2X receptors are observed in many central and peripheral tissues, reinforcing the concept of an important role for ATP in intercellular communication [11], much less is known about their human counterparts. Excitatory ATP-gated channels play a specific role in sensory systems [12][13][14], therefore the development of subtype-specific P2X antagonists with analgesic properties should take into account functional differences between mammalian species. The reports on the expression of cloned human P2X orthologs of P2Xi [15], P2X 3 [16], P2X 4 [17] and P2X 7 [18] emphasized both pharmacological and anatomical specificities that seriously undermine the relevance of our knowledge based on rodent systems for extrapolation to human fast purinergic transmission.…”

Section: Introductionmentioning

confidence: 99%

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Primary structure and expression of a naturally truncated human P2X ATP receptor subunit from brain and immune system

Lê¹,

Paquet²,

Nouel³

et al. 1997

FEBS Letters

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A novel member of the ionotropic ATP receptor gene family has been identified in human brain. This 422 amino acid long P2X receptor subunit has 62% sequence identity with rat P2X 5 . Several characteristic motifs of ATP-gated channels are present in its primary structure, but this P2Xs-related subunit displays a single transmembrane domain. Heterologous expression of chimeric subunits containing the ( -terminal domain of rat P2Xs leads to the formation of desensitizing functional ATPgated channels in Xenopus oocytes. The developmental^ regulated mRNA, found in two splicing variant forms, is expressed at high levels in brain and immune system.

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Section: Resultssupporting

confidence: 58%

Section: Introductionmentioning

confidence: 99%

Primary structure and expression of a naturally truncated human P2X ATP receptor subunit from brain and immune system

Lê¹,

Paquet²,

Nouel³

et al. 1997

FEBS Letters

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show abstract

“…[16]. Calcium signaling in olfactory bulb neurons, however, could not be recorded upon application of ATP in these studies, although histological data imply the expression of P2X receptors in mitral cells, granule cells, periglomerular cells, and sensory axons themselves in the olfactory bulb [17][18][19][20]. This discrepancy could be explained by technical inadequateness of the calcium imaging studies to record purinergic responses in neurons.…”

Section: Electronic Supplementary Materialsmentioning

confidence: 79%

“…P2X 2 RNA was detected in olfactory bulb tissue using in situ hybridisation [27], and mitral cells, tufted cells as well as granule cells were stained with anti-P2X 2 antibodies [18,20]. P2X 4 RNA and protein was also demonstrated in the olfactory bulb, with particular high expression in mitral cells [19,[28][29][30][31]. In addition, P2X 5 and P2X 6 expression was detected in mitral cells [17,28].…”

Section: P2 Receptors In the Olfactory Bulbmentioning

confidence: 96%

P2Y1 receptor activation by photolysis of caged ATP enhances neuronal network activity in the developing olfactory bulb

Fischer

Rotermund

Lohr

et al. 2011

Purinergic Signalling

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It has recently been shown that adenosine-5′-triphosphate (ATP) is released together with glutamate from sensory axons in the olfactory bulb, where it stimulates calcium signaling in glial cells, while responses in identified neurons to ATP have not been recorded in the olfactory bulb yet. We used photolysis of caged ATP to elicit a rapid rise in ATP and measured whole-cell current responses in mitral cells, the output neurons of the olfactory bulb, in acute mouse brain slices. Wide-field photolysis of caged ATP evoked an increase in synaptic inputs in mitral cells, indicating an ATP-dependent increase in network activity. The increase in synaptic activity was accompanied by calcium transients in the dendritic tuft of the mitral cell, as measured by confocal calcium imaging. The stimulating effect of ATP on the network activity could be mimicked by photo release of caged adenosine 5′-diphosphate, and was inhibited by the P2Y 1 receptor antagonist MRS 2179. Local photolysis of caged ATP in the glomerulus innervated by the dendritic tuft of the recorded mitral cell elicited currents similar to those evoked by wide-field illumination. The results indicate that activation of P2Y 1 receptors in the glomerulus can stimulate network activity in the olfactory bulb.

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“…It is known that the P2X 6 subunit can associate with both P2X 2 and P2X 4 to form heteromeric receptors, which have properties distinct from the corresponding homomers [27,41]. Furthermore, P2X 6 is co-localized with both P2X 2 and P2X 4 in many parts of the central and peripheral nervous systems [22,42,43,61,64,66,69,72]. It is possible, therefore, that the P2X 6 subunit operates as a modulatory subunit rather than a receptor in its own right.…”

Section: Homo-oligomeric Receptorsmentioning

confidence: 99%

Determination of the architecture of ionotropic receptors using AFM imaging

Barrera

Henderson

Edwardson

2007

Pflugers Arch - Eur J Physiol

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Fast neurotransmission in the nervous system is mediated by ionotropic receptors, all of which contain several subunits surrounding an integral ion channel. There are three major families of ionotropic receptors: the 'Cysloop' receptors (including the nicotinic receptor for acetylcholine, the 5-HT 3 receptor, the GABA A receptor and the glycine receptor), the glutamate receptors (including the α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid, kainate and N-methyl-D-aspartic acid receptors) and the P2X receptors for adenosine triphosphate. These receptors are often built from multiple types of subunit, raising the question of the stoichiometry and subunit arrangement within the receptors. This question is of therapeutic significance because in some cases drug-binding sites are located at subunit-subunit interfaces. In this paper, we describe a general method, based on atomic force microscopy imaging, to solve the architecture of multi-subunit proteins, such as the ionotropic receptors. Specific epitope tags are engineered onto each receptor subunit. The subunits are then expressed exogenously in cultured cells, and the receptors are isolated from detergent extracts of membrane fractions by affinity chromatography. The receptors are imaged both alone and in complex with anti-epitope antibodies. The size of the imaged particles provides an estimate of the subunit stoichiometry, whereas the geometry of the receptor-antibody complexes produces more detailed information about the receptor architecture. We use an automated, unbiased system to identify receptors and receptor-antibody complexes and to determine the geometry of the complexes. We are also able to determine the orientation of the receptors on the mica substrate, which will allow us to solve the subunit arrangement within receptors, such as the GABA A receptor, which contain three types of subunits.

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Sensory presynaptic and widespread somatodendritic immunolocalization of central ionotropic P2X ATP receptors

Cited by 145 publications

References 34 publications

Primary structure and expression of a naturally truncated human P2X ATP receptor subunit from brain and immune system

Primary structure and expression of a naturally truncated human P2X ATP receptor subunit from brain and immune system

P2Y1 receptor activation by photolysis of caged ATP enhances neuronal network activity in the developing olfactory bulb

Determination of the architecture of ionotropic receptors using AFM imaging

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