ATP Crossing the Cell Plasma Membrane Generates an Ionic Current in Xenopus Oocytes

Bodas, Elena; Aleu, Jordi; Pujol, Gemma; Martı́n-Satué, Mireia; Marsal, Jordi; Solsona, Carles

doi:10.1074/jbc.m000894200

Cited by 47 publications

(51 citation statements)

References 49 publications

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“…It has recently been proposed that strong hyperpolarization of the oocyte (i.e. to Ϫ200 mV) may activate an ATP-selective conductance (16). However, our studies indicate similar hyperpolarizations activate a nonselective conductance that fails to saturate with prolonged hyperpolarization and recovers only slowly (i.e.…”

Section: Resultscontrasting

confidence: 78%

Brefeldin A Block of Integrin-dependent Mechanosensitive ATP Release from Xenopus Oocytes Reveals a Novel Mechanism of Mechanotransduction

Maroto

Hamill

2001

Journal of Biological Chemistry

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Many animal cells release ATP into the extracellular medium, and often this release is mechanosensitive. However, the mechanisms underlying this release are not well understood. Using the luciferin-luciferase bioluminescent assay we demonstrate that a Xenopus oocyte releases ATP at a basal rate ϳ0.01 fmol/s, and gentle mechanical stimulation can increase this to 50 fmol/s. Brefeldin A, nocodazole, and progesterone-inducedmaturation block basal and mechanosensitive ATP release. These treatments share the common feature of disrupting the Golgi complex and vesicle trafficking to the cell surface and thereby block protein secretion and membrane protein insertion. We propose that ATP release occurs when protein transport vesicles enriched in ATP fuse with the plasma membrane. Collagenase, integrin-binding peptides, and cytochalasin D also block ATP release, indicating that extracellular, membrane and cytoskeletal elements are involved in the release process. Elevation of intracellular Ca 2؉ does not evoke ATP release but potentiates mechanosensitive ATP release. Our study indicates a novel mechanism of mechanotransduction that would allow cells to regulate membrane trafficking and protein transport/secretion in response to mechanical loading.Many, if not all, animal cells release ATP (or UTP) into the extracellular medium, and often this release is MS 1 (1-6). External ATP acts on ATP receptors that regulate diverse functions, including pain and touch sensation, smooth muscle contractility, synaptic transmission, platelet aggregation, epithelial fluid secretion, and endothelial release of vasorelaxants (6 -8). Furthermore, abnormalities in ATP release may contribute to specific human diseases, most notably cystic fibrosis (9). Although several mechanisms have been proposed to contribute to ATP release, including synaptic vesicular release and various membrane ion channels (10 -16), the mechanism of MS ATP release remains unknown.Our interest in MS ATP release was stimulated by the discovery of Nakamura and Strittmatter (1) that mechanical stimulation of the Xenopus oocyte evokes ATP release without causing an increase in membrane conductance. Here, we test the hypothesis that ATP release from the oocyte is mediated by the high rate (4,000 -16,000/s) of membrane fusion of vesicles involved in transporting proteins from the Golgi complex to the cell surface (17). This idea seemed plausible given the identification of a specific ATP transporter that concentrates ATP in the Golgi/ER lumen 50 -100-fold above that in the cytoplasm (18,19). To test the hypothesis we have examined the effects of BFA and other treatments that are known to disrupt membrane trafficking and thereby block protein secretion (20 -22).A key issue for any MS process is the pathway by which mechanical forces are transmitted to that process. For example, specific membrane channel proteins in bacteria and animal cells respond directly to tension developed in the lipid bilayer (23), while other MS processes may be activated by forces transmitted via elem...

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Section: Resultscontrasting

confidence: 78%

Brefeldin A Block of Integrin-dependent Mechanosensitive ATP Release from Xenopus Oocytes Reveals a Novel Mechanism of Mechanotransduction

Maroto

Hamill

2001

Journal of Biological Chemistry

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“…It has been suggested that NTPDase1 could function as an ATP release channel. Release of ATP from NTPDase1-transfected Xenopus oocytes could be induced by hyperpolarizing pulses and required functional ecto-ATPase activity [143].…”

Section: Oligomeric Structurementioning

confidence: 99%

Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

872

922

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Ecto-nucleotidases play a pivotal role in purinergic signal transmission. They hydrolyze extracellular nucleotides and thus can control their availability at purinergic P2 receptors. They generate extracellular nucleosides for cellular reuptake and salvage via nucleoside transporters of the plasma membrane. The extracellular adenosine formed acts as an agonist of purinergic P1 receptors. They also can produce and hydrolyze extracellular inorganic pyrophosphate that is of major relevance in the control of bone mineralization. This review discusses and compares four major groups of ectonucleotidases: the ecto-nucleoside triphosphate diphosphohydrolases, ecto-5′-nucleotidase, ecto-nucleotide pyrophosphatase/phosphodiesterases, and alkaline phosphatases. Only recently and based on crystal structures, detailed information regarding the spatial structures and catalytic mechanisms has become available for members of these four ecto-nucleotidase families. This permits detailed predictions of their catalytic mechanisms and a comparison between the individual enzyme groups. The review focuses on the principal biochemical, cell biological, catalytic, and structural properties of the enzymes and provides brief reference to tissue distribution, and physiological and pathophysiological functions.

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“…Since we could not inhibit the response by other known transport inhibitors, such as ABC transporter inhibitors, it seems likely that the ENT transporters are involved in both processes. Yet another possibility is that ATP is secreted by CD39 protein, recently recognized as an ATP-transporting protein (Bodas et al, 2000). As the ENT1 nucleoside transporters are distributed on nerve terminals and also on astrocytes and endothelial cells (Anderson et al, 1999), the cellular source of ATP-evoked purine efflux could be either nerve terminals, glial cells or endothelial cells.…”

Section: B Sperlágh Et Almentioning

confidence: 99%

Homo‐ and heteroexchange of adenine nucleotides and nucleosides in rat hippocampal slices by the nucleoside transport system

Sperlágh

Szabó

Erdélyi

et al. 2003

British J Pharmacology

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1 Here, we investigated how nucleotides and nucleosides affect the release of tritiated purines and endogenous adenosine 5 0 -triphosphate (ATP) from superfused rat hippocampal slices.2 ATP elicited concentration-dependent [ 4 Reverse transcription-coupled-polymerase chain reaction analysis revealed that mRNAs encoding a variety of P2X and P2Y receptor proteins are expressed in the rat hippocampus. Nevertheless, neither P2 receptor (i.e. pyridoxal-5-phosphate-6-azophenyl-2 0 ,4 0 -disulphonic acid, 30 mM, suramin, 300 mM and reactive blue 2, 10 mM), nor adenosine receptor (8-cyclopentyl-1,3-dipropylxanthine, 250 nM and dimethyl-1-propargylxanthine, 250 nM) antagonists modified the effect of ATP (300 mM) to evoke [ 3 H]purine release. 5 The nucleoside transport inhibitors, dipyridamole (10 mM), nitrobenzylthioinosine (10 mM) and adenosine deaminase (2 -10 U ml 6 In summary, we found that ATP and other nucleotides and nucleosides promote the release of one another and themselves by the nucleoside transport system. This action could have relevance during physiological and pathological elevation of extracellular purine levels high enough to reverse the nucleoside transporter.

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ATP Crossing the Cell Plasma Membrane Generates an Ionic Current in Xenopus Oocytes

Cited by 47 publications

References 49 publications

Brefeldin A Block of Integrin-dependent Mechanosensitive ATP Release from Xenopus Oocytes Reveals a Novel Mechanism of Mechanotransduction

Brefeldin A Block of Integrin-dependent Mechanosensitive ATP Release from Xenopus Oocytes Reveals a Novel Mechanism of Mechanotransduction

Cellular function and molecular structure of ecto-nucleotidases

Homo‐ and heteroexchange of adenine nucleotides and nucleosides in rat hippocampal slices by the nucleoside transport system

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