Impact of ectonucleotidases in autonomic nervous functions

Cardoso, Andréia Machado; Schetinger, Maria Rosa Chitolina; Correia-de-Sá, Paulo; Sévigny, Jean

doi:10.1016/j.autneu.2015.04.014

Cited by 31 publications

(26 citation statements)

References 136 publications

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“…In the gut, the expression of NTPDase2 has been further noted on glial cells, while NTPDase3 localizes to both glia and neurons (54, 62, 63). In both humans and mice, NTPDase3 antibodies positively stain nerve fibers penetrating the smooth muscle layers, whereas the expression of NTPDase2 in these areas is less prominent (Feldbrügge et al, 2017, in press and see Fig.…”

Section: Other Ntpdases Expressed In the Gastrointestinal Tract And Pmentioning

confidence: 99%

Purinergic signaling during intestinal inflammation

et al. 2017

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Section: Other Ntpdases Expressed In the Gastrointestinal Tract And Pmentioning

confidence: 99%

Purinergic signaling during intestinal inflammation

et al. 2017

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“…For example, under physiological conditions, astrocytes and neurons are responsible for releasing small amounts of ATP, which can then act on purinergic receptors – either P2X ion channels or P2Y G protein-coupled receptors - expressed on both neurons and glial cells. In healthy tissues, ATP released from cells is tightly regulated with cell surface ectonucleotidases serving to terminate purinergic signaling (Cardoso et al, 2015) (this is analogous to the activity of cholinesterases at cholinergic synapses). However, when released from injured cells, ATP can initiate inflammation and further amplify and sustain cell-mediated immunity through P2 receptors (Idzko et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

P2X4 Receptor Function in the Nervous System and Current Breakthroughs in Pharmacology

et al. 2017

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Adenosine 5′-triphosphate is a well-known extracellular signaling molecule and neurotransmitter known to activate purinergic P2X receptors. Information has been elucidated about the structure and gating of P2X channels following the determination of the crystal structure of P2X4 (zebrafish), however, there is still much to discover regarding the role of this receptor in the central nervous system (CNS). In this review we provide an overview of what is known about P2X4 expression in the CNS and discuss evidence for pathophysiological roles in neuroinflammation and neuropathic pain. Recent advances in the development of pharmacological tools including selective antagonists (5-BDBD, PSB-12062, BX430) and positive modulators (ivermectin, avermectins, divalent cations) of P2X4 will be discussed.

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“…For example, ATP activates the ligand-gated P2X receptors and some G-protein-coupled P2Y receptors (e.g., P2Y1, P2Y2, P2Y11, and P2Y12), whereas ADP stimulates primarily P2Y1, P2Y12, and P2Y13 receptors (38). Ecto-nucleotidases have the ability to either terminate P2 receptor-mediated responses to ATP and/or to favor the activation of ADP and adenosine-sensitive receptors (19). To prolong the action of ATP that is released in the extracellular space either as a neurotransmitter or an autocrine and paracrine mediator, many investigators use E-NTPDase inhibitors such as ARL-67156 or POM-1 (see Introduction).…”

Section: Discussionmentioning

confidence: 99%

“…E-NTPDase 1, 2, 3 and 8 are cell surface members of the NTPDase/CD39 family. [17][18][19] In the GI tract in particular, NTPDase 1, 2 and 3 are responsible for ecto-ATPase activity. 20 Thus, mRNA for NTPDase 1, 2 and 3 is present throughout all regions of the mouse intestine, including the colon.…”

Section: Introductionmentioning

confidence: 99%

A commonly used ecto‐ATPase inhibitor, ARL‐67156, blocks degradation of ADP more than the degradation of ATP in murine colon

Durnin

Moreland

Lees

et al. 2016

Neurogastroenterology Motil

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Background Adenosine 5’-triphosphate (ATP) is released extracellularly as a neurotransmitter and an autocrine or paracrine mediator in numerous systems, including the gastrointestinal tract. It is rapidly degraded to active and inactive metabolites by membrane-bound enzymes. Investigators frequently use inhibitors of ATP hydrolysis such as ARL-67156 and POM-1 to suppress the catabolism of ATP and prolong its effects in pharmacological studies. Our aim was to investigate directly the effects of ARL-67156 and POM-1 on the degradation of ATP and ADP in mouse colonic muscles. Methods The degradation of ATP and ADP was evaluated by superfusing tissues with 1,N6-etheno-ATP (eATP) and 1,N6-etheno-ADP (eADP) as substrates and monitoring the decrease of substrate and increase of products (i.e., eADP, eAMP, and e-adenosine) by high-performance liquid chromatography techniques with fluorescence detection. Relaxation responses to etheno-derivatized and non-derivatized ATP and ADP were examined in isometric tension experiments. Key results ARL-67156 inhibits the degradation of ADP but not of ATP whereas POM-1 inhibits the degradation of ATP but not of ADP in murine colonic muscles. Consequently, ARL-67156 enhances relaxation responses to both ATP and ADP whereas POM-1 reduces relaxation to ATP and does not affect relaxation to ADP. Conclusions & Inferences Studies that use ARL-67156 to inhibit ATP degradation in smooth muscle likely evaluate responses to accumulated ADP rather than ATP. POM-1 appears to be a more selective inhibitor of ATP degradation in the mouse colon. The choice of pharmacological tools in studies on extracellular ATP signaling may affect the interpretation of experimental data in functional studies.

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Impact of ectonucleotidases in autonomic nervous functions

Cited by 31 publications

References 136 publications

Purinergic signaling during intestinal inflammation

Purinergic signaling during intestinal inflammation

P2X4 Receptor Function in the Nervous System and Current Breakthroughs in Pharmacology

A commonly used ecto‐ATPase inhibitor, ARL‐67156, blocks degradation of ADP more than the degradation of ATP in murine colon

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