Pharmacological characterization of purinergic inhibitory neuromuscular transmission in the human colon

Gallego, Diana; Gil, Víctor; Aleu, Jordi; Martínez-Cutillas, M.; Clavé, Père; Jiménez, Marcel

doi:10.1111/j.1365-2982.2011.01725.x

Cited by 48 publications

(86 citation statements)

References 42 publications

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“…The homo-or hetero-trimeric P2X receptors (seven subtypes, P2X1 to P2X7) are activated by ATP and represent Na + -, K + -, and Ca 2+ -permeable ion channels. Ligand preferences (in brackets) of the eight human P2Y receptors are as follows: P2Y 1 (ADP), P2Y 2 (UTP0ATP), P2Y 4 (UTP), P2Y 6 (UDP), P2Y 11 (ATP, NAD + ), P2Y 12 (ADP), P2Y 13 (ADP), and P2Y 14 (UDP, UDP-glucose and other nucleotide sugars). In addition, the P2Y-like receptor G protein-coupled receptor (GPR) 17 responds to both uracil nucleotides (such a UDP-glucose) and cysteinylleukotrienes [8].…”

Section: Substrates Relevant For Purinergic Signalingmentioning

confidence: 99%

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Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

876

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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Section: Substrates Relevant For Purinergic Signalingmentioning

confidence: 99%

“…Dinucleoside polyphosphates act on some P2X and P2Y receptors [9,10]. Moreover, evidence has been provided that NAD + [11][12][13] and ADP ribose [14] function as ligands at P2Y receptors.…”

Section: Substrates Relevant For Purinergic Signalingmentioning

confidence: 99%

Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

876

922

View full text Add to dashboard Cite

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“…A consensus about the involvement of the P2Y 1 receptor in smooth muscle relaxation in the whole GI tract now exists (King, 2012;Gil et al, 2013;Goyal et al, 2013). The identification of P2Y 1 receptors has been crucial in understanding the process of co-transmission between purines and NO and in establishing pharmacological criteria for identifying potential agonists able to mimic endogenous responses (Gallego et al, 2006;Mutafova-Yambolieva et al, 2007;Gallego et al, 2011;Durnin et al, 2012;Gil et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

α,β-meATP mimics the effects of the purinergic neurotransmitter in the human and rat colon

Martínez-Cutillas¹,

Gil²,

Gallego³

et al. 2014

European Journal of Pharmacology

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“…The development of specific P2Y 1 antagonists (35,40) has allowed the isolation of both the purinergic and nitrergic components of inhibitory neurotransmission (24,26). Currently, none of the available ATP-labeling techniques ensure 100% reliability in the identification of purinergic neurons.…”

Section: Functional No-atp Co-transmissionmentioning

confidence: 99%

Mechanisms responsible for neuromuscular relaxation in the gastrointestinal tract

Gallego¹,

Mañé²,

Gil³

et al. 2016

Rev Esp Enferm Dig

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The enteric nervous system (ENS) is responsible for the genesis of motor patterns ensuring an appropriate intestinal transit. Enteric motor neurons are classified into afferent neurons, interneurons and motorneurons. Motorneurons are excitatory or inhibitory causing smooth muscle contraction and relaxation respectively. Muscle relaxation mechanisms are key for the understanding of physiological processes such as sphincter relaxation, gastric accommodation, or the descending phase of the peristaltic reflex. Nitric oxide (NO) and ATP or a related purine are the primary inhibitory neurotransmitters. Nitrergic neurons synthesize NO through nNOS enzyme activity. NO diffuses across the cell membrane to bind guanylyl cyclase, and then activates a number of intracellular mechanisms that ultimately result in muscle relaxation. ATP is an inhibitory neurotransmitter together with NO. The P2Y1 receptor has been identified as a the purine receptor responsible for smooth muscle relaxation. Although, probably, no clinician doubts about the significance of NO in the pathophysiology of gastrointestinal motility, the relevance of purinergic neurotransmission is apparently much lower, as ATP has not been associated with any specific motor dysfunction yet. The goal of this review is to discuss the function of both relaxation mechanisms in order to establish the physiological grounds of potential motor dysfunctions arising from impaired intestinal relaxation.

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Pharmacological characterization of purinergic inhibitory neuromuscular transmission in the human colon

Cited by 48 publications

References 42 publications

Cellular function and molecular structure of ecto-nucleotidases

Cellular function and molecular structure of ecto-nucleotidases

α,β-meATP mimics the effects of the purinergic neurotransmitter in the human and rat colon

Mechanisms responsible for neuromuscular relaxation in the gastrointestinal tract

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