Schwann Cells Sense and Control Acetylcholine Spillover at the Neuromuscular Junction by α7 Nicotinic Receptors and Butyrylcholinesterase

Петров, К. А.; Girard, Emmanuelle; Nikitashina, Alexandra D.; Colasante, Cesare; Bernard, Véronique; Нуруллин, Л. Ф.; Leroy, Jacqueline; Samigullin, Dmitry; Çolak, Ömer; Nikolsky, E. E.; Plaud, Benoît; Krejci, Éric

doi:10.1523/jneurosci.0329-14.2014

Cited by 56 publications

(49 citation statements)

References 60 publications

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“…To complicate the scenario there is the recent discovery of BChE anchored by PRiMA on the surface of TSCs at mouse NMJs (Petrov et al, 2014). In conclusion, the cellular origin of the AChE released in the plasma in ALS and the consequences of its absence at the NMJ is still unclear, since many other functions, not related to the ACh hydrolysis, have been described (Soreq and Seidman, 2001).…”

Section: Cholinergic Dysfunction In Alsmentioning

confidence: 99%

Neuromuscular Junction Impairment in Amyotrophic Lateral Sclerosis: Reassessing the Role of Acetylcholinesterase

Campanari

García‐Ayllón

Ciura

et al. 2016

Front. Mol. Neurosci.

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Amyotrophic Lateral Sclerosis (ALS) is a highly debilitating disease caused by progressive degeneration of motorneurons (MNs). Due to the wide variety of genes and mutations identified in ALS, a highly varied etiology could ultimately converge to produce similar clinical symptoms. A major hypothesis in ALS research is the “distal axonopathy” with pathological changes occurring at the neuromuscular junction (NMJ), at very early stages of the disease, prior to MNs degeneration and onset of clinical symptoms. The NMJ is a highly specialized cholinergic synapse, allowing signaling between muscle and nerve necessary for skeletal muscle function. This nerve-muscle contact is characterized by the clustering of the collagen-tailed form of acetylcholinesterase (ColQ-AChE), together with other components of the extracellular matrix (ECM) and specific key molecules in the NMJ formation. Interestingly, in addition to their cholinergic role AChE is thought to play several “non-classical” roles that do not require catalytic function, most prominent among these is the facilitation of neurite growth, NMJ formation and survival. In all this context, abnormalities of AChE content have been found in plasma of ALS patients, in which AChE changes may reflect the neuromuscular disruption. We review these findings and particularly the evidences of changes of AChE at neuromuscular synapse in the pre-symptomatic stages of ALS.

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Section: Cholinergic Dysfunction In Alsmentioning

confidence: 99%

Neuromuscular Junction Impairment in Amyotrophic Lateral Sclerosis: Reassessing the Role of Acetylcholinesterase

Campanari

García‐Ayllón

Ciura

et al. 2016

Front. Mol. Neurosci.

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“…However, ACh released at mammalian NMJs can coactivate mAChRs to stimulate vasodilation in nearby blood vessels (WELSH AND SEGAL 1997), although the physiological significance of this stimulation is uncertain (HONG AND KIM 2017). ACh spillover has also been observed when quantal content is increased or when acetylcholinesterases are inhibited (STANCHEV AND SARGENT 2011;PETROV et al 2014). We have similarly observed that C. elegans ace-3 mutants with reduced acetylcholinesterase activity produce prolonged peristalses that are dependent on GAR-3.…”

Section: Ach Spillover May Produce Prolonged Peristalses In Eat-2 Mutmentioning

confidence: 77%

Crosstalk with the GAR-3 receptor contributes to feeding defects inCaenorhabditis elegans eat-2mutants

Kozlova

Lotfi

Okkema

2019

Preprint

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Article SummaryAcetylcholine stimulates different contractions in adjacent muscle cells in the C. elegans pharynx called pumping and peristalsis. The signaling mechanisms stimulating pumping have been characterized, but how these mechanisms affect peristalsis is unknown. Here we examined muscle contractions and Ca 2+ transients during peristalsis in wild-type animals and acetylcholine signaling mutants. Surprisingly we found that while mutants affecting the eat-2 nicotinic acetylcholine receptor exhibited reduced pumping, they also hyperstimulated peristalses. This hyperstimulation depends on crosstalk with the GAR-3 muscarinic acetylcholine receptor in adjacent cells, and it contributes to the well-characterized dietary restriction and extended adult lifespan observed in eat-2 mutants. AbstractPrecise signaling at the neuromuscular junction (NMJ) is essential for proper muscle contraction.In the C. elegans pharynx, acetylcholine (ACh) released from the MC and M4 motor neurons stimulates two different types of contractions in adjacent muscle cells, termed pumping and isthmus peristalsis. MC stimulates rapid pumping through the nicotinic ACh receptor EAT-2, which is tightly localized at the MC NMJ, and eat-2 mutants exhibit a slow pump rate.Surprisingly, we found that eat-2 mutants also hyperstimulated peristaltic contractions, and these are characterized by increased and prolonged Ca 2+ transients in the isthmus muscles.This hyperstimulation depends on crosstalk with the GAR-3 muscarinic acetylcholine receptor as gar-3 mutation specifically suppressed the prolonged contraction and increased Ca 2+ observed in eat-2 mutant peristalses. Similar GAR-3 dependent hyperstimulation was also observed in mutants lacking the ace-3 acetylcholinesterase, and we suggest that NMJ defects in eat-2 and ace-3 mutants result in ACh stimulation of extrasynaptic GAR-3 receptors in isthmus muscles. gar-3 mutation also suppressed slow larval growth and prolonged lifespan phenotypes that result from dietary restriction in eat-2 mutants, indicating that crosstalk with the GAR-3 receptor has a long-term impact on feeding behavior and eat-2 mutant phenotypes.

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“…Another function of BChE is hydrolysis of the neurotransmitter acetylcholine. BChE acts as an independent and complementary modulator of acetylcholine levels at the mouse neuromuscular junction [27]. …”

Section: Discussionmentioning

confidence: 99%

Monoclonal antibodies to human butyrylcholinesterase reactive with butyrylcholinesterase in animal plasma

Peng

Brimijoin

Hrabovská

et al. 2016

Chemico-Biological Interactions

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Five mouse anti-human butyrylcholinesterase (BChE) monoclonal antibodies bind tightly to native human BChE with nanomolar dissociation constants. Pairing analysis in the Octet system identified the monoclonal antibodies that bind to overlapping and independent epitopes on human BChE. The nucleotide and amino acid sequences of 4 monoclonal antibodies are deposited in GenBank. Our goal was to determine which of the 5 monoclonal antibodies recognize BChE in the plasma of animals. Binding of monoclonal antibodies 11D8, B2 18-5, B2 12-1, mAb2 and 3E8 to BChE in animal plasma was measured using antibody immobilized on Pansorbin cells and on Dynabeads Protein G. A third method visualized binding by the shift of BChE activity bands on nondenaturing gels stained for BChE activity. Gels were counterstained for carboxylesterase activity. The three methods agreed that B2 18-5 and mAb2 have broad species specificity, but the other monoclonal antibodies interacted only with human BChE, the exception being 3E8, which also bound chicken BChE. B2 18-5 and mAb2 recognized BChE in human, rhesus monkey, horse, cat, and tiger plasma. A weak response was found with rabbit BChE. Monoclonal mAb2, but not B2 18-5, bound pig and bovine BChE. Gels stained for carboxylesterase activity confirmed that plasma from humans, monkey, pig, chicken, and cow does not contain carboxylesterase, but plasma from horse, cat, tiger, rabbit, guinea pig, mouse, and rat has carboxylesterase. Rabbit plasma carboxylesterase hydrolyzes butyrylthiocholine. In conclusion monoclonal antibodies B2 18-5 and mAb2 can be used to immunoextract BChE from the plasma of humans, monkey and other animals.

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Schwann Cells Sense and Control Acetylcholine Spillover at the Neuromuscular Junction by α7 Nicotinic Receptors and Butyrylcholinesterase

Cited by 56 publications

References 60 publications

Neuromuscular Junction Impairment in Amyotrophic Lateral Sclerosis: Reassessing the Role of Acetylcholinesterase

Neuromuscular Junction Impairment in Amyotrophic Lateral Sclerosis: Reassessing the Role of Acetylcholinesterase

Crosstalk with the GAR-3 receptor contributes to feeding defects inCaenorhabditis elegans eat-2mutants

Monoclonal antibodies to human butyrylcholinesterase reactive with butyrylcholinesterase in animal plasma

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