Acetylcholinesterase at Neuromuscular Junctions

L. Anglister; J. R. Stiles; B. Haesaert; J. Eichler; M. M. Salpeter

doi:10.1007/978-1-4899-1051-6_55

Acetylcholinesterase at Neuromuscular Junctions

L. Anglister, J. R. Stiles, B. Haesaert, J. Eichler, M. M. Salpeter

Institute for Medical Research Israel-Canada (IMRIC)

Research output: Chapter in Book/Report/Conference proceeding › Chapter

Abstract

Acetylcholinesterase (AChE) which is concentrated at vertebrate neuromuscular junctions between the presynaptic release sites and the postsynaptic receptors (AChR), hydrolyzes acetylcholine (ACh) and thereby assists in termination of neuromuscular transmission. Knowledge of junctional AChE and AChR concentrations is crucial for understanding transmission at this synapse. However, although AChR density has been measured in endplates of several species, and shows little variability (Fertuck and Salpeter, 1976; Matthews-Bellinger and Salpeter, 1978; Land et al., 1980), AChE density has been determined only in mouse endplates (Rogers et al., 1969; Salpeter et al., 1972, 1978).

Original language	American English
Title of host publication	Enzymes of the Cholinesterase Family
Editors	Daniel M. Quinn, A. S. Balasubramanian, Bhupendra P. Doctor, Palmer Taylor
Place of Publication	Boston, MA
Publisher	Springer US; Imprint: Springer
Pages	277-285
Number of pages	9
ISBN (Print)	978-1-4899-1051-6
DOIs	https://doi.org/10.1007/978-1-4899-1051-6_55
State	Published - 1995

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title = "Acetylcholinesterase at Neuromuscular Junctions",

abstract = "Acetylcholinesterase (AChE) which is concentrated at vertebrate neuromuscular junctions between the presynaptic release sites and the postsynaptic receptors (AChR), hydrolyzes acetylcholine (ACh) and thereby assists in termination of neuromuscular transmission. Knowledge of junctional AChE and AChR concentrations is crucial for understanding transmission at this synapse. However, although AChR density has been measured in endplates of several species, and shows little variability (Fertuck and Salpeter, 1976; Matthews-Bellinger and Salpeter, 1978; Land et al., 1980), AChE density has been determined only in mouse endplates (Rogers et al., 1969; Salpeter et al., 1972, 1978).",

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AU - Eichler, J.

AU - Salpeter, M. M.

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N2 - Acetylcholinesterase (AChE) which is concentrated at vertebrate neuromuscular junctions between the presynaptic release sites and the postsynaptic receptors (AChR), hydrolyzes acetylcholine (ACh) and thereby assists in termination of neuromuscular transmission. Knowledge of junctional AChE and AChR concentrations is crucial for understanding transmission at this synapse. However, although AChR density has been measured in endplates of several species, and shows little variability (Fertuck and Salpeter, 1976; Matthews-Bellinger and Salpeter, 1978; Land et al., 1980), AChE density has been determined only in mouse endplates (Rogers et al., 1969; Salpeter et al., 1972, 1978).

AB - Acetylcholinesterase (AChE) which is concentrated at vertebrate neuromuscular junctions between the presynaptic release sites and the postsynaptic receptors (AChR), hydrolyzes acetylcholine (ACh) and thereby assists in termination of neuromuscular transmission. Knowledge of junctional AChE and AChR concentrations is crucial for understanding transmission at this synapse. However, although AChR density has been measured in endplates of several species, and shows little variability (Fertuck and Salpeter, 1976; Matthews-Bellinger and Salpeter, 1978; Land et al., 1980), AChE density has been determined only in mouse endplates (Rogers et al., 1969; Salpeter et al., 1972, 1978).

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M3 - Chapter

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EP - 285

BT - Enzymes of the Cholinesterase Family

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A2 - Balasubramanian, A. S.

A2 - Doctor, Bhupendra P.

A2 - Taylor, Palmer

PB - Springer US; Imprint: Springer

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ER -

Acetylcholinesterase at Neuromuscular Junctions

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