Chemico-Biological Interactions 119 – 120 (1999) 301 – 308
Acetylcholinesterase in the neuromuscular junction
Rok Gas pers ic , Blaz Koritnik, Neva C rne-Finderle, Janez Sketelj *
Institute of Pathophysiology, School of Medicine, Uniersity of Ljubljana, Zalos ka 4,
1000 Ljubljana, Sloenia
Abstract
New findings regarding acetylcholinesterase (AChE) in the neuromuscular junction (NMJ),
obtained in the last decade, are briefly reviewed. AChE is highly concentrated in the NMJs
of vertebrates. Its location remains stable after denervation in mature rat muscles but not in
early postnatal muscles. Agrin in the synaptic basal lamina is able to induce sarcolemmal
differentiations accumulating AChE even in the absence of a nerve ending. Asymmetric A
12
AChE form is the major molecular form of AChE in vertebrate NMJs. Extrajunctional
suppression of this form is a developmental phenomenon. Motor nerve is able to reinduce
expression of the A
12
AChE form in the ectopic NMJs even in muscles with complete
extrajunctional suppression of this form. The ‘tail’ of the A
12
AChE form is made of collagen
Q. It contains domains for binding AChE to basal lamina with ionic and covalent
interactions. Muscle activity is required for normal AChE expression in muscles and its
accumulation in the NMJs. In addition, the pattern of muscle activation also regulates AChE
activity in the NMJs, demonstrating that the pattern of synaptic transmission is able to
modulate one of the key synaptic components. © 1999 Elsevier Science Ireland Ltd. All
rights reserved.
Keywords: Acetylcholinesterase; Muscle; Neuromuscular junction; Motor endplate; Synapse;
Denervation
* Corresponding author. Tel.: +386-61-310841; fax: +386-61-302272.
E-mail address: sketelj ibmi.mf.uni-lj.si (J. Sketelj)
0009-2797/99/$ - see front matter © 1999 Elsevier Science Ireland Ltd. All rights reserved.
PII:S0009-2797(99)00040-X