Factors that Determine AChE Efficacy in Synaptic Function

Lili Anglister

doi:10.1007/978-1-4899-1540-5_10

Factors that Determine AChE Efficacy in Synaptic Function

Lili Anglister

Institute for Medical Research Israel-Canada (IMRIC)

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

Abstract

Acetylcholinesterase (AChE) at neuromuscular junctions (nmj’s) is concentrated in the synaptic cleft. AChE consists of several molecular forms, some of which are specifically adherent to synaptic basal lamina (for review, see 20). Since all molecular forms of AChE have similar catalytic activity the major factors that determine the efficacy of AChE action in synaptic function involve the position of AChE molecules in the synaptic cleft, the cellular origin and regulation of AChE molecular forms, and the density of AChE. Various aspects concerning these factors have been studied recently in our laboratory and are reviewed in this chapter.

Original language	American English
Title of host publication	Structure and Function of Cholinesterases and Related Proteins
Editors	Bhupendra P. Doctor, Palmer Taylor, Daniel M. Quinn, Richard L. Rotundo, Mary K. Gentry
Place of Publication	Boston, MA
Publisher	Springer US; Imprint: Springer
Pages	71-77
Number of pages	7
ISBN (Print)	978-1-4899-1540-5
DOIs	https://doi.org/10.1007/978-1-4899-1540-5_10
State	Published - 1998

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10.1007/978-1-4899-1540-5_10

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title = "Factors that Determine AChE Efficacy in Synaptic Function",

abstract = "Acetylcholinesterase (AChE) at neuromuscular junctions (nmj{\textquoteright}s) is concentrated in the synaptic cleft. AChE consists of several molecular forms, some of which are specifically adherent to synaptic basal lamina (for review, see 20). Since all molecular forms of AChE have similar catalytic activity the major factors that determine the efficacy of AChE action in synaptic function involve the position of AChE molecules in the synaptic cleft, the cellular origin and regulation of AChE molecular forms, and the density of AChE. Various aspects concerning these factors have been studied recently in our laboratory and are reviewed in this chapter.",

author = "Lili Anglister",

year = "1998",

doi = "10.1007/978-1-4899-1540-5\_10",

language = "American English",

isbn = "978-1-4899-1540-5",

pages = "71--77",

editor = "Doctor, \{Bhupendra P.\} and Palmer Taylor and Quinn, \{Daniel M.\} and Rotundo, \{Richard L.\} and Gentry, \{Mary K.\}",

booktitle = "Structure and Function of Cholinesterases and Related Proteins",

publisher = "Springer US; Imprint: Springer",

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TY - CHAP

T1 - Factors that Determine AChE Efficacy in Synaptic Function

AU - Anglister, Lili

PY - 1998

Y1 - 1998

N2 - Acetylcholinesterase (AChE) at neuromuscular junctions (nmj’s) is concentrated in the synaptic cleft. AChE consists of several molecular forms, some of which are specifically adherent to synaptic basal lamina (for review, see 20). Since all molecular forms of AChE have similar catalytic activity the major factors that determine the efficacy of AChE action in synaptic function involve the position of AChE molecules in the synaptic cleft, the cellular origin and regulation of AChE molecular forms, and the density of AChE. Various aspects concerning these factors have been studied recently in our laboratory and are reviewed in this chapter.

AB - Acetylcholinesterase (AChE) at neuromuscular junctions (nmj’s) is concentrated in the synaptic cleft. AChE consists of several molecular forms, some of which are specifically adherent to synaptic basal lamina (for review, see 20). Since all molecular forms of AChE have similar catalytic activity the major factors that determine the efficacy of AChE action in synaptic function involve the position of AChE molecules in the synaptic cleft, the cellular origin and regulation of AChE molecular forms, and the density of AChE. Various aspects concerning these factors have been studied recently in our laboratory and are reviewed in this chapter.

U2 - 10.1007/978-1-4899-1540-5_10

DO - 10.1007/978-1-4899-1540-5_10

M3 - Chapter

SN - 978-1-4899-1540-5

SP - 71

EP - 77

BT - Structure and Function of Cholinesterases and Related Proteins

A2 - Doctor, Bhupendra P.

A2 - Taylor, Palmer

A2 - Quinn, Daniel M.

A2 - Rotundo, Richard L.

A2 - Gentry, Mary K.

PB - Springer US; Imprint: Springer

CY - Boston, MA

ER -

Factors that Determine AChE Efficacy in Synaptic Function

Abstract

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