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Tetrameric (G 4 ) Acetylcholinesterase: Structure, Localization, and Physiological Regulation
Author(s) -
Fernandez Hugo L.,
Moreno Ricardo D.,
Inestrosa Nibaldo C.
Publication year - 1996
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1996.66041335.x
Subject(s) - acetylcholinesterase , neuroscience , chemistry , biophysics , microbiology and biotechnology , biochemistry , biology , enzyme
Abstract: Acetylcholinesterase (AChE), a highly conserved enzyme in the animal kingdom, is distributed throughout a wide range of vertebrate tissues where it is expressed as multiple molecular forms comprising different arrangements of catalytic and structural subunits. The major AChE form in the CNS is an amphiphilic globular tetramer (G 4 AChE) consisting of four identical catalytic subunits attached to cellular membranes by a hydrophobic noncatalytic subunit (P‐subunit). This study focuses primarily on current data involving the structure of the G 4 AChE P‐subunit, the expression and regulation of G 4 AChE during development and adulthood, and its role(s) in certain neurological disorders including Alzheimer's disease.