TETRAMERIC (G(4)) ACETYICHOLINESTERASE - STRUCTURE, LOCALIZATION, ANDPHYSIOLOGICAL REGULATION

Citation
Hl. Fernandez et al., TETRAMERIC (G(4)) ACETYICHOLINESTERASE - STRUCTURE, LOCALIZATION, ANDPHYSIOLOGICAL REGULATION, Journal of neurochemistry, 66(4), 1996, pp. 1335-1346
Citations number
118
Categorie Soggetti
Biology,Neurosciences
Journal title
ISSN journal
00223042
Volume
66
Issue
4
Year of publication
1996
Pages
1335 - 1346
Database
ISI
SICI code
0022-3042(1996)66:4<1335:T(A-SL>2.0.ZU;2-2
Abstract
Acetylcholinesterase (AChE), a highly conserved enzyme in the animal k ingdom, is distributed throughout a wide range of vertebrate tissues w here 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 b y a hydrophobic noncatalytic subunit (P-subunit). This study focuses p rimarily on current data involving the structure of the G(4) AChE P-su bunit, the expression and regulation of G(4) AChE during development a nd adulthood, and its role(s) in certain neurological disorders includ ing Alzheimer's disease.