Abstract:
:Acetylcholinesterase (AChE) inhibitors were first administered in Europe to human subjects in the 1860s, and synthetic derivatives of the natural alkaloid inhibitors were developed in the 1930s to modulate peripheral cholinergic function. However, only within the last decade have these agents been systematically studied for therapy of central cholinergic deficits. This time interval parallels the cloning of the gene and determination of the structure of the target molecule, AChE. Because AChE in mammals is encoded by a single gene and the portion of the gene encoding the catalytic domain is invariant, selectivity of action can be achieved only by altering parameters of disposition and pharmacokinetics of action of the inhibitor rather than its specificity for particular AChE isozymes in various regions of the CNS. This article describes the mechanism of action of short-acting, carbamoylating, and phosphorylating inhibitors of cholinesterase and suggests possible strategies for enhancing therapeutic efficacy.
journal_name
Neurologyjournal_title
Neurologyauthors
Taylor Pdoi
10.1212/wnl.51.1_suppl_1.s30subject
Has Abstractpub_date
1998-07-01 00:00:00pages
S30-5; discussion S65-7issue
1 Suppl 1eissn
0028-3878issn
1526-632Xjournal_volume
51pub_type
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