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Biogenesis, assembly and trafficking of acetylcholinesterase
Author(s) -
Rotundo Richard L.
Publication year - 2017
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 - 10.1111/jnc.13982
Subject(s) - acetylcholinesterase , homomeric , microbiology and biotechnology , biology , neuroscience , cholinergic , biogenesis , biochemistry , enzyme , gene , protein subunit
Acetylcholinesterase ( AC hE) is expressed as several homomeric and heterooligomeric forms in a wide variety of tissues such as neurons in the central and peripheral nervous systems and their targets including skeletal muscle, endocrine and exocrine glands. In addition, glycolipid‐anchored forms are expressed in erythropoietic and lymphopoietic cells. While transcriptional and post‐transcriptional regulation is important for determining which AC hE oligomeric forms are expressed in a given tissue, translational and post‐translational regulatory mechanisms at the level of protein folding, assembly and sorting play equally important roles in assuring that the AC hE molecules reach their intended sites on the cell surface in the appropriate numbers. This brief review will focus on the latter events in the cell with the goal of providing novel therapeutic interventional strategies for the treatment of organophosphate and carbamate pesticide and nerve agent exposure. This is an article for the   special issue XVth International Symposium on Cholinergic Mechanisms .

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