Expression of a human acetylcholinesterase promoter-reporter construct in developing neuromuscular junctions of Xenopus embryos.

Abstract

We have employed Xenopus embryos to express human acetylcholinesterase (AcChoEase; EC 3.1.

Quaternary Associations of Acetylcholinesterase

“…These proportions also depend on the nature and state of differentiation of the cell; for example, it varies during development of the nervous system (for review, see Ref. 1), and AChE T subunits are expressed in a tissue-specific manner in Xenopus embryos, even under the control of a viral promoter (29,30). In culture, the yield of AChE activity was markedly less in rat basoleukemia cells than in COS cells, in parallel transient transfections (17).…”

Human Erythrocyte but Not Brain Acetylcholinesterase Hydrolyses Heroin to Morphine

“…53-4) and antihuman AChE (no. 101-1) 7 were gratefully received from Dr B. Norgaard-Pedersen BRIEF REVIEW (Copenhagen, Denmark). Heroin HCl, 6-monoacetylmorphine (6-MAM) and 3-monoacetylmorphine (3-MAM) were purified and standardized prior to experimentation as previously described.…”

“…Acetylcholinesterase, whose main catalytic activity is to hydrolyse the neurotransmitter acetylcholine, appears in three C-terminally distinct isoforms, derived from alternatively spliced AChE mRNA species. 7 Therefore, nervous system AChE differs from red blood cell AChE in its C-terminal peptide. Because both 6-MAM and morphine, but not heroin, are physiologically active in the mammalian brain, 8 another issue arises: whether the brain and red blood cell variants of AChE differ in their capacity to hydrolyse heroin and/or 6-MAM.…”

Muscle Induces Neuronal Expression of Acetylcholinesterase in Neuron-Muscle Co-culture

“…20 different views were randomly selected for each well. cDNA Transfection-The ϳ2.2-kb DNA fragment of human AChE promoter (24) and the CRE site mutated human AChE promoter (25) were subcloned into BglII and HindIII sites of pGL3 basic vector (Promega, Madison, WI) having a downstream tagged luciferase, which was named as pAChE-Luc (27) and pAChE ⌬CRE -Luc (25), respectively. This ϳ2.2-kb regulatory element was shown to reflect the genuine situation of AChE regulation in a C2C12 cell; the activity of this promoter was in parallel with the endogenous AChE expression during the myogenic differentiation of C2C12 myotube (26).…”

“…The transcriptional activity of the AChE gene has been demonstrated to play a role in AChE regulation, and several regulatory elements within the promoter have been reported to regulate the transcriptional activity of AChE gene in Torpedo (20), mice (21,22), rats (23), and humans (24). Among these possible AChE regulatory elements, a cAMP-responsive element (CRE) site located on the human AChE promoter has been shown to regulate the level of AChE transcripts in muscle (25,26) and neuron (27).…”