Membrane-bound choline acetyltransferase is a cell surface marker of the differentiated NS-20Y cholinergic cell line

Barochovsky, O.; Docherty, Maureen; Bradford, H. F.

doi:10.1016/0304-3940(88)90209-1

Cited by 16 publications

(6 citation statements)

References 13 publications

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“…It is, however, known that the majority of ChAT (80-90%) is a soluble form and not involved in the rate-limiting step, but subpopulation of ChAT (10-20%) is a membrane-bound form and may be intimately involved in ACh synthesis and release (Barochovsky et al, 1988;Benishin and Carroll, 1981;Prado et al, 2002). It has been reported that a plant alkaloid veratridine, which is known to affect Na + channels like pyrethroids, keeps the channels open and delay their inactivation (Meir et al, 1999).…”

Section: Discussionmentioning

confidence: 97%

Neuromechanical effects of pyrethroids, allethrin, cyhalothrin and deltamethrin on the cholinergic processes in rat brain

et al. 2005

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Section: Discussionmentioning

confidence: 97%

Neuromechanical effects of pyrethroids, allethrin, cyhalothrin and deltamethrin on the cholinergic processes in rat brain

et al. 2005

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“…The presence of a membrane form of ChAT has been reinvestigated, and a fraction that is high-salt insoluble and detergent extractable has been reported in Torpedo, rat, mouse, and human (Benishin and Carroll, 1983;Eder-Colli and Amato, 1985). Three putative membrane-associated forms of ChAT have been characterized on the basis of their elution from membranes with (a) 100 mM sodium phosphate, (b) 500 mM NaC1, and (c) detergent (Benishin and Carroll, 1983;Barochovsky et al, 1988). It has been suggested that these enzyme forms represent an ionically and a nonionically membrane-bound form of ChAT inside cholinergic nerve terminals (Eder-Colli and Amato, 1985).…”

Section: Intracellular Localization Of Chatmentioning

confidence: 99%

“…Docherty et al (1987) reported the purification of cholinergic synaptosomes using antisera that recognized ChAT, indicating an extracellular localization for a fraction of the enzyme. The membranebound ChAT also has been suggested to act as a cell surface marker of the differentiated NS-20Y cholinergic cell line (Barochovsky et al, 1988). However, it has recently been shown that the antisera used in the studies of Docherty et al…”

Section: Intracellular Localization Of Chatmentioning

confidence: 99%

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Choline Acetyltransferase: Celebrating Its Fiftieth Year

Hersh

1994

Journal of Neurochemistry

154

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It is well known that the regulation of choline acetyltransferase (ChAT) activity under physiological and pathological conditions is important for the development and neuronal activities of cholinergic systems involved in many fundamental brain functions. This review focuses on recent progress in understanding the regulation of ChAT at the levels of both the protein and the mRNA. A deficiency in ChAT activity has been reported for neurodegenerative conditions such as Alzheimer's disease, amyotrophic lateral sclerosis, and schizophrenia. Although a major feature of ChAT regulation is likely to involve the spatial and temporal control of transcription, regulation of expression can also be at the level of RNA processing, transport/ translocation, turnover, or translation. In addition, there is increasing evidence that ChAT might be regulated at the posttranslational level by compartmentation and/or covalent modification, i.e., phosphorylation, as well as noncovalent modification (protein‐protein interaction, etc.). Synaptic activity and the state of neuronal transmission may also involve the regulation of ChAT at different levels via both positive and negative feedback loops, as was demonstrated in the characterization of two ChAT mutant Drosophila strains. Clearly, identification of cholinergic‐specific elements and the characterization of the trans‐acting factors that bind to them represent an important area of future research. Equally important is research on the mechanisms governing ChAT as an enzymatic entity. The future should be an exciting time during which we look forward to the elucidation of the cholinergic signal and its regulation as well as the determination of the three‐dimensional structure of the enzyme.

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“…Some investigators have suggested that particulate ChAT may play a critical role in the activation of acetylcholine (ACh) synthesis during depolarization (Carroll and Ivy, 1988;Myluta and Collier, 1989). Others have suggested that membrane-bound ChAT may serve as a cell-surface marker (Docherty and Bradford, 1986; Barochovsky et al, 1988). Exactly how ChAT is associated with membranes remains unclear.…”

mentioning

confidence: 99%

Effect of Phospholipase C from Bacillus cereus on the Release of Membrane‐Bound Choline‐O‐Acetyltransferase from Rat Hippocampal Tissue

Carroll

Smith

1990

Journal of Neurochemistry

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Some of the enzyme choline-O-acetyltransferase (ChAT) associated with central cholinergic nerve terminals appears to be non-ionically associated with membranes. In the present study, we tested the possibility that some membrane-bound ChAT might be anchored to membranes by a phosphatidylinositol linkage by incubating rat hippocampal tissue with phospholipase C (PLC) from Bacillus cereus. The PLC selectively augmented the release of ChAT; also, the glycosylphosphatidylinositol-PLC inhibitor, zinc, blocked this increase in release. When control and PLC-treated hippocampal tissues were subjected to Triton X-114 phase separation, a procedure that separates amphiphilic from hydrophilic proteins, the detergent-soluble, membrane-bound fraction of tissue ChAT appeared to be the source of the ChAT released by PLC into the incubation medium. Zinc also blocked the temperature-dependent release of ChAT, but not lactic dehydrogenase, from hippocampal tissue. Extracellular membrane-bound ChAT appeared to be the source of the ChAT released by a low exogenous concentration of PLC, as well as that released by a temperature-dependent process during tissue incubation. Phosphatidylinositol-specific PLC from Bacillus thuringiensis released ChAT, but not lactic dehydrogenase, from a crude synaptosomal fraction prepared from rat hippocampal tissue. These results suggest that some of the membrane-bound ChAT in rat hippocampal tissue may be extracellular and anchored to the membrane by phosphatidylinositol, and also that an endogenous factor in hippocampal tissue may function to remove this extracellular ChAT from the membrane.

show abstract

Membrane-bound choline acetyltransferase is a cell surface marker of the differentiated NS-20Y cholinergic cell line

Cited by 16 publications

References 13 publications

Neuromechanical effects of pyrethroids, allethrin, cyhalothrin and deltamethrin on the cholinergic processes in rat brain

Neuromechanical effects of pyrethroids, allethrin, cyhalothrin and deltamethrin on the cholinergic processes in rat brain

Choline Acetyltransferase: Celebrating Its Fiftieth Year

Effect of Phospholipase C from Bacillus cereus on the Release of Membrane‐Bound Choline‐O‐Acetyltransferase from Rat Hippocampal Tissue

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