Background: Alzheimer’s disease (AD) is a neurodegenerative disease characterized by decreased cognitive function in patients due to forming Aβ peptides and neurofibrillary tangles (NFT) in the brain. Therefore, the need to develop new treatments can reduce this risk. Acetylcholinesterase is one of the targets used in the design of new drugs for the treatment of AD. The researchers obtain new i...

Acetylcholinesterase, an erythroid marker constitutively expressed in K-562 cells, can be further induced by sodium butyrate. The highest level of acetylcholinesterase induction is reached in approximately equal to 3 days, in parallel with increased hemoglobin expression. Acetylcholinesterase induction is reversible, and repeated addition of butyrate is necessary to maintain a high level of the...

Objective(s): Alzheimer’s disease (AD) as progressive cognitive decline and the most common form of dementia is due to degeneration of the cholinergic neurons in the brain. Therefore, administration of the acetylcholinesterase (AChE) inhibitors such as donepezil is the first choice for treatment of the AD. In the present study, we focused on the synthesis and anti-cholinesterase evaluation of n...

OBJECTIVE The aim of this study was to investigate whether plasma serotonin levels or acetylcholinesterase activities determined upon intensive care unit admission could predict the occurrence of acute brain dysfunction in intensive care unit patients. METHODS A prospective cohort study was conducted with a sample of 77 non-consecutive patients observed between May 2009 and September 2010. De...

Acetylcholinesterase, an erythroid marker constitutively ex pressed in K-562 cells, can be further induced by sodium butyrate. The highest level of acetylcholinesterase induction is reached in =3 days, in parallel with increased hemoglobin expres sion. Acetylcholinesterase induction is reversible, and repeated addition of butyrate is necessary to maintain a high level of the enzyme. Actinomycin...

Acetylcholinesterase levels were determined in cerebrospinal fluid and serum of 272 patients with various neurological disorders. The patients were ordered in 13 diagnostic groups. The assay employed was an antigen capture assay based on an immobilized monoclonal antibody selective for neuronal acetylcholinesterase (Rasmussen et al., Clin. Chim. Acta 166 (1987) 17-25 (1)). In 100% of the cases ...

In immature animals, ablation of the entorhinal cortex elicited a rapid intensification of acetylcholinesterase (EC 3.1.1.7) staining in the outer one-quarter of the molecular layer of the dentate gyrus. Subsequent lesions of the septum eliminated this acetylcholinesterase intensification. Electron-microscopic histochemical analysis demonstrated a 30-fold increase in the number of acetylcholine...

The interaction between acetylcholinesterase (EC 3.1.1.7) and heparin, a sulphated glycosaminoglycan, was studied by affinity chromatography. A specific binding of the asymmetric acetylcholinesterase to an agarose gel containing covalently bound heparin was demonstrated. This interaction required an intact collagenous tail, shown by the fact that the binding is abolished by pretreatment with co...

A chemiluminescence method for determining acetylcholinesterase activity is described. It is an adaptation of the chemiluminescence assay of acetylcholine described by Israël & Lesbats [(1981) Neurochem. Int. 3, 81-90; (1981) J. Neurochem. 37, 1475-1483]. The acetylcholinesterase activity is measured by monitoring the increase in light emission produced by the accumulation of choline or by dete...

An acetylcholinesterase inhibitor-Sepharose conjugate was prepared by coupling a derivative of the powerful acetylcholinesterase inhibitor, N-methylacridinium, to CNBr-activated Sepharose. Use of this conjugate permitted direct purification, by affinity chromatography, of the two molecular forms of acetylcholinesterase, 14 and 18 S, present in fresh electric organ tissue. The purified 14S and 1...