An Amphiphile‐Dependent Form of Human Brain Caudate Nucleus Acetylcholinesterase: Purification and Properties

Sørensen, Keld E.; Gentinetta, R.; Brodbeck, Urs

doi:10.1111/j.1471-4159.1982.tb11496.x

Cited by 90 publications

(17 citation statements)

References 35 publications

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“…This mechanism has also been pointed as relevant to justify the adverse effects in the farmers' health who were exposed to the agricultural pesticides (Surajudeen et al, 2014). Despite of this, the biological AChE role present in the erythrocyte membrane is not well explained, and it is known that this enzyme is present in the red blood cells and it has several similar proprieties like in the purified shape obtained from the brain tissue (Sorensen, Gentinetta, & Brodbeck, 1982). Therefore, the AChE activity in erythrocytes can be considered an indicator of the central cholinergic state (Kaizer et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

Effect of the Cymbopogon citratus Infusion on the Activity of Acetylcholinesterase Enzyme and on the Redox Profile in Farmers’ Erythrocytes

Mori¹,

Horn²,

Oliveira³

et al. 2017

JAS

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Agrochemicals were more prominent in 1960, marked due to the agricultural modernization process. As a result of this widespread use for food production, there was also an increase in cases of intoxication caused by these agents which made it necessary to search for alternative therapies for agricultural workers. Thus, considering that phytochemical characterization revealed the presence of antioxidants in Cymbopogon citratus extract, the objective of this study was to evaluate the effect of this plant infusion on the enzyme acetylcholinesterase activity (AChE) and on the redox response in farmers' erythrocytes. These erytrocytes were processed and subjected to treatment with the Cymbopogon citratus infusion (5, 10, 25 and 50 g/L). In these samples the following were determined: the AChE enzyme activity, the levels of thiobarbituric acid reactive substances (TBARS), protein carbonyls (CPs) and reduced glutathione (GSH). In general, it was discovered that the inhibition of AChE activity is negative regarding to the increase of protein carbonyl levels and positive regarding the GSH levels. In addition, Cymbopogon citratus infusions could not even reverse this inhibition or the high levels of TBARS and CPs. On the other hand, levels of GSH were increased by infusions demonstrating the increased antioxidant activity in rural workers' erythrocytes.

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Section: Introductionmentioning

confidence: 99%

Effect of the Cymbopogon citratus Infusion on the Activity of Acetylcholinesterase Enzyme and on the Redox Profile in Farmers’ Erythrocytes

Mori¹,

Horn²,

Oliveira³

et al. 2017

JAS

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“…As previously mentioned, hydrophobic AChE has also been purified to homogeneity from the brains of a number of vertebrate species, including bovine [121], rat [122, 1231, human [124] and chicken [125]. In all these cases the purified brain enzyme occurs as a G4 tetramer.…”

Section: Globular Forms Purification Characterization and Hydrophobimentioning

confidence: 99%

Modes of attachment of acetylcholinesterase to the surface membrane

Silman

Futerman

1987

European Journal of Biochemistry

173

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Acetylcholinesterase (AChE) occurs in multiple molecular forms differing in their quaternary structure and mode of anchoring to the surface membrane. Attachment is achieved by post‐translational modification of the catalytic subunits. Two such mechanisms are described. One involves attachment to catalytic subunit tetramers, via disulfide bridges, of a collagen‐like fibrous tail. This, in turn, interacts, primarily via ionic forces, with a heparin‐like proteoglycan in the extracellular matrix. A second such modification involve the covalent attachment of a single phosphatidylinositol molecule at the carboxyl‐terminus of each catalytic subunit polypeptide; the diacylglycerol moiety of the phospholipid serves to anchor the modified enzyme hydrophobically to the lipid bilayer of the plasma membrane. The detailed molecular structure of these two classes of acetylcholinesterase are discussed, as well as their biosynthesis and mode of anchoring.

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“…Unless otherwise stated, purifications were carried out on a resin containing trimethylammonium m-phenylenediamine as affinity ligand [38] as follows: AChE from bovine and human erythrocyte membranes according to Brodbeck et al [38]; AChE from rat brain, bovine brain, and human brain according to Smensen et al [39,40]; AChE from electric organ of T . marmorata according to Stieger and Brodbeck [41].…”

Section: Antibodiesmentioning

confidence: 99%

The monoclonal antibody 2G8 is carbohydrate‐specific and distinguishes between different forms of vertebrate cholinesterases

Liao

Heider

Sun³

et al. 1991

European Journal of Biochemistry

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The monoclonal antibody (mAb) 2G8 (subclass IgG2,) raised against acetylcholinesterase (AChE, EC 3.1.1.7) from electric organ of Torpedo nacline timilei crossreacted with AChE from Torpedo marmorata, electric eel (Electrophorus electricus), flounder (Platichthys Jlesus) body muscle, rat brain, bovine brain, and human brain, this suggests that the epitope to which mAb 2G8 bound had been highly conserved during evolution. No crossreaction was found with AChE from human and bovine erythrocytes, nor with butyrylcholinesterase (BtChE, EC 3.1.1 3) from human serum. Binding of mAb 2G8 to the globular G z form of AChE from T. marmorata strongly decreased enzyme activity, while no significant inhibition was found with either collagen-tailed, asymmetric forms, or with the enzymes from flounder body muscle or mammalian sources. The possibility that mAb 2G8 bound to anionic sites of AChE could be excluded since neither edrophonium chloride nor decamethonium bromide influenced the binding of 2G8 to the enzymes. Enzyme-linked immunosorbent assay and Western blot showed that heat-denatured, diisopropylfluorophosphate-treated, CNBr-and trypsin-digested AChE from T. marmorata still reacted with mAb 2G8; this indicates that the epitope to which 2G8 bound, at least partially, belonged to a continuous determinant. Treatment of cholinesterases with N-glycosidase F abolished crossreaction with 2G8, showing that an essential part of the epitope consisted of N-linked carbohydrates.

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An Amphiphile‐Dependent Form of Human Brain Caudate Nucleus Acetylcholinesterase: Purification and Properties

Cited by 90 publications

References 35 publications

Effect of the Cymbopogon citratus Infusion on the Activity of Acetylcholinesterase Enzyme and on the Redox Profile in Farmers’ Erythrocytes

Effect of the Cymbopogon citratus Infusion on the Activity of Acetylcholinesterase Enzyme and on the Redox Profile in Farmers’ Erythrocytes

Modes of attachment of acetylcholinesterase to the surface membrane

The monoclonal antibody 2G8 is carbohydrate‐specific and distinguishes between different forms of vertebrate cholinesterases

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