Molecular form of human lymphocyte membrane-bound acetylcholinesterase

Bartha, E.; Rakonczay, Zoltán; Kása, P.; Hollán, Susan R.; Gyévai, A

doi:10.1016/0024-3205(87)90705-3

Cited by 16 publications

(8 citation statements)

References 24 publications

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“…According to the literature, human peripheral lymphocytes exhibit only the 6.5 S dimeric form (Bartha et al, 1987), whereas homogenates of rat thymuses contain 4 and 10 S forms (Israel and Skau, 1986). With regard to the murine thymus, different results have been reported by Israel and Skau (1986) (4 S) and by Bulloch and Lucito (1988) (4 and 10 S).…”

Section: Ache Molecular Formsmentioning

confidence: 99%

Acetylcholinesterase distribution in subpopulations of murine thymocyte

Rossi

Vicini

Scarsella

et al. 1991

J of Neuroscience Research

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The presence of acetylcholinesterase has been detected in the thymus of several species both biochemically and histochemically. In this study we have investigated the molecular forms and the level of this enzyme in separate compartments of the murine thymus and in different thymocyte subpopulations. Similar levels of acetylcholinesterase activity are present both in thymocytes and in the stromal component. Sucrose density gradient analysis revealed the presence of a single molecular form of about 5 S, presumably a dimeric form. Moreover the results demonstrate a preferential association of AChE with mature thymocyte subsets (Peanut Agglutinin negative and Corticoresistant). This finding correlates with the preferential sensitivity of these cells to cholinergic drugs and supports the hypothesis that acetylcholinesterase modulates the cholinergic effects on thymocytes.

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Section: Ache Molecular Formsmentioning

confidence: 99%

Acetylcholinesterase distribution in subpopulations of murine thymocyte

Rossi

Vicini

Scarsella

et al. 1991

J of Neuroscience Research

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“…Incubation of blood from paretic cows with the Ca-Mg solution approximately doubled the level of free AChE antibodies in serum, since prior to incubation 5 mg/ml IgG was required for changing the Arrhenius plot, and after incubation only 2.5 mg/ml. This should depend on release of antibodies from AChE on blood corpuscles as erythrocytes and lymphocytes (BARTHA et al, 1987). However, that does not fully account for the increase in free AChE antibodies following one injection of Ca-salts and MgC12.…”

Section: Discussionmentioning

confidence: 99%

IgG from Cows with Parturient Paresis Changes the Thermodynamic Behaviour of Bovine Erythrocyte Acetylcholinesterase

Axelsson

Yong

Karlsson

1990

Journal of Veterinary Medicine, Series B

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Summary Parturient paresis affects about 10% of all cows. The most common treatment is injection of various Ca‐salts and MgCl2 and about 80% recover after repeated injections. The effect of IgG on the Arrhenius plot of bovine erythrocyte AChE was studied. The plot was normal, i. e. biphasic (a broken line) in the presence of IgG from healthy cows. The highest concentration tested was 10 mg/ml. Before one injection of the Ca‐Mg solution 5 mg/ml IgG from sera of paretic cows (n=10) changed the Arrhenius plots to monophasic (linear). Thus, paretic cows have antibodies against AChE. After injection the change to linear plots was observed already with 1 mg/ml IgG. Apparently, the level of antibodies in serum affecting AChE increased about 5‐fold. This is considered to be due to dissociation of bound antibodies from various AChEs. All cows recovered after one injection and release of AChE antibodies might be important for the recovery. Incubation of blood from paretic cows (n = 3) with Ca‐salts and MgCl2 increased the amount of free AChE‐antibodies about twofold; the Arrhenius plots became linear at 2.5 mg/ml IgG compared with 5 mg/ml before the incubation. This should be due to release from AChEs on blood corpuscles as erythrocytes and lymphocytes. But the increase of antibodies after incubation of blood does not account for the whole increase following the treatment of paretic cows. AChE antibodies are probably also dissociated from other sites, such as neuromuscular junctions.

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“…In order to obtain information on the forces holding the subunits together, several groups have, in the past, investigated the conditions under which oligomeric forms of AChE could be monomerized. The -conversion of the glycosyl-phosphatidylinositol (G-PI)-anchored G2 form of AChE into enzymically active monomers was achieved with AChE from Torpedo californica (Lee et al, 1982), with AChE from human erythrocytes (Ott et al, 1983) and with AChE from human lymphocytes (Bartha et al, 1987). In the case of the G-PI-anchored G2 form of AChE, the mere reduction of the inter-subunit disulphide bond -was sufficient -to render the enzyme -monomeric, indicating that there are no additional forces holding the subunits together (Ott et al, 1983).…”

Section: Discussionmentioning

confidence: 99%

Monomerization of tetrameric bovine caudate nucleus acetylcholinesterase. Implications for hydrophobic assembly and membrane anchor attachment site

Heider

Brodbeck

1992

Biochemical Journal

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Tetrameric detergent-soluble bovine caudate nucleus acetylcholinesterase (AChE) was reduced and alkylated under conditions in which at least 95% of initial activity is retained. This treatment alone did not result in monomerization of AChE, nor did it create a hydrophilic enzyme. However, in the presence of SDS the enzyme became monomerized. Incubation of AChE with trypsin in the presence of the reversible inhibitor edrophonium rendered the enzyme hydrophilic and led to catalytically active monomers being produced. SDS/PAGE of this preparation in non-reducing conditions revealed only a small decrease in the subunit molecular mass. N-Terminal sequencing of the enzyme, before and after trypsin treatment, yielded identical N-termini showing that the enzyme was monomerized subsequent to C-terminal tryptic cleavage. From our results, we conclude that the most C-terminal cysteine residue is involved in inter-subunit disulphide bonding as well as in the attachment of AChE to the membrane anchor. Furthermore, the C-terminal region in the primary structure provides an area for hydrophobic contacts between the different subunits and also between the subunits and the membrane anchor.

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Molecular form of human lymphocyte membrane-bound acetylcholinesterase

Cited by 16 publications

References 24 publications

Acetylcholinesterase distribution in subpopulations of murine thymocyte

Acetylcholinesterase distribution in subpopulations of murine thymocyte

IgG from Cows with Parturient Paresis Changes the Thermodynamic Behaviour of Bovine Erythrocyte Acetylcholinesterase

Monomerization of tetrameric bovine caudate nucleus acetylcholinesterase. Implications for hydrophobic assembly and membrane anchor attachment site

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