Acetylcholinesterase molecular forms from rat and human erythrocyte membrane

Biagionia, S.; Scarsella, G.; Settimi, Laura; Traina, M.E.

doi:10.1007/bf00229602

Cited by 10 publications

(1 citation statement)

References 28 publications

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“…On the other hand, its high level in several tumor cell types suggested a possible role in cell proliferation or invasive migration (Noda et al, 1998). Furthermore, a noncholinergic role for AChE was also suggested by its presence in red blood cells (Ott et al, 1975; Biagioni et al, 1982). Finally, the association of AChE with cell membrane and its expression in the migrating neural crest cells (Cochard and Coltey, 1983) have also suggested a possible involvement of this molecule in cell interactions.…”

Section: Discussionmentioning

confidence: 98%

Alternative acetylcholinesterase molecular forms exhibit similar ability to induce neurite outgrowth

Jaco

Augusti-Tocco

Biagioni

2002

J of Neuroscience Research

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Several groups have reported that acetylcholinesterase (AChE), through a mechanism not involving its catalytic activity, may have a role in fiber elongation. These observations were performed on experimental systems in which acetylcholine synthesis was active. Because neurite outgrowth can be modulated by neurotransmitters, we used the N18TG2 neuroblastoma line, which is defective for neurotransmitter production, to evaluate whether AChE may modulate neurite sprouting in nonenzymatic ways. To avoid the possibility that differences between transfected and mock-transfected clones may be due to the selection procedure, N18TG2 cells were previously subcloned, and the FB5 subclone was used for transfections. We performed transfections of FB5 cells with three distinct constructs encoding for the glycosylphosphoinositol-anchored AChE form, the tetrameric AChE form, and a soluble monomeric AChE form truncated in its C-terminus. A morphometric analysis of retinoic acid-differentiated clones was also undertaken. The results revealed that higher AChE expression following transfection brings about a greater ability of the clones to grow fibers with respect to nontransfected or mock-transfected cells irrespective of the used construct. Having observed no differences between the morphology of the transfected clones, we tested the possibility that the culture substrate can affect the capability of the clones to extend fibers. Also in this case we revealed no differences between the clones cultured on uncoated or collagen-pretreated dishes. These data indicate that alternative AChE molecular forms that differ in their C-teminal region exhibit similar ability to induce fiber outgrowth and suggest that the protein region responsible for this role is located in the invariant portion of the AChE molecule.

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Section: Discussionmentioning

confidence: 98%

Alternative acetylcholinesterase molecular forms exhibit similar ability to induce neurite outgrowth

Jaco

Augusti-Tocco

Biagioni

2002

J of Neuroscience Research

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Some High-Molecular-Weight Oligomeric Proteins and Enzymes of Reticulocytes and Erythrocytes

Harris¹

1990

Blood Cell Biochemistry

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In vitro influences of alcohols on mouse synaptosomes, and structure-activity relationships

1995

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Little information is available on the structure-central nervous system membrane toxicity relationship of alcohols. The purpose of the present study was to study in vitro influence of alcohols (n = 20) on the activity of the toxic indicator Na+/K(+)-adenosine triphosphatase (Na+/K(+)-ATPase) and acetylcholinesterase (AchE), and membrane fluidity in mouse brain synaptosomes, in terms of the structure-activity relationship. The potency of inhibition for the enzymes (IC50) and the potency of increasing membrane fluidity (IC12.5) were determined experimentally, and n-octanol/water partition coefficient (P) and the steric constant Taft Es are cited from the literature. Regression analysis revealed that log 1/IC50 for Na+/K(+)-ATPase is a function of log P and Taft Es. The situation was true for AchE activity. The results indicate that the hydrophobicity expressed as log P and the steric effect of the alcohols play an important role in inhibiting both enzyme activities. A linear relationship between log 1/IC12.5 for membrane fluidity and log P is shown, indicating a significant effect of the alcohols on membrane fluidity. Based on these results, it is suggested that the alcohols inhibit the Na+/K(+)-ATPase and AchE activity through a direct action on the enzymes and/or through changing the membrane fluidity.

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Acetylcholinesterase molecular forms from rat and human erythrocyte membrane

Cited by 10 publications

References 28 publications

Alternative acetylcholinesterase molecular forms exhibit similar ability to induce neurite outgrowth

Alternative acetylcholinesterase molecular forms exhibit similar ability to induce neurite outgrowth

Some High-Molecular-Weight Oligomeric Proteins and Enzymes of Reticulocytes and Erythrocytes

In vitro influences of alcohols on mouse synaptosomes, and structure-activity relationships

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