Neonatal acetylcholinesterase inhibition by fasciculin 2 in rats: A model for the study of central nervous system development?

Bolioli, B.; Blasina, Fernanda; Silveira, Ricardo dos Reis; Dajas, Federico

doi:10.1016/0041-0101(95)00025-h

“…In vivo experiments with intracisternal CNS injection of FAS in neonate rats have shown permanent growth impairment of the animals, supporting the idea that AChE influences CNS development in vivo (Bolioli et al 1995). In agreement with these effects of FAS, neonate rats treated systemically with monoclonal antibodies against AChE were impaired in their growth and in the proper development of the cholinergic system (Rakonczay et al 1993).…”

Section: Introductionmentioning

confidence: 56%

Evidence for a noncholinergic function of acetylcholinesterase during development of chicken retina as shown by fasciculin

Blasina¹,

Faria²,

Gardino³

et al. 2000

Cell and Tissue Research

1

0

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Fasciculin 2 (FAS), an acetylcholinesterase (AChE) peripheral site ligand that inhibits mammalian AChE in the picomolar range and chicken AChE only at micromolar concentrations, was used in chick retinal cell cultures to evaluate the influence of AChE on neuronal development. The effects of other AChE inhibitors that bind the active and/or the peripheral site of the enzyme [paraoxon, eserine, or 1,5-bis(4-allyldimethylammoniumphenyl) pentan-3-one dibromide (BW284c51)] were also studied. Morphological changes of cultured neurons were observed with the drugs used and in the different cell culture systems studied. Cell aggregates size decreased by more than 35% in diameter after 9 days of FAS treatment, mainly due to reduction in the presumptive plexiform area of the aggregates. Eserine showed no effect on the morphology of the aggregates, although it fully inhibited the activity of AChE. In dense stationary cell culture, cluster formation increased after 3 days and 6 days of FAS treatment. However, FAS, at concentrations in which changes of morphological parameters were observed, did not inhibit the AChE activity as measured histochemically. In contrast, paraoxon treatment produced a slight morphological alteration of the cultures, while a strong inhibition of enzyme activity caused by this agent was observed. BW284c51 showed a harmful, probably toxic effect, also causing a slight AChE inhibition. It is suggested that the effect of an anticholinesterase agent on the morphological modifications of cultured neurons is not necessarily associated with the intensity of the AChE inhibition, especially in the case of FAS. Moreover, most of the effects of AChE on culture morphology appear to be independent of the cholinolytic activity of the enzyme. The results obtained demonstrate that FAS is not toxic for the cells and suggest that regions of the AChE molecule related to the enzyme peripheral site are likely to be involved with the nonclassical role of AChE.

show abstract

Evidence for a noncholinergic function of acetylcholinesterase during development of chicken retina as shown by fasciculin

Blasina

¹

,

Faria

²

,

Gardino

³

et al. 2000

View full text Add to dashboard Cite

Fasciculin 2 (FAS), an acetylcholinesterase (AChE) peripheral site ligand that inhibits mammalian AChE in the picomolar range and chicken AChE only at micromolar concentrations, was used in chick retinal cell cultures to evaluate the influence of AChE on neuronal development. The effects of other AChE inhibitors that bind the active and/or the peripheral site of the enzyme [paraoxon, eserine, or 1,5-bis(4-allyldimethylammoniumphenyl) pentan-3-one dibromide (BW284c51)] were also studied. Morphological changes of cultured neurons were observed with the drugs used and in the different cell culture systems studied. Cell aggregates size decreased by more than 35% in diameter after 9 days of FAS treatment, mainly due to reduction in the presumptive plexiform area of the aggregates. Eserine showed no effect on the morphology of the aggregates, although it fully inhibited the activity of AChE. In dense stationary cell culture, cluster formation increased after 3 days and 6 days of FAS treatment. However, FAS, at concentrations in which changes of morphological parameters were observed, did not inhibit the AChE activity as measured histochemically. In contrast, paraoxon treatment produced a slight morphological alteration of the cultures, while a strong inhibition of enzyme activity caused by this agent was observed. BW284c51 showed a harmful, probably toxic effect, also causing a slight AChE inhibition. It is suggested that the effect of an anticholinesterase agent on the morphological modifications of cultured neurons is not necessarily associated with the intensity of the AChE inhibition, especially in the case of FAS. Moreover, most of the effects of AChE on culture morphology appear to be independent of the cholinolytic activity of the enzyme. The results obtained demonstrate that FAS is not toxic for the cells and suggest that regions of the AChE molecule related to the enzyme peripheral site are likely to be involved with the nonclassical role of AChE.

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Synthetic peptides derived from the central loop of fasciculin: structural analysis and evaluation as inhibitors of acetylcholinesterase

Falkenstein

¹

,

Peña

²

1997

Biochimica et Biophysica Acta (BBA) - Protein Structure and Mol

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Neonatal acetylcholinesterase inhibition by fasciculin 2 in rats: A model for the study of central nervous system development?

Cited by 3 publications

References 16 publications

Evidence for a noncholinergic function of acetylcholinesterase during development of chicken retina as shown by fasciculin

Evidence for a noncholinergic function of acetylcholinesterase during development of chicken retina as shown by fasciculin

Evidence for a noncholinergic function of acetylcholinesterase during development of chicken retina as shown by fasciculin

Synthetic peptides derived from the central loop of fasciculin: structural analysis and evaluation as inhibitors of acetylcholinesterase

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