Developmental modulation of physicochemical variants of the tailed asymmetric (16S) acetylcholinesterase by neuromuscular activity and innervation in the mouse embryo

Houenou, Lucien J.; Garcı́a, Luis; Verdière‐Sahuqué, Martine; Villageois, Albert; Rieger, François

doi:10.1002/jnr.490290215

Cited by 3 publications

(1 citation statement)

References 37 publications

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“…The result shown in Figure 5 also indicate that amphiphilic asymmetric forms are more abundant in DM than in NM. The balance of amphiphilic/hydrophilic A,, forms appears to shift in favor of the hydrophilic variants during normal mouse embryonic development (Houenou et al, 1991). A relative enrichment in amphiphilic A, , forms should be expected if, as suggested by Skau (1990), the AChE abnormalities in DM constitute an index of a maturation defect.…”

Section: Discussionmentioning

confidence: 91%

Amphiphilic properties of molecular forms of acetylcholinesterase in normal and dystrophic muscle

Cabezas‐Herrera

Campoy

Vidal

1994

J of Neuroscience Research

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Acetylcholinesterase (AChE) molecular forms were studied in normal (NM) and in dystrophic (DM) 129B6F1/J mouse muscle. Successive extractions of the tissue with saline and saline-Triton X-100 buffers yielded two soluble fractions, S1 and S2. Forty percent of the AChE in NM was measured in S1 and 60% in S2, and 65% and 35%, respectively, in extracts from DM. A12, A8, G4, G2, and G1 forms of AChE were found in S1 and S2 from NM and DM. A similar content of asymmetric molecules was noticed between NM and DM. G4 AChE was a minor species in DM, and G1 and G2 AChE were more abundant in DM than in NM. The amphiphilic properties of the several molecules were assessed by Triton X-114 phase-partitioning and hydrophobic chromatography. Thirty and 70% of the enzyme in a mixture of S1 and S2 partitioned in the detergent-rich and in the detergent-poor phases, respectively, whether the extracts were obtained from NM or DM. Asymmetric and G4 AChE predominated in the aqueous phase and G1 and G2 in the detergent phase. Ten and 25% of the enzyme in S1 from NM or DM, respectively, was adsorbed to the phenyl-agarose. Elution of the retained enzyme followed by sedimentation analysis revealed that a certain amount of asymmetric and most of the G1 and G2 forms were associated with the matrix. The content of amphiphilic asymmetric and light globular forms was notably higher in DM than in NM. The results suggest that dystrophic muscle produces a specific pattern of molecular forms of AChE.

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Section: Discussionmentioning

confidence: 91%

Amphiphilic properties of molecular forms of acetylcholinesterase in normal and dystrophic muscle

Cabezas‐Herrera

Campoy

Vidal

1994

J of Neuroscience Research

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Calcium influxes and calmodulin modulate the expression and physicochemical properties of acetylcholinesterase molecular forms during developmentin vivo

Houenou

Sahuqué²,

Villageois³

1993

Cell Mol Neurobiol

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1. Acetylcholinesterase (AcChoE; EC 3.1.1.7) exists in several molecular forms that may be anchored to cell membranes or associated with extracellular matrix. AcChoE bound to lipidic membranes is detergent extractable (DE AcChoE), whereas the enzyme associated with extracellular matrix is high salt soluble (HSS AcChoE). The latter variant is accumulated in synaptic regions by an unknown mechanism. 2. We have suggested previously that depolarization-induced Ca2+ influx is a major factor that modulates AcChoE synthesis in vivo, as well as the conversion of some DE AcChoE to HSS variant. In the present study, we have examined (i) the effects of depolarization-induced skeletal muscle inactivity and ionophore-induced Ca2+ influxes on the expression of AcChoE molecular forms and (ii) the hypothesis that Ca(2+)-dependent calmodulin may be involved in the conversion of at least some forms of DE AcChoE to HSS variant in vivo. 3. Chick embryos were treated in ovo during the early period of nerve-muscle interactions with d-tubocurarine (dTC; a competitive neuromuscular blocking agent) or with decamethonium (dMET; a depolarizing agent). Both dTC and dMET equally and significantly reduced embryonic neuromuscular activity (motility). However, dTC significantly decreased AcChoE overall activity, whereas dMET had virtually no effect on AcChoE expression, compared to controls. 4. Treatment of embryos with the Ca2+ ionophore A23187 significantly increased the total AcChoE activity as well as the DE/HSS ratio of each AcChoE molecular form. However, treatment with N-(6-Aminohexyl)-5-chloro-1-naphthalenesulfonamide (also termed W-7), a calmodulin antagonist, did not alter the total AcChoE activity, but significantly increased the DE/HSS ratio of AcChoE forms. 5. These results support the idea that (i) depolarization and/or Ca2+ influxes, but not muscle contraction, may regulate AcChoE expression in skeletal muscle and (ii) Ca(2+)-dependent calmodulin activation may be involved in the conversion of some DE AcChoE to their HSS variant in vivo.

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The effect of the mode of delivery on the maternal–neonatal erythrocyte membrane acetylcholinesterase activity

Vlachos¹,

Schulpis

Parthimos³

et al. 2008

Clinical Biochemistry

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Developmental modulation of physicochemical variants of the tailed asymmetric (16S) acetylcholinesterase by neuromuscular activity and innervation in the mouse embryo

Cited by 3 publications

References 37 publications

Amphiphilic properties of molecular forms of acetylcholinesterase in normal and dystrophic muscle

Amphiphilic properties of molecular forms of acetylcholinesterase in normal and dystrophic muscle

Calcium influxes and calmodulin modulate the expression and physicochemical properties of acetylcholinesterase molecular forms during developmentin vivo

The effect of the mode of delivery on the maternal–neonatal erythrocyte membrane acetylcholinesterase activity

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