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Query: EC:3.1.1.7 (acetylcholinesterase)
 28,390 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have studied the physicochemical properties of acetylcholinesterase (AChE) during embryonic development of normal and functionally impaired mouse skeletal muscle, focusing on the tailed asymmetric (16S) form of the enzyme. The muscle-specific 16S AChE exists in two different variants. One is associated with extracellular matrix and is high-salt soluble (HSS, also termed hydrophilic AChE), whereas the other form is anchored to cell membranes and is detergent extractable (DE, or hydrophobic AChE). Before innervation during normal embryonic development, both hydrophilic and hydrophobic 16S AChE exist in equal amounts. After muscle innervation, there was an increase (amounting three-fold on E18) in the levels of hydrophilic vs. hydrophobic 16S AChE. This alteration of the relative proportions of the two variants of 16S AChE did not occur in chronically inactive muscles either from the mouse mutant, muscular dysgenesis, or from tetrodotoxin-treated mouse embryos. Taken together with previous reports, the present results suggest that postsynaptic membrane depolarization-induced Ca2+ fluxes are important in modulating not only the synthesis of 16S AChE, but also the relative proportions of both physicochemical variants of this molecular form of AChE.
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PMID:Developmental modulation of physicochemical variants of the tailed asymmetric (16S) acetylcholinesterase by neuromuscular activity and innervation in the mouse embryo. 189 Jul 3

In primary cell cultures of rat superior cervical ganglia (SCG) the tailed asymmetric 16S molecular form of acetylcholinesterase (AChE) possesses hydrophilic (high-salt soluble, HSS) and hydrophobic (detergent extracted, DE) variants. Hydrophobic tailed acetylcholinesterase is associated with membranes through a glycolipid anchor. In the presence of tunicamycin, an antibiotic which inhibits protein glycosylation, the cellular amount of the hydrophobic DE 16S AChE is increased. Exposure of the cells to the calcium ionophore A 23187 leads to a decrease in DE 16S AChE and a correlated increase in hydrophilic HSS 16S AChE. These results suggest the existence of an endogenous processing of tailed AChE, transforming the hydrophobic variant into an hydrophilic one controlled through glycosylation and intracellular calcium.
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PMID:Cell modulation of hydrophobic tailed 16S acetylcholinesterase by intracellular calcium in rat superior cervical ganglion neurons. 209 23

We have determined partial N-terminal sequences of acetylcholinesterase (AChE) catalytic subunits from Torpedo marmorata electric organs and from bovine caudate nucleus. We obtain identical sequences (23 amino acids) for the soluble ('low-salt-soluble' or LSS fraction) and particulate ('detergent-soluble', or DS fraction) amphiphilic dimers (G2 form) and for the asymmetric, collagen-tailed forms ('high-salt-soluble', or HSS fraction, A12 + A8 forms). There are two amino acid differences, at position 3 (Asp/His) and 20 (Ile/Val), with the sequences obtained for T. californica by MacPhee-Quigley et al. [(1985) J. Biol. Chem. 260, 12185-12189] for the soluble G2 form and the lytic G4 form which is derived from asymmetric AChE. The bovine sequence (12 amino acids) presents an identity of 4 amino acids (Glu-Leu-Leu-Val) with that of Torpedo, at positions 5-8 (Torpedo) and 7-10 (bovine). There is also a clear homology with the sequence of human butyrylcholinesterase [(1986) Lockridge et al. J. Biol. Chem., in press] indicating that these enzymes probably derive from a common ancestor.
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PMID:Identical N-terminal peptide sequences of asymmetric forms and of low-salt-soluble and detergent-soluble amphiphilic dimers of Torpedo acetylcholinesterase. Comparison with bovine acetylcholinesterase. 379 44

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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PMID:Calcium influxes and calmodulin modulate the expression and physicochemical properties of acetylcholinesterase molecular forms during development in vivo. 824 86

We prepared myofiber basal lamina sheaths (BLs) using the in vivo experimental procedure of Sanes et al. (J. Cell Biol.78, 176-198, 1978) on frog cutaneus pectoris muscle. On the 15 days post-operatively, acetylcholinesterase (AChE) is still found concentrated in native BLs and purified BLs preparations and both globular and asymmetric molecular forms coexist (Nicolet et al., J. Cell Biol., 107, 762-768, 1986). We describe here at least two distinct AChE pools, according to their differential solubility in non-ionic detergent and high-salt media. One is detergent-extracted (DE) and the other is detergent-insoluble, high-salt extracted (HSS). In the BLs preparation as well as in control motor end-plate rich regions (MEP-r) of muscle, both globular and asymmetric forms of AChE are found as DE and HSS variants. These observations suggest that all AChE forms are present in the extracellular muscle basal lamina and are bound through not only hydrophilic but also hydrophobic bonds, to probably distinct structural domains of the muscle basal lamina.
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PMID:Hydrophilic and hydrophobic attachment of both globular and asymmetric acetylcholinesterase to frog muscle basal lamina sheaths. 2050 Nov 61