Parallel regulation of acetylcholinesterase and pseudocholinesterase in normal, denervated and dystrophic chicken skeletal muscle

Silman, Israel; Giamberardino, L. Di; Lyles, Joan M.; Couraud, Jean-Yves; Barnard, Eric A.

doi:10.1038/280160a0

Cited by 90 publications

(57 citation statements)

References 22 publications

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“…In adult rats and chickens, they disappear after denervation Bacou et al, 1982;Lai et al, 1986), whereas the total AChE activity decreases in the rat (Berman et al, 1987) but increases severalfold in the chicken Silman et al, 1979). In 1-day-old chick muscle, the asymmetric AChE, in fact, exists predominantly as a hybrid molecule of AChE and butyryicholinesterase (BuChE; EC 3.1.1 .~)catalytic subunits attached by way of disulfides to a common collagen-like tail (Tsim et al, 1988a); the identification of this asymmetric hybrid enzyme could explain the coregulation of AChE and BuChE in the chick muscle in many physiological states Tsim et al, 1988a,b).…”

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confidence: 99%

A Globular, Not Asymmetric, Form of Acetylcholinesterase Is Expressed in Chick Motor Neurons: Down‐Regulation Toward Maturity and After Denervation

Tsim

Choi

Dong

et al. 1997

Journal of Neurochemistry

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Abstract:In vertebrate neuromuscular junctions, the postsynaptic specializations include the accumulation of acetylcholinesterase (AChE) at the synaptic basal lamina and the muscle fiber. Several lines of evidence indicate that the presynaptic motor neuron is able to synthesize and secrete AChE at the neuromuscular junctions. By using anti-AChE catalytic subunit, anti-butyrylcholinesterase (BuChE) catalytic subunit, and anti-AChE collagenous tail monoclonal antibodies, we demonstrated that the motor neurons of chick spinal cord expressed AChE in vivo and the predominant AChE was the globular form of the enzyme. Neither asymmetric AChE nor BuChE was detected in the motor neurons. The molecular mass of AChE catalytic subunit in the motor neuron was~-~1O5 kDa, which was similar to that of the globular enzyme from low-salt extracts of muscle; both of them were~5 kDa smaller than the asymmetric AChE from high-salt extracts of muscle. The level of AChE expression in the motor neurons decreased, as found by immunochemical and enzymatic analysis, during the different stages of the chick's development and after nerve lesion. Thus, the AChE activity at the neuromuscular junctions that is contributed by the presynaptic motor neurons is primarily the globular, not the asymmetric, form of the enzyme, and these contributions decreased toward maturity and after denervation. Key Words: Butyryicholinesterase-Collagen-like tail-Muscle development-Neuromuscular junctions-Postsynaptic specializations.

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A Globular, Not Asymmetric, Form of Acetylcholinesterase Is Expressed in Chick Motor Neurons: Down‐Regulation Toward Maturity and After Denervation

Tsim

Choi

Dong

et al. 1997

Journal of Neurochemistry

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“…Both enzymes are rare ubiquitous proteins that exist in parallel arrays of multiple molecular forms with similar kinetic properties. The molecular forms differ in the number of catalytic subunits (2), in their level of hydrophobicity (3) and mode of glycosylation (4), and in their cellular and subcellular localization (1). In the human brain (5), AcChoEase is the major species, accompanied by minor BtChoEase activities.…”

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confidence: 99%

Isolation and characterization of full-length cDNA clones coding for cholinesterase from fetal human tissues.

Prody¹,

Zevin-Sonkin²,

Gnatt³

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

158

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“…The enzyme exists in multiple molecular forms [l] with similar kinetic properties. The asymmetric and globular forms differ in their cellular localization [l], in number of catalytic subunits [2], in level of hydrophobicity [3] and mode of glycosylation [4]. In blood, amphipathic acetylcholinesterase dimers of globular form are bound to the erythrocyte membrane [5,6].…”

Section: Acetylcholinesterasementioning

confidence: 99%

Purification and partial amino acid sequence analysis of human erythrocyte acetylcholinesterase

Chhajlani¹,

Derr²,

Earles³

et al. 1989

FEBS Letters

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A single step immunoaffinity purification procedure for human erythrocyte acetylcholinesterase is described which permitted the isolation of milligram quantities of enzyme from 10 U of erythrocytes, with 113 000-fold purification and a yield of about 22%. In SDS-PAGE analysis, the enzyme corresponds to a disulfide linked dimer of 140 kDa which is converted to a 70 kDa monomer upon disultide reduction. The tryptic peptides generated from purified enzyme were separated by reverse-phase HPLC. Five of these peptides were analysed to determine the amino acid sequences. The obtained sequences showed no homology to the already known amino acid sequences for human serum and brain butyrylcholinesterase and Torpedo californica acetylcholinesterase.

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Parallel regulation of acetylcholinesterase and pseudocholinesterase in normal, denervated and dystrophic chicken skeletal muscle

Cited by 90 publications

References 22 publications

A Globular, Not Asymmetric, Form of Acetylcholinesterase Is Expressed in Chick Motor Neurons: Down‐Regulation Toward Maturity and After Denervation

A Globular, Not Asymmetric, Form of Acetylcholinesterase Is Expressed in Chick Motor Neurons: Down‐Regulation Toward Maturity and After Denervation

Isolation and characterization of full-length cDNA clones coding for cholinesterase from fetal human tissues.

Purification and partial amino acid sequence analysis of human erythrocyte acetylcholinesterase

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