Subunit Assembly and Glycosylation of Mammalian Brain Acetylcholinsterase

Brodbeck, Urs; Liao, Jian

doi:10.1007/978-1-4615-3046-6_4

Multidisciplinary Approaches to Cholinesterase Functions 1992

DOI: 10.1007/978-1-4615-3046-6_4

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Subunit Assembly and Glycosylation of Mammalian Brain Acetylcholinsterase

Urs Brodbeck

Jian Liao

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Cited by 3 publications

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The membrane form of acetylcholinesterase from rat brain contains a 20 kDa hydrophobic anchor

1994

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Rat brain acetylcholinesterase (AChE, EC 3.1.1.7) consists of about 80% amphiphilic detergent-soluble (DS-) AChE and 20% hydrophilic salt-soluble (SS-) AChE. DS-AChE contains about 65% tetrameric, 20% dimeric and 10% monomeric, SS-AChE about 40% tetrameric and 60% monomeric forms. N-terminal sequencing of DS- and SS-AChE gave identical N-termini corresponding to the published cDNA sequence of the mature enzyme. The band pattern on SDS-gels is similar to that of AChE from human and bovine brain. SDS-PAGE of hydrophobically labeled DS-AChE revealed the presence of a disulfide bonded hydrophobic membrane anchor of about 20 kDa. Monoclonal antibodies (mAbs) recognizing the anchor-containing subunits of mammalian brain DS-AChE, crossreacted with rat brain DS-AChE but not with SS-AChE. DS- and SS-AChE also reacted with antibodies raised against a peptide comprising the last 10 amino acids of the sequence of bovine brain AChE. Our results led us to conclude that both DS- and SS-AChE from rat brain contain T-type catalytic subunits, and DS-AChE in addition a P-type hydrophobic anchor similar to other mammalian brain DS-AChE.

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The membrane form of acetylcholinesterase from rat brain contains a 20 kDa hydrophobic anchor

1994

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Overexpressed Monomeric Human Acetylcholinesterase Induces Subtle Ultrastructural Modifications in Developing Neuromuscular Junctions of Xenopus laevis Embryos

Seidman

Aziz-Aloya

Timberg

et al. 1994

Journal of Neurochemistry

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Formation of a functional neuromuscular junction (NMJ) involves the biosynthesis and transport of numerous muscle‐specific proteins, among them the acetylcholine‐hydrolyzing enzyme acetylcholinesterase (AChE). To study the mechanisms underlying this process, we have expressed DMA encoding human AChE downstream of the cytomegalovirus promoter in oocytes and developing embryos of Xenopus laevis. Recombinant human AChE (rHAChE) produced in Xenopus was biochemically and immunochemically indistinguishable from native human AChE but clearly distinguished from the endogenous frog enzyme. In microinjected embryos, high levels of catalytically active rHAChE induced a transient state of over‐expression that persisted for at least 4 days postfertilization. rHAChE appeared exclusively as nonassembled monomers in embryos at times when endogenous Xenopus AChE displayed complex oligomeric assembly. Nonetheless, cell‐associated rHAChE accumulated in myotomes of 2‐and 3‐day‐old embryos within the same sub‐cellular compartments as native Xenopus AChE. NMJs from 3‐day‐old DNA‐injected embryos displayed fourfold or greater overexpression of AChE, a 30% increase in postsynaptic membrane length, and increased folding of the postsynaptic membrane. These findings indicate that an evolutionarily conserved property directs the intracellular trafficking and synaptic targeting of AChE in muscle and support a role for AChE in vertebrate synaptogenesis.

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A Simple Method for Isolation of a Soluble Acetylcholinesterase from Rat Brain

Jeliazkova

Minkov

1999

Biotechnology & Biotechnological Equipment

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A soluble impure acetylcholinesterase (AChE), (EC 3.1.1. 7) was isolated from rat brain. The enzyme showed tendency to form aggregates in a medium of low ionic strength that leaded to a decrease of the acetylcholinesterase activity. After an increase of the protein concentration of the obtained soluble enzyme, was observed a decrease or absolute loss of the activity which regenerated after diluting with water. Aforeover detachment of the enzyme from the membrane (.<;o/ubilization) leaded up to raising of the total AChE activity as well as the activity of the residual membrane bound AChE. Possible reason might be the transition of the enzyme to more active form with lower degree of aggregation. The soluble AChE was further purified by ion exchange chromatography (FPLC), but the obtained enzyme was not stable enough and rapidly lost its activity in a high ionic strength environment.

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Subunit Assembly and Glycosylation of Mammalian Brain Acetylcholinsterase

Cited by 3 publications

References 26 publications

The membrane form of acetylcholinesterase from rat brain contains a 20 kDa hydrophobic anchor

The membrane form of acetylcholinesterase from rat brain contains a 20 kDa hydrophobic anchor

Overexpressed Monomeric Human Acetylcholinesterase Induces Subtle Ultrastructural Modifications in Developing Neuromuscular Junctions of Xenopus laevis Embryos

A Simple Method for Isolation of a Soluble Acetylcholinesterase from Rat Brain

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