Interaction of acetylcholinesterase with the G4 domain of the laminin alpha1-chain

The Biochemical Journal
Glynis JohnsonSamuel W Moore

Abstract

Although the primary function of AChE (acetylcholinesterase) is the synaptic hydrolysis of acetylcholine, it appears that the protein is also able to promote various non-cholinergic activities, including cell adhesion, neurite outgrowth and amyloidosis. We have observed previously that AChE is able to bind to mouse laminin-111 in vitro by an electrostatic mechanism. We have also observed that certain mAbs (monoclonal antibodies) recognizing AChE's PAS (peripheral anionic site) inhibit both laminin binding and cell adhesion in neuroblastoma cells. Here, we investigated the interaction sites of the two molecules, using docking, synthetic peptides, ELISAs and conformational interaction site mapping. Mouse AChE was observed on docking to bind to a discontinuous, largely basic, structure, Val(2718)-Arg-Lys-Arg-Leu(2722), Tyr(2738)-Tyr(2739), Tyr(2789)-Ile-Lys-Arg-Lys(2793) and Val(2817)-Glu-Arg-Lys(2820), on the mouse laminin alpha1 G4 domain. ELISAs using synthetic peptides confirmed the involvement of the AG-73 site (2719-2729). This site overlaps extensively with laminin's heparin-binding site, and AChE was observed to compete with heparan sulfate for laminin binding. Docking showed the major component of the interaction site on ...Continue Reading

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Citations

Feb 6, 2014·Journal of Molecular Neuroscience : MN·Yves Bourne, Pascale Marchot
Oct 13, 2009·Chemico-biological Interactions·Anna HrabovskaJaromir Myslivecek
Jun 7, 2018·Journal of Enzyme Inhibition and Medicinal Chemistry·Carlos RocaNuria E Campillo
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Sep 13, 2008·The FEBS Journal·Glynis JohnsonSamuel W Moore
Nov 11, 2009·Acta Biochimica Et Biophysica Sinica·Xiaowen GongXuejun Zhang

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