A glia-derived acetylcholine-binding protein that modulates synaptic transmission

A.B. Smit, N.I. Syed, D. Schaap, J. van Minnen, J. Klumperman, K.S. Kits, J.C. Lodder, R.C. van der Schors, R. van Elk, B. Sorgedrager, K. Brejc, T.K. Sixma, W.P.M. Geraerts

Research output: Contribution to JournalArticleAcademicpeer-review


There is accumulating evidence that glial cells actively modulate neuronal synaptic transmission. We identified a glia-derived soluble acetylcholine-binding protein (AChBP), which is a naturally occurring analogue of the ligand-binding domains of the nicotinic acetylcholine receptors (nAChRs). Like the nAChRs, it assembles into a homopentamer with ligand-binding characteristics that are typical for a nicotinic receptor; unlike the nAChRs, however, it lacks the domains to form a transmembrane ion channel. Presynaptic release of acetylcholine induces the secretion of AChBP through the glial secretory pathway. We describe a molecular and cellular mechanism by which glial cells release AChBP in the synaptic cleft, and propose a model for how they actively regulate cholinergic transmission between neurons in the central nervous system.
Original languageEnglish
Pages (from-to)261-268
Number of pages8
Issue number6835
Publication statusPublished - 2001


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