The synaptic form of acetylcholinesterase binds to cell-surface heparan sulfate proteoglycans.

We have previously communicated that heparan sulfate and heparin released 16S acetylcholinesterase (AChE) from cholinergic synapses. These experiments suggest that heparan-like molecules are involved in the anchorage of AChE to the neuromuscular junction. In order to prove the in vivo interaction between the 16S AChE and heparan sulfate residues, the binding of exogenously added 16S enzyme to intact cells rich in cell-surface heparan sulfate proteoglycans was examined; 16S AChE form was shown to bind to intact endothelial cells in a specific, time-dependent, saturable fashion. A single class of binding sites was involved and at saturation around 2.52 X 10(11) molecules of 16S AChE/cm2 were bound. Fifty percent of the binding of the 16S AChE was blocked by heparan sulfate, heparin, or previous treatment of the cell with heparitinase. The binding was reversed by exogenous heparin, but not by chondroitin sulfate or hyaluronic acid. Our results demonstrate that the synaptic form of AChE binds to heparan sulfate proteoglycans on the surface of the cell.