Heparin is capable of solubilizing a subset of collagen-tailed (A) acetylcholinesterase (AChE) molecules from skeletal muscle fibers, but cannot detach AChE from the synaptic basal lamina (Rossi, S. G., and Rotundo, R. L.(1993) J. Biol. Chem. 268, 19152-19159). In the present study, we used tissue-cultured quail myotubes to show that, like adult fibers, neither heparin- nor high salt-containing buffers detached AChE molecules from cell-surface clusters. Prelabeling clustered AChE molecules with anti-AChE monoclonal antibody 1A2 followed by incubation in heparin-containing medium showed that there was no reduction in the number or size of pre-existing AChE clusters. In contrast, incubation of myotubes with culture medium containing heparin for up to 4 days reversibly blocked the accumulation of new cell-surface AChE molecules without affecting the rate of AChE synthesis or assembly. Newly synthesized A AChE becomes tightly attached to the extracellular matrix following externalization. However, in the presence of heparin, blocking the initial interactions between A AChE and the extracellular matrix results in release of AChE into the medium with a t of 3 h. Together, these results suggest that once A AChE is localized on the cell surface, initially attached via electrostatic interactions, additional factors or events are responsible for its selective and more permanent retention on the basal lamina.

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