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The Journal of Neuroscience, October 1, 1999, 19(19):8252-8259

Stability and Secretion of Acetylcholinesterase Forms in Skeletal Muscle Cells

Claire Legay¹, Fawzi A. Mankal², Jean Massoulié¹, and Bernard J. Jasmin²

¹ Laboratoire de Neurobiologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique UMR 8544, Ecole Normale Supérieure, 75005 Paris, France, and ² Department of Cellular and Molecular Medicine, Faculty of Medicine, University of Ottawa, Ottawa, Ontario, Canada K1H 8M5

Muscle cells express a distinct splice variant of acetylcholinesterase (AChE_T), but the specific mechanisms governing this restricted expression remain unclear. In these cells, a fraction of AChE subunits is associated with a triple helical collagen, ColQ, each strand of which can recruit a tetramer of AChE_T. In the present study, we examined the expression of the various splice variants of AChE by transfection in the mouse C2C12 myogenic cells in vitro, as well as in vivo by injecting plasmid DNA directly into tibialis anterior muscles of mice and rats. Surprisingly, we found that transfection with an ACHE_H cDNA, generating a glycophosphatidylinositol-anchored enzyme species, produced much more activity than transfection with AChE_T cDNA in both C2C12 cells and in vivo. This indicates that the exclusive expression of AChE_T in mature muscle is governed by specific splicing. Interaction of AChE_T subunits with the complete collagen tail ColQ increased enzyme activity in cultured cells, as well as in muscle fibers in vivo. Truncated ColQ subunits, presenting more or less extensive C-terminal deletions, also increased AChE activity and secretion in C2C12 cells, although the triple helix could not form in the case of the larger deletion. This suggests that heteromeric associations are stabilized compared with isolated AChE_T subunits. Coinjections of AChE_T and ColQ resulted in the production and secretion of asymmetric forms, indicating that assembly, processing, and externalization of these molecules can occur outside the junctional region of muscle fibers and hence does not require the specialized junctional Golgi apparatus.

Key words: acetylcholinesterase; collagen tail; C2C12 muscle cells; skeletal muscle; alternative splicing; synaptic proteins; neuromuscular junctions

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Copyright © 1999 Society for Neuroscience  0270-6474/99/19198252-08$05.00/0

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