Abstract
Tissue-specific expression of acetylcholinesterase (AChE) is correlated with 3’ alternative splicing events which allows for the generation of distinct mRNAs. These encode three types of catalytic subunits corresponding to AChET, AChEH and AChER that are expressed, respectively, in muscle and neurons, hematopoietic cells and during early stages of embryonic development. The H subunit contains a C-terminal signal for addition of a GPI-anchor whereas the T subunit can interact with a collagenic structural subunit (Q) to produce asymmetric forms. The R sequence lacks an essential cysteine residue suggesting that it is not able to form complex oligomers. In the present studies, we have examined the post-translational mechanisms involved in the assembly, stabilization and secretion of the different splice variants of AChE in muscle cells. To this end, we overexpressed cDNAs encoding AChET, AChEH and AChER in the myogenic C2C12 cell line and measured total activity (cell associated and secreted) in differentiated myotubes. Expression of the H subunit, corrected for transfection efficiency, was significantly higher (6-fold) than that of the T subunit. Although expression of the R catalytic subunit was lower than that of T, a greater percentage of R was secreted into the media as non-amphiphilic monomers. Immunofluorescence and PI-PLC experiments indicated that H occurred predominantly as GPI-anchored dimers inserted in the sarcolemma whereas T and R catalytic subunits were either secreted or retained inside the myotubes. Translation of these three transcripts in transfected muscle cells indicates that tissue-specific expression of distinct AChE molecular forms in vivo relies primarily on regulated alternative splicing events.
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© 1998 Springer Science+Business Media New York
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Mankal, F.A., Massoulié, J., Jasmin, B.J., Legay, C. (1998). Assembly, Stability and Secretion of Acetylcholinesterase in Cultured Mouse Muscle Cells. In: Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. (eds) Structure and Function of Cholinesterases and Related Proteins. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1540-5_28
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DOI: https://doi.org/10.1007/978-1-4899-1540-5_28
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4899-1542-9
Online ISBN: 978-1-4899-1540-5
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