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Originally published In Press as doi:10.1074/jbc.M206498200 on July 24, 2002

J. Biol. Chem., Vol. 277, Issue 39, 36129-36136, September 27, 2002
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A Cyclic AMP-dependent Pathway Regulates the Expression of Acetylcholinesterase during Myogenic Differentiation of C2C12 Cells*

Nina L. SiowDagger , Roy C. Y. ChoiDagger , Anthony W. M. ChengDagger , Joy X. S. JiangDagger , David C. C. Wan§, Shang Q. ZhuDagger , and Karl W. K. TsimDagger ||

From the Dagger  Department of Biology and Molecular Neuroscience Center, The Hong Kong University of Science and Technology, Clear Water Bay Road, Hong Kong, China and the § Department of Biochemistry, The Chinese University of Hong Kong, Shatin, Hong Kong, China

The expression of acetylcholinesterase (AChE) is markedly increased during myogenic differentiation of C2C12 myoblasts to myotubes; the expression is mediated by intrinsic factor(s) during muscle differentiation. In order to analyze the molecular mechanisms regulating AChE expression during myogenic differentiation, a ~2.2-kb human AChE promoter tagged with a luciferase reporter gene, namely pAChE-Luc, was stably transfected into C2C12 cells. The profile of promoter-driven luciferase activity during myogenic differentiation of C2C12 myotubes was found to be similar to that of endogenous expression of AChE catalytic subunit. The increase of AChE expression was reciprocally regulated by a cAMP-dependent signaling pathway. The level of intracellular cAMP, the activity of cAMP-dependent protein kinase, the phosphorylation of cAMP-responsive element binding protein and the activity of cAMP- responsive element (CRE) were down-regulated during the myotube formation. Mutating the CRE site of human AChE promoter altered the original myogenic profile of the promoter activity and its suppressive response to cAMP. In addition, the suppressive effect of the CRE site is dependent on its location on the promoter. Therefore, our results suggest that a cAMP-dependent signaling pathway serves as a suppressive element in regulating the expression of AChE during early myogenesis.

* This work was supported by Research Grants Council of Hong Kong Grants HKUST 6112/00M and 2/99C (to K. W. K. T.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

A visiting professor, supported by a Chinese Academy of Sciences-University of Science and Technology Joint Research Grant, from the Shanghai Institute of Biochemistry, Chinese Academy of Sciences.

|| To whom correspondence should be addressed: Dept. of Biology, The Hong Kong University of Science and Technology, Clear Water Bay Road, Kowloon, Hong Kong (SAR), China. Tel.: 852-2358-7332; Fax: 852-2358-1559; E-mail: BOTSIM@UST.HK.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


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