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Originally published In Press as doi:10.1074/jbc.M100631200 on February 8, 2001

J. Biol. Chem., Vol. 276, Issue 19, 16418-16424, May 11, 2001
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Binding of Serum Response Factor to CArG Box Sequences Is Necessary but Not Sufficient to Restrict Gene Expression to Arterial Smooth Muscle Cells*

Mark StrobeckDagger §, Steven Kim§, Janet C. L. ZhangDagger §, Cynthia Clendenin, Kevin L. DuDagger , and Michael S. ParmacekDagger ||

From the Dagger  Department of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104 and the  Department of Medicine, University of Chicago, Chicago, Illinois 60637

Serum response factor (SRF) plays an important role in regulating smooth muscle cell (SMC) development and differentiation. To understand the molecular mechanisms underlying the activity of SRF in SMCs, the two CArG box-containing elements in the arterial SMC-specific SM22alpha promoter, SME-1 and SME-4, were functionally and biochemically characterized. Mutations that abolish binding of SRF to the SM22alpha promoter totally abolish promoter activity in transgenic mice. Moreover, a multimerized copy of either SME-1 or SME-4 subcloned 5' of the minimal SM22alpha promoter (base pairs -90 to +41) is necessary and sufficient to restrict transgene expression to arterial SMCs in transgenic mice. In contrast, a multimerized copy of the c-fos SRE is totally inactive in arterial SMCs and substitution of the c-fos SRE for the CArG motifs within the SM22alpha promoter inactivates the 441-base pair SM22alpha promoter in transgenic mice. Deletion analysis revealed that the SME-4 CArG box alone is insufficient to activate transcription in SMCs and additional 5'-flanking nucleotides are required. Nuclear protein binding assays revealed that SME-4 binds SRF, YY1, and four additional SMC nuclear proteins. Taken together, these data demonstrate that binding of SRF to specific CArG boxes is necessary, but not sufficient, to restrict transgene expression to SMCs in vivo.

* This work was supported in part by National Institutes of Health Grant R0156915 (to M. S. P.).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.

§ Contributed equally to the results of this manuscript.

|| Established Investigator of the American Heart Association. To whom correspondence should be addressed: University of Pennsylvania School of Medicine, 9123 Founders Pavilion, Philadelphia, PA 19104-4283. Tel.: 215-662-3140; Fax: 215-349-8017; E-mail: parmacek@mail.med.upenn.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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