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J. Biol. Chem., Vol. 280, Issue 9, 7694-7701, March 4, 2005

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B-Myb Represses Elastin Gene Expression in Aortic Smooth Muscle Cells^*

Claudia S. Hofmann, Xiaobo Wang, Christopher P. Sullivan, Paul Toselli, Phillip J. Stone, Sean E. McLean, Robert P. Mecham¶, Barbara M. Schreiber, and Gail E. Sonenshein||

From the Department of Biochemistry, Boston University School of Medicine, Boston, Massachusetts 02118 and the Departments of Surgery and ^¶Cell Biology, Washington University School of Medicine, St. Louis, Missouri 63110

B-Myb represses collagen gene transcription in vascular smooth muscle cells (SMCs) in vitro and in vivo. Here we sought to determine whether elastin is similarly repressed by B-Myb. Levels of tropoelastin mRNA and protein were lower in aortas and isolated SMCs of adult transgenic mice expressing the human B-myb gene, driven by the basal cytomegalovirus promoter, compared with age-matched wild type (WT) animals. However, the vessel wall architecture and levels of insoluble elastin revealed no differences. Since elastin deposition occurs early in development, microarray analysis was performed using nontransgenic mice. Aortic levels of tropoelastin mRNA were low during embryonal growth and increased substantially in neonates, whereas B-myb levels varied inversely. Tropoelastin mRNA expression in aortas of 6-day-old neonatal transgenic and WT animals was comparable. Recently, we demonstrated that cyclin A-Cdk2 prevents B-Myb-mediated repression of collagen promoter activity. Cyclin A2 levels were higher in neonatal versus adult WT or transgenic mouse aortas. Ectopic cyclin A expression reversed the ability of B-Myb to repress elastin gene promoter activity in adult SMCs. These results demonstrate for the first time that B-Myb represses SMC elastin gene expression and that cyclin A plays a role in the developmental regulation of elastin gene expression in the aorta. Furthermore, the findings provide additional insight into the mechanism of B-myb-mediated resistance to femoral artery injury.

Received for publication, November 4, 2004 , and in revised form, December 8, 2004.

^* This work was supported by National Institutes of Health Grant PO1 HL13262 (to B. M. S. and G. E. S.) and American Heart Association Grant 0455846T (to B. M. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^|| To whom correspondence should be addressed: Dept. of Biochemistry, Boston University School of Medicine, 715 Albany St., Boston, MA 02118. Tel.: 617-638-4120; E-mail: gsonensh{at}bu.edu.

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