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Originally published In Press as doi:10.1074/jbc.C200113200 on March 20, 2002

J. Biol. Chem., Vol. 277, Issue 19, 16347-16350, May 10, 2002
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ACCELERATED PUBLICATION
A Biotin Analog Inhibits Acetyl-CoA Carboxylase Activity and Adipogenesis*

Keith L. Levert, Grover L. Waldrop, and Jacqueline M. StephensDagger

From the Division of Biochemistry and Molecular Biology, Louisiana State University, Baton Rouge, Louisiana 70803

Acetyl-CoA carboxylase catalyzes the first committed step in the synthesis of long chain fatty acids. In this study, we observed that treatment of 3T3-L1 cells with biotin chloroacetylated at the 1' nitrogen reduced the enzymatic activity of cytosolic acetyl-CoA carboxylase and concomitantly inhibited the differentiation of 3T3-L1 cells in a dose-dependent manner. Treatment with chloroacetylated biotin blocked the induction of PPARgamma , STAT1, and STAT5A expression that normally occurs with adipogenesis. Moreover, addition of chloroacetylated biotin inhibited lipid accumulation, as judged by Oil Red O staining. Our results support recent studies that indicate that acetyl-CoA carboxylase may be a suitable target for an anti-obesity therapeutic.

* This work was supported in part by National Institutes of Health Grants R01DK5268-02 (to J. M. S.) and GM51261 (to G. L. W.).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.

Dagger To whom correspondence should be addressed: Dept. of Biological Sciences, Rm. 202 Life Sciences Bldg., Louisiana State University, Baton Rouge, LA 70803. Tel.: 225-578-1749; Fax: 225-578-2597; E-mail: jsteph1@lsu.edu.

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


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Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.