A biotin analog inhibits acetyl-CoA carboxylase activity and adipogenesis.

The Journal of Biological Chemistry
Keith L LevertJacqueline M Stephens

Abstract

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.

References

Oct 27, 1999·Proceedings of the National Academy of Sciences of the United States of America·E M KhalilP A Cole
Mar 9, 2002·Biochemical and Biophysical Research Communications·Keith L Levert, Grover L Waldrop

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Citations

Jul 6, 2011·Journal of Medicinal Chemistry·Hanley N Abramson
Jan 11, 2013·Biological & Pharmaceutical Bulletin·Junichi IidaKiyomi Ito
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