Title
A biotin analog inhibits acetyl-CoA carboxylase activity and adipogenesis
Document Type
Article
Publication Date
5-10-2002
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.
Publication Source (Journal or Book title)
The Journal of biological chemistry
First Page
16347
Last Page
50
Recommended Citation
Levert, K. L., Waldrop, G. L., & Stephens, J. M. (2002). A biotin analog inhibits acetyl-CoA carboxylase activity and adipogenesis. The Journal of biological chemistry, 277 (19), 16347-50. https://doi.org/10.1074/jbc.C200113200