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AMP-activated protein kinase and ATP-citrate lyase are two distinct molecular targets for ETC-1002, a novel small molecule regulator of lipid and carbohydrate metabolism
Open accessAbstract
ETC-1002 (8-hydroxy-2,2,14,14-tetramethylpentadecanedioic acid) is a novel investigational drug being developed for the treatment of dyslipidemia and other cardio-metabolic risk factors. The hypolipidemic, anti-atherosclerotic, anti-obesity, and glucose-lowering properties of ETC-1002, characterized in preclinical disease models, are believed to be due to dual inhibition of sterol and fatty acid synthesis and enhanced mitochondrial long-chain fatty acid β-oxidation. However, the molecular mechanism(s) mediating these activities remained undefined. Studies described here show that ETC-1002 free acid activates AMP-activated protein kinase in a Ca(2+)/calmodulin-dependent kinase β-independent and liver kinase β 1-dependent manner, without detectable changes in adenylate energy charge. Furthermore, ETC-1002 is shown to rapidly form a CoA thioester in liver, which directly inhibits ATP-citrate lyase. These distinct molecular mechanisms are complementary in their beneficial effects on lipid and carbohydrate metabolism in vitro and in vivo. Consistent with these mechanisms, ETC-1002 treatment reduced circulating proatherogenic lipoproteins, hepatic lipids, and body weight in a hamster model of hyperlipidemia, and it reduced body weight and improved glycemic control in a mouse model of diet-induced obesity. ETC-1002 offers promise as a novel therapeutic approach to improve multiple risk factors associated with metabolic syndrome and benefit patients with cardiovascular disease.
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Role of AMP-Activated Protein Kinase in Mechanism of Metformin Action
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Broadfield, L. A., Pane, A. A., Talebi, A., Swinnen, J. V., & Fendt, S.-M. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.04.013 · Cited by 758
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Pinkosky, S. L., Newton, R. S., Day, E. A., Ford, R. J., Lhotak, S., Austin, R. C., Birch, C. M., Smith, B. K., Filippov, S., Groot, P. H. E., et al. (2016) · Nature Communications · doi:10.1038/ncomms13457 · Cited by 498
Self-citationBallantyne, C. M., Laufs, U., Ray, K. K., Leiter, L. A., Bays, H. E., Goldberg, A. C., Stroes, E. S., MacDougall, D., Zhao, X., & Catapano, A. L. (2020) · European Journal of Preventive Cardiology · doi:10.1177/2047487319864671 · Cited by 358
Metadata
- Authors
- Pinkosky, S. L., Filippov, S., Srivastava, R. A. K., Hanselman, J. C., Bradshaw, C. D., Hurley, T. R., Cramer, C. T., Spahr, M. A., Brant, A. F., Houghton, J. L., Baker, C., Naples, M., Adeli, K., & Newton, R. S.
- Venue
- Journal of Lipid Research
- Publisher
- Elsevier BV
- Published
- 2013-01
- Volume
- 54
- Issue
- 1
- Pages
- 134-151
- ISSN
- 0022-2275 (ISSN-L)
- OpenAlex
- W2086222405
- Cited by
- 239
- References
- 18
- FWCI
- 2.90
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: AMP-activated protein kinase and ATP-citrate lyase are two distinct molecular targets for ETC-1002, a novel small molecule regulator of lipid and carbohydrate metabolism. https://app.cochat.ai/papers/10.1194/jlr.m030528
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- Pinkosky, S. L., Filippov, S., Srivastava, R. A. K., Hanselman, J. C., Bradshaw, C. D., Hurley, T. R., Cramer, C. T., Spahr, M. A., Brant, A. F., Houghton, J. L., Baker, C., Naples, M., Adeli, K., & Newton, R. S. (2013). AMP-activated protein kinase and ATP-citrate lyase are two distinct molecular targets for ETC-1002, a novel small molecule regulator of lipid and carbohydrate metabolism. Journal of Lipid Research. https://doi.org/10.1194/jlr.m030528
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
