FFAR1 binds rosiglitazone

Stable Identifier
Reaction [binding]
Homo sapiens
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Free fatty acid receptor 1 (FFAR1, aka GR40) is a G-protein coupled receptor that plays an important role in glucose homeostasis. Fatty acid binding to FFAR1 increases glucose-stimulated insulin secretion. FFA1 is found in high concentrations in the pancreas and the brain.

Both preclinical and clinical studies have demonstrated that activation of FFAR1 improves glycaemic control by stimulating glucose-dependent insulin secretion. Rosiglitazone is an anti-diabetic drug of the thiazolidinedione class. Like other thiazolidinediones, rosiglitazone acts via activation of peroxisome proliferator-activated receptors (PPARs), specifically PPARĪ³. FFAR1 has also been shown to mediate responses to antidiabetic drugs of the thiazolidinedione class (Kotarsky et al. 2003).

Attempts to develop new FFAR1 agonists have so far been unsuccessful (Governa et al. 2021). Fasiglifam (TAK-875) was a novel antidiabetic drug (Yabuki et al. 2013) but phase 3 clinical trials were terminated due to potential liver toxicity (Otieno et al. 2018).
Literature References
PubMed ID Title Journal Year
24130766 A novel antidiabetic drug, fasiglifam/TAK-875, acts as an ago-allosteric modulator of FFAR1

Maeda, R, Mori, M, Takeuchi, K, Matsuda-Nagasumi, K, Habata, Y, Ito, R, Komatsu, H, Sakuma, K, Tsujihata, Y, Miyawaki, K, Yabuki, C, Kikuchi, N

PLoS One 2013
12565875 A human cell surface receptor activated by free fatty acids and thiazolidinedione drugs

Olde, B, Flodgren, E, Owman, C, Kotarsky, K, Nilsson, NE

Biochem Biophys Res Commun 2003
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