Bongkrekic acid as a selective activator of the peroxisome proliferator-activated receptor y (PPARy) isoform

Hiroyuki Okazaki, Shuso Takeda, Eriko Ikeda, Yoshifumi Fukunishi, Hiroyuki Ishii, Aya Taniguchi, Miki Tokuyasu, Taichi Himeno, Kazuhiro Kakizoe, Kenji Matsumoto, Mitsuru Shindo, Hironori Aramaki

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)


Bongkrekic acid (BKA), an antibiotic isolated from Pseudomonas cocovenans, is an inhibitory molecule of adenine nucleotide translocase. Since this translocase is a core component of the mitochondrial permeability transition pore (MPTP) formed by apoptotic stimuli, BKA has been used as a tool to abrogate apoptosis. However, the other biochemical properties of BKA have not yet been resolved. Although the definition of a fatty acid is a carboxylic acid (-COOH) with a long hydrocarbon chain (tail), when focused on the chemical structure of BKA, the molecule was revealed to be a branched unsaturated tricarboxylic acid that resembled the structure of polyunsaturated fatty acids (PUFAs). Peroxisome proliferator-activated receptors (PPARs) consist of a subfamily of three isoforms: a, (3, and y, the ligands of which include PUFAs. Using completely synthesized BKA together with simplified BKA derivatives (purity: > 98%), we herein demonstrated the utility of BKA as a selective activator of the human PPARy isoform, which may not be associated with the anti-apoptotic nature of BKA. We also discussed the possible usefulness of BKA.

Original languageEnglish
Pages (from-to)223-233
Number of pages11
JournalJournal of Toxicological Sciences
Issue number2
Publication statusPublished - 2015

All Science Journal Classification (ASJC) codes

  • Toxicology


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