Farnesylacetone

Farnesylacetone acts as a transcriptional regulator, RNA synthesis regulator, and protein synthesis regulator. Farnesylacetone is synthesized in the androgenic glands of the green crab (Carcinus maenas). Farnesylacetone modulates transcriptional processes, inhibits uridine incorporation into all types of RNA and leucine incorporation into ovaries, while stimulating uridine incorporation into tRNA/poly (A)⁺ RNA and leucine incorporation into testes. Farnesylacetone inhibits electron transport in mitochondrial Complex I and Complex II. Farnesylacetone inhibits vitellogenesis in crustacean ovaries and stimulates uridine incorporation in crustacean intestines. Farnesylacetone functions as an androgen in crustaceans^[1][2]. In Vitro:Farnesylacetone (100 nM; 1-3 h) inhibits protein and RNA synthesis in immature and mature ovaries of Carcinus maenas, promotes protein and RNA synthesis in testes of Carcinus maenas, and exerts its effects at the transcriptional level rather than directly acting on the translation process^[1].
Farnesylacetone (20 ng/mL; 3 h) stimulates RNA synthesis in the intestine of Carcinus maenas (shore crab), and exhibits organ specificity, as it only inhibits RNA synthesis in the ovary^[1].
Farnesylacetone (228 μM) inhibits electron transfer through Complex I (NADH ubiquinone reductase) and Complex II (succinate ubiquinone reductase) in isolated rat liver mitochondria, but does not inhibit electron transfer through Complex IV (cytochrome c oxidase); among these, succinate-driven electron transfer is more sensitive to it than NADH-driven electron transfer^[2].
Farnesylacetone (228-380 μM) specifically inhibits electron transfer between succinate dehydrogenase within Complex II and the ubiquinone pool in isolated rat liver mitochondria, with no inhibitory effect on succinate dehydrogenase itself; 380 μM Farnesylacetone reduces Complex II activity by 68.5% while increasing succinate dehydrogenase activity by 8%^[2].
Farnesylacetone (1 mM) neither inhibits the oxidation of DQH₂ nor the reduction of DQ in a cell-free system; instead, it stimulates electron transfer from the NADH + DQ conjugate to cytochrome c^[2].