Carbon chain length of perfluoroalkylated carboxylic acids determines inhibitory strength on gonadal 3β-hydroxysteroid dehydrogenases in humans, rats, and mice

IC50型 类固醇 化学 抑制性突触后电位 生物化学 立体化学 生物 内科学 内分泌学 体外 激素 医学
作者
Huina Zhang,Shaowei Wang,Ya Chen,Jingjing Li,Yingna Zhai,Yunbing Tang,Huitao Li,Jianmin Sang,Hong Wang,Jieqiang Lv,Ren‐Shan Ge
出处
期刊:Toxicology Letters [Elsevier BV]
卷期号:389: 45-58 被引量:1
标识
DOI:10.1016/j.toxlet.2023.10.011
摘要

Perfluoroalkylated carboxylic acids (PFCAs) are a subclass of man-made chemicals that have been widely used in industrial production and consumer products. As a result, PFCAs have been found to accumulate in the environment and bioaccumulate in organisms, leading to potential health and environmental impacts. This study investigated the inhibition of 11 PFCAs on gonadal 3β-hydroxysteroid dehydrogenases in humans, rats, and mice. We observed a V-shaped inhibition pattern against human granulosa (KGN) cell 3β-HSD2 starting from C9 (half-maximal inhibitory concentration, IC50, 100.8 μM) to C11 (8.92 μM), with a V-shaped turn. The same V-shaped inhibition pattern was also observed for PFCAs against rat testicular 3β-HSD1 from C9 (IC50, 50.43 μM) to C11 (6.60 μM). Mouse gonadal 3β-HSD6 was insensitive to the inhibition of PFCAs, with an IC50 of 50.43 μM for C11. All of these PFCAs were mixed inhibitors of gonadal 3β-HSDs. Docking analysis showed that PFCAs bind to the nicotinamide adenine dinucleotide (NAD+)/steroid binding sites of these enzymes and bivariate correlation analysis showed that molecular length determines the inhibitory pattern of PFCAs on these enzymes. In conclusion, the carbon chain length determines the inhibitory strength of PFCAs on human, rat, and mouse gonadal 3β-HSDs, and the inhibitory strength of PFCAs against human and rat 3β-HSD enzymes shows V-shaped turn.
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