Akr1b10, an aldo-keto reductase family 1 member B10, is a human nicotinamide adenine dinucleotide phosphate (NADPH)-dependent reductase [3]. It catalyzes the reduction of aldehydes, some ketones and quinones, and is involved in multiple biological processes. It interacts with acetyl-CoA carboxylase and heat shock protein 90α. AKR1B10 has been implicated in pathways related to cell proliferation, migration, invasion, and metabolic reprogramming, which are crucial in various physiological and pathophysiological conditions [3].

In breast cancer, overexpression of Akr1b10 promotes cell proliferation, migration, and invasion via the PI3K/AKT/NF-κB signaling pathway [1]. In lung cancer-derived brain metastasis, silencing Akr1b10 increases sensitivity to pemetrexed, as Akr1b10-enhanced Warburg effect contributes to acquired resistance through regulating glycolysis and histone lactylation [2]. In non-alcoholic fatty liver disease (NAFLD), berberine targets Akr1b10 to modulate lipid and glucose metabolism disorders [4].

In conclusion, Akr1b10 plays significant roles in cancer development, chemoresistance, and metabolic diseases. Loss-of-function experiments in models, such as silencing in cell lines, have revealed its functions in promoting cancer cell progression and contributing to drug resistance in cancer, as well as its role in metabolic regulation in NAFLD. These findings suggest Akr1b10 as a potential target for diagnosing and treating these diseases [1,2,3,4].