AKR1B10 is an NADPH-dependent oxidoreductase that catalyzes the reduction of diverse carbonyl-containing compounds to their corresponding alcohols 1. The enzyme displays strong activity toward retinoids (all-trans-retinal, 9-cis-retinal, and 13-cis-retinal) and plays a critical role in detoxifying unsaturated carbonyls derived from diet and lipid peroxidation, including crotonaldehyde, 4-hydroxynonenal, and their glutathione conjugates 23. Unlike other aldo-keto reductases, AKR1B10 lacks reductase activity toward glucose 1. AKR1B10 has emerged as a clinically significant biomarker in metabolic and neoplastic diseases. In nonalcoholic fatty liver disease (NAFLD), circulating AKR1B10 concentrations strongly correlate with disease activity and fibrosis stage, with endoplasmic reticulum stress upregulating its expression 45. In hepatocellular carcinoma, AKR1B10 expression is elevated and promotes tumor progression through histone lactylation pathways 67. In breast cancer, AKR1B10 overexpression enhances cell migration and invasion via ERK signaling activation 8. Additionally, AKR1B10 mediates acquired chemoresistance to pemetrexed in lung cancer brain metastasis by promoting glycolysis and histone lactylation 9. Recent evidence demonstrates that direct AKR1B10 inhibition by berberine ameliorates NAFLD through PPAR signaling modulation 10, suggesting therapeutic potential for targeting this enzyme.