Carbonyl reductase 1 (CBR1) is a monomeric NADPH-dependent oxidoreductase found in various human tissues. It exhibits broad substrate specificity, primarily targeting carbonyl compounds. CBR1 plays a crucial role in detoxifying toxic environmental quinones and metabolizing pharmacologically significant substrates. Notably, it facilitates the conversion of prostaglandin E2 to prostaglandin F2-alpha.
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Carbonyl Reductase-1 (CBR1) is an enzyme that belongs to the short-chain dehydrogenases/reductases (SDR) family. This enzyme is widely distributed in human tissues and plays a crucial role in the metabolism of various carbonyl compounds, including quinones, prostaglandins, and xenobiotics . CBR1 is known for its NADPH-dependent oxidoreductase activity, which allows it to reduce carbonyl groups to their corresponding alcohols .
CBR1 is involved in several important biological processes. It metabolizes toxic environmental quinones and pharmacologically relevant substrates, such as the anticancer drug doxorubicin . Additionally, CBR1 converts prostaglandin E2 to prostaglandin F2-alpha, which is significant in various physiological processes . The enzyme also plays a protective role in oxidative stress, neurodegeneration, and apoptosis by inactivating lipid aldehydes during oxidative stress in cells .
CBR1 has been studied for its role in protecting cells against oxidative stress and its potential therapeutic applications. For instance, it has been identified as a target to improve the effect of radiotherapy on head and neck squamous cell carcinoma (HNSCC) . Research has shown that inhibiting CBR1 can enhance radiosensitivity in HNSCC cells, leading to better treatment outcomes . This makes CBR1 a promising target for developing new therapeutic strategies for cancer treatment.