Article
Human carbonyl reductase 1 participating in intestinal first-pass drug metabolism is inhibited by fatty acids and acyl-CoAs.
Biochemical pharmacology - 15 Aug 2017
Hara Akira, Endo Satoshi, Matsunaga Toshiyuki, El-Kabbani Ossama, Miura Takeshi, Nishinaka Toru, Terada Tomoyuki
Abstract excerpt
Human carbonyl reductase 1 (CBR1), a member of the short-chain dehydrogenase/reductase (SDR) superfamily, reduces a variety of carbonyl compounds including endogenous isatin, prostaglandin E2 and 4-oxo-2-nonenal. It is also a major non-cytochrome P450 enzyme in the phase I metabolism of carbonyl-containing drugs, and is highly expressed in the intestine. In this study, we found that long-chain fatty acids and...
Topics
- Acyl Coenzyme A
- Alcohol Oxidoreductases
- Binding Sites
- Binding, Competitive
- Cell Line, Tumor
- Drug Resistance, Neoplasm
- Fatty Acids, Nonesterified
- Food-Drug Interactions
- Humans
- Intestinal Mucosa
- Mutation
- Myristic Acid
- Neoplasm Proteins