AI Article Synopsis
- The study focuses on the human cytochrome P450 2U1 (CYP2U1), a recently identified enzyme primarily found in the brain and thymus, and linked to the conversion of arachidonic acid into important compounds.
- Researchers investigated genetic variations in CYP2U1 among 70 French individuals, identifying four specific polymorphisms in its coding and regulatory regions.
- The most common mutations identified did not appear to affect CYP2U1's expression in the lung, indicating that this enzyme likely plays a crucial role in internal biological processes with limited genetic variability.
Article Abstract
The human cytochrome P450 2U1 (CYP2U1) has been described as a novel extrahepatic P450. CYP2U1 is a highly conserved gene mainly expressed in brain and thymus, but also at lower levels in kidney, lung or heart. This selective tissue distribution suggests important endogenous functions, in particular in the conversion of arachidonic acid into two bioactive compounds, the 19- and 20-HETE. To investigate the extent of CYP2U1 genetic polymorphism in 70 French individuals, a screening for sequence variations in the 5'-flanking and protein encoding regions was performed using PCR-SSCP and sequencing strategies. Four polymorphisms were identified and correspond to -204C>A and -241T>C in the 5'-flanking region, -37G>A in the 5'-untranslated region, and IVS2-17T>C in the intron 2. The most frequent mutations, -241T>C (59.7%) and IVS2-17T>C (66.0%), did not seem to alter CYP2U1 lung expression. These results suggest that CYP2U1 exhibits few genetic variations and support a probable role in endogenous processes.
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| http://dx.doi.org/10.1016/j.plefa.2010.06.005 | DOI Listing |
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