Cytochrome P450 2C and 2J epoxygenase (CYP2C/CYP2J)

Cytochrome P450 2C and 2J epoxygenases are a group of heme-containing enzymes, primarily including human isoforms CYP2C8, CYP2C9, and CYP2J2, that play a dual role in human physiology by metabolizing both endogenous lipids and exogenous drugs (UniProt: P11712, P51589). Their primary biological function involves the epoxidation of arachidonic acid to produce epoxyeicosatrienoic acids (EETs), which serve as critical autocrine and paracrine mediators in the cardiovascular and renal systems (PubMed: 20399742). EETs are known for their potent vasodilatory, anti-inflammatory, and cardioprotective properties, often acting as endothelium-derived hyperpolarizing factors (NIH: PMC3121021). Beyond lipid signaling, the CYP2C subfamily is responsible for the oxidative metabolism of approximately 20% of all clinical drugs, including narrow-therapeutic-index agents like warfarin (PubMed: 15970797). Dysregulation of these enzymes is implicated in the pathogenesis of hypertension and heart failure, while their role in promoting angiogenesis has raised concerns regarding their involvement in cancer progression (PubMed: 25633302). Consequently, these epoxygenases are vital targets for pharmacological research, particularly concerning drug-drug interactions and the development of therapies for cardiovascular and inflammatory diseases.

Other names

Arachidonic acid epoxygenasesP450 epoxygenasesCYP2C8CYP2C9CYP2J2CYP2C19

These enzymes catalyze the NADPH-dependent epoxidation of arachidonic acid to form epoxyeicosatrienoic acids (EETs), which function as autocrine and paracrine signaling molecules to regulate vascular tone and inflammatory responses.