Cytochrome P450 family 4 subfamily Z member 1 (CYP4Z1)

Cytochrome P450 family 4 subfamily Z member 1 (CYP4Z1) is an enzyme in the cytochrome P450 superfamily, functioning as an in-chain fatty acid monooxygenase, primarily catalyzing hydroxylation of lauric and myristic acid at multiple internal positions[2][4]. CYP4Z1 is almost exclusively and highly overexpressed in several human cancers—including breast, ovarian, prostate, colon, adrenal cortex, and others—while having minimal or no expression in corresponding normal tissues[5]. Its cancer-associated overexpression correlates with poor prognosis and enhanced tumor angiogenesis, possibly due to increased production of signaling lipid molecules such as 20-hydroxyeicosatetraenoic acid (20-HETE) and vascular endothelial growth factor-A (VEGF-A)[1][5]. Experimental evidence suggests it may be regulated by glucocorticoid and progesterone receptor activation[1][5]. CYP4Z1 is being studied as a biomarker and possible therapeutic target for drug screening and cancer therapy development, though selective inhibitors remain a challenge[3][5].

Other names

CYP4Z1Cytochrome P450 4Z1CYP4A20CYPIVZ1Laurate 7-monooxygenasecytochrome P450, family 4, subfamily Z, polypeptide 1UNQ3060/PRO9882

Enzyme inhibition (experimental use of CYP4 inhibitors such as HET0016, although with low efficacy for CYP4Z1) Prodrug strategies (potential use of CYP4Z1-expressing models to activate prodrugs selectively in cancer)