CYP51A1 encodes lanosterol 14 alpha-demethylase, an enzyme involved in steroid biosynthesis (Stroemstedt et al, 1996; Strushkevich et al, 2010). CYP51A1 is upregulated during Schwann cell myelination in an EGR2- and SREBF2-dependent manner, and sites for these factors have been identified in the upstream promoter region (Nagarajan et al, 2001; Halder et al, 2002; LeBlanc et al, 2005; Jang et al, 2010).
Lanosterol 14-alpha demethylase (CYP51A1) catalyses oxidative C14-demethylation of lanosterol (LNSOL) to 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol (4,4DMCHOLtrienol). Although the reaction is annotated here as a single concerted event, studies with purified rat enzyme indicate that the methyl group is converted successively to an alcohol and an aldehyde before being released as formate (Stromstedt et al. 1996, Strushkevich et al. 2010).
SREBP1A (SREBF1A) or SREBP2, together with NF-Y and SP1, bind and transactivate the promoter of the CYP51A1 gene (Pai et al. 1998, Reed et al. 2008, Rome et al. 2008). SREBP1A and SREBP2 activate CYP51A1 equally (Pai et al. 1998).
CYP51A1 encodes lanosterol 14 alpha-demethylase, a protein involved in steroid biosynthetic pathways (Stromstedt et al, 1996; Strushkevich et al, 2010). Consistent with its expression during Schwann cell myelination, expression is synergistically activated by EGR2 and SREBF2 acting through cognate sites in the promoter (Nagarajan et al, 2001; Halder et al, 2002; LeBlanc et al, 2005; Jang et al, 2010).
The CYP51A1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein. SREBF1A (SREBP1A) and SREBF2 (SREBP2) bind the promoter of the Lanosterol Demethylase (CYP51A1) gene and enhance transcription (Pai et al. 1998, Sakakura et al. 2001, Halder et al. 2002, Reed et al. 2008, reviewed in Horton et al. 2002).