High impact information on SC4MOL

• Characterization of yeast methyl sterol oxidase (ERG25) and identification of a human homologue [1].
• A human homologue of ERG25 was cloned, sequenced, and mapped to human chromosome 4q32-34 [1].
• Finally, in cell transfection experiments SREBP-2 overexpression blocks ERG25 downregulation caused by LDL [2].
• Downregulation of ERG25 by LDL was abolished by an inhibitor of neutral cysteine proteases (N-acetyl-leucyl-leucyl-norleucinal) that abrogates SREBP catabolism [2].
• ERG25, an enzyme involved in cholesterol biosynthesis, is expressed in vascular endothelial and SMC from porcine and human origin and is downregulated by LDL in a time- and dose-dependent manner [2].

Anatomical context of SC4MOL

• METHODS: Expression levels of C-4 sterol methyl oxidase gene (ERG25), sterol regulatory element binding protein (SREBP)-1 and -2 were evaluated in porcine aortic endothelial cells (PAEC), porcine and human smooth muscle cells (SMC) and in the vascular wall from normolipemic and hyperlipemic pigs by RT-PCR [2].

Associations of SC4MOL with chemical compounds

• Sequence analysis and functional assays indicated that the cloned gene was identical to ERG25, a gene that codes for methyl sterol oxidase [1].

Other interactions of SC4MOL

• CONCLUSIONS: Our results indicate that LDL modulate ERG25 expression in the vascular wall and suggest the involvement of SREBP-2 in this mechanism [2].

Analytical, diagnostic and therapeutic context of SC4MOL

• KTC exposure induced transcription of genes involved in lipid, fatty acid, and sterol metabolism, including ERG11, ERG3, ERG25, ERG6, ERG26, ERG24, ERG4, CPO, INO1, DW700960, CPR, DW696584, DW406350, and ATG15 [3].

References