The class
Sodium butyrate induces a 3- to 4-fold rise in CETP mRNA in HepG2 liver cells, a model for CETP hepatic regulation (Eur J Biochem 1993)
Original title: The expression of human plasma cholesteryl-ester-transfer protein in HepG2 cells is induced by sodium butyrate. Quantification of low mRNA levels by polymerase chain reaction
Because CETP expression is very low in most transformed liver cell lines despite being primarily synthesized in the liver, researchers used the human hepatoma line HepG2, together with a quantitative reverse-transcribed PCR assay capable of measuring low CETP mRNA levels, as a model system for studying CETP gene regulation. Sodium butyrate produced a time-dependent and concentration-dependent 3- to 4-fold induction of CETP mRNA in these cells. CETP mass secreted into the culture medium also increased with butyrate treatment, though the effect at the protein level was less pronounced than at the mRNA level, establishing HepG2 cells with butyrate induction as a workable model for probing hepatic CETP transcriptional regulation.
Original abstract
Although human plasma cholesteryl-ester-transfer protein (CETP) is primarily synthesized in the liver, its expression in a number of transformed liver cell lines is very low. However the use of the human hepatoma cell line HepG2 as a model system for the regulation of CETP on mRNA level is facilitated by a quantitative reverse-transcribed polymerase chain reaction. We demonstrate a time-dependent and concentration-dependent 3-4-fold induction of CETP mRNA by sodium butyrate. CETP mass in the medium is also augmented; however, the effect on protein level is less pronounced.
Summary written by cetpinhibition.org from the published abstract; figures as published. Page updated 19 August 2026. Methods.