HDL biology
CETP mRNA sequences are detected in ovary, lung, intestine, and heart tissue, not just liver, suggesting a locally active membrane-bound CETP form (Biochem Biophys Res Commun 1994)
Original title: Membrane bound CETP mediates the transfer of free cholesterol between lipoproteins and membranes
While CETP is known to transfer cholesteryl esters among plasma lipoproteins, this study found that when reconstituted into phosphatidylcholine liposomes, the 74,000-molecular-weight protein mediates transfer of HDL-bound [3H]cholesterol into the artificial membrane system above non-specific values. Using oligonucleotide probes designed from the known CETP cDNA sequence, the authors examined RNA isolated from liver, a known CETP-producing tissue, and from ovary, lung, intestine, and heart, tissues not thought to synthesize and secrete CETP. Hybridization experiments detected CETP sequences regardless of tissue type tested. The authors suggest that a membrane-bound form of CETP might have locally important physiological effects.
Original abstract
Cholesteryl ester transfer protein (CETP) has been shown to transfer cholesteryl esters among plasma lipoproteins. However, when reconstituted into phosphatidylcholine liposomes, the 74,000 protein mediates above non-specific values the transfer of HDL bound [3H]cholesterol into the artificial membrane system. Employing the known cDNA sequence of CETP, we synthesized a series of oligonucleotides with specific sequences for different regions of CETP and RNA isolated from tissues known to be producers of CETP (liver), and tissues not design to synthesize and secrete CETP (ovary, lung, intestine and heart). Hybridization experiments showed that independently of the type of tissue tested CETP sequences were found. It is suggested that a membrane form of CETP might have important repercussions locally.
Summary written by cetpinhibition.org from the published abstract; figures as published. Page updated 19 August 2026. Methods.