Mechanisms
A monoclonal antibody that blocks CETP's triglyceride transfer but not cholesteryl-ester transfer suggests the two lipids use distinct binding sites (J Biochem 1992)
Original title: Establishment of anti-human cholesteryl ester transfer protein monoclonal antibodies and radioimmunoassaying of the level of cholesteryl ester transfer protein in human plasma
Plasma cholesteryl ester transfer protein (CETP) facilitates net transfer and exchange of cholesteryl ester (CE), triglyceride (TG) and phospholipids between lipoproteins. The authors raised a series of monoclonal antibodies (mAbs) against human CETP, comprising mAbs that either inhibited or did not inhibit its transfer activities. One mAb, LT-J1, inhibited TG transfer activity almost completely but not CE transfer, suggesting the CE and TG binding sites on CETP may be distinct and that this mAb specifically recognizes the TG binding site. The authors also established a radioimmunoassay for CETP levels using these mAbs, finding plasma CETP levels in 20 normolipemic Japanese adults ranged from 2.1 to 2.7 mg/liter.
Original abstract
Plasma cholesteryl ester transfer protein (CETP) facilitates the net transfer and exchange of cholesteryl ester (CE), triglyceride (TG), and phospholipids between lipoproteins. A series of monoclonal antibodies (mAbs) against human CETP was obtained, comprising mAbs either inhibiting or not inhibiting these transfer activities. One mAb (LT-J1) inhibited the transfer activity of TG almost completely, but not that of CE, indicating that CE and TG binding sites on the CETP molecule may be distinct from each other, and that this mAb may specifically recognize the TG binding site. A radioimmunoassay system for determining the level of CETP was also established using these mAbs, and the plasma CETP levels in 20 normolipemic Japanese adults were found to range from 2.1 to 2.7 mg/liter.
Summary written by cetpinhibition.org from the published abstract; figures as published. Page updated 19 August 2026. Methods.