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Neutralizing antibodies against the 74kDa CETP eliminate essentially all plasma cholesteryl ester and triglyceride transfer activity, proving CETP is the responsible protein (J Biol Chem 1988)

Original title: Monoclonal antibodies to the Mr 74,000 cholesteryl ester transfer protein neutralize all of the cholesteryl ester and triglyceride transfer activities in human plasma

J Biol Chem · · 9

Hesler CB, Tall AR, Swenson TL, Weech PK, Marcel YL, Milne RW

A cholesteryl ester transfer protein (CETP) of apparent Mr 74,000 had recently been purified from human plasma. The authors obtained three monoclonal neutralizing antibodies to CETP by immunizing mice with the purified protein. Each antibody, recognizing a similar CETP epitope, caused parallel and complete immunotitration of plasma cholesteryl ester and triglyceride transfer activities, but only partial inhibition of phospholipid transfer activity. Monoclonal immunoaffinity chromatography of plasma or its fractions completely removed cholesteryl ester and triglyceride transfer activities but only incompletely removed phospholipid transfer activity. SDS gel electrophoresis and immunoblotting of the immunoaffinity-retained fractions showed only the Mr 74,000 protein was immunoreactive. The previously characterized CETP thus accounts for all cholesteryl ester and triglyceride transfer activity in human plasma, but only part of the phospholipid transfer activity.

PubMed

Original abstract

A cholesteryl ester transfer protein (CETP) of apparent Mr 74,000 has recently been purified from human plasma. Three monoclonal neutralizing antibodies to the CETP were obtained by immunizing mice with purified CETP. The antibodies, each recognizing a similar epitope on CETP, caused parallel and complete immunotitration of plasma cholesteryl ester and triglyceride transfer activities but only partial inhibition of phospholipid transfer activity. Monoclonal immunoaffinity chromatography of plasma or its fractions showed complete removal of cholesteryl ester and triglyceride transfer activities but incomplete removal of phospholipid transfer activity. Sodium dodecyl sulfate gel electrophoresis and immunoblotting of the immunoaffinity-retained fractions showed that only the Mr 74,000 protein was immunoreactive. The results suggest that the previously characterized CETP accounts for all of the cholesteryl ester and triglyceride transfer activity in human plasma but only part of the phospholipid transfer activity.

mechanisms

Summary written by cetpinhibition.org from the published abstract; figures as published. Page updated 19 August 2026. Methods.