A newly discovered CETP splice variant in rabbit intestine, and its human counterpart, lacks the lipid-transfer-critical carboxy-end (Mol Cell Biochem 2003)

The cholesterol ester transfer protein (CETP) is found in plasma mediating the transfer of cholesterol esters and triacylglycerides between lipoproteins. The last 26 amino acids of its carboxy-end correspond to an amphipathic a-helix whose hydrophobic side has been directly involved in the transfer of lipids. Alterations in this region lead to the reduction or loss of lipid transfer activity. To date, the only variant of the CETP messenger that has been reported lacks exon 9, which translates into an inactive isoform regarding neutral lipid transfer. In this study, we describe a new version of the messenger RNA of rabbit CETP identified exclusively in the small intestine of wild type (WT) rabbits. This isoform includes several of the intron bases prior to exon 16. The presence of a stop codon within this sequence prevents translation of exon 16, substituting the original carboxy-end sequence and therefore generating a random structure that does not contain the region responsible for neutral lipid transfer. Antibodies generated against a peptide within the carboxy-end sequence of the new isoform show the presence of this new protein in human plasma.