[Analysis of cDNA and protein structure of tree shrew cholesterol ester transfer protein]

To obtain the nucleotide sequence and deduced amino acid sequence of cholesteryl ester transfer protein (CETP) cDNA of tree shrew, mammalian insusceptible to atherosclerosis.

The first strand of cDNA of tree shrew was obtained from its liver. The sequence of tree shrew CETP cDNA was obtained by using techniques of switching mechanism at 5' end of RNA transcript (SMART) and rapid amplification of cDNA end (RACE), The CETP amino acid sequence was deduced from this cDNA and its primary and secondary structures were predicted by using DNAMAN, a software of molecular biology. Results The tree shrew CETP cDNA sequence covers 1636 bp, including a 178 bp fragment at the 3' of untranslated region and a 1458 bp fragment in the coding region, coding the complete sequence of mature tree shrew CETP except the initiator methionine. There are 477 amino acids in its mature protein, one amino acid more than that in human beings, with an extra Gly318. The homology of tree shrew CETP and human CETP and rabbit CETP is 88% and 82% respectively judged by comparing the amino acid sequence of tree shrew CETP and those of human beings and rabbit. The regions concerning the CETP function of binding and transferring neutral lipids in tree shrew CETP amino acid sequence are highly conservative. However, there is a deletion of N-linked glycosylation site at Asn342 in tree shrew protein that may increase the ability of removing peripheral cholesterol and cholesteryl ester.

The glycosylation in tree shrew CETP may be one of the mechanisms of insusceptibility to atherosis of tree shrew.