Alternative splicing of human plasma cholesteryl ester transfer protein mRNA in Caco-2 cells and its modulation by oleic acid

作者：Dessi M^*; Motti C; Cortese C; Leonardis E; Giovannini C; Federici G; Piemonte F

来源：Molecular and Cellular Biochemistry, 1997, 177(1-2): 107-112.

DOI：10.1023/A:1006823601032

• cholesteryl ester
• CETP
• Caco-2
• polymerase chain reaction
• gene expression
• mRNA
• alternative splicing

Cholesteryl ester transfer protein (CETP) is a plasma protein involved in the reverse cholesterol transport and expressed in several human tissues and cell lines. We studied CETP expression in Caco-2 cell line, a model of the human enterocyte epithelium. By reverse-transcriptase polymerase chain reaction, we could demonstrate that in basal condition Caco-2 cells have a low rate of expression of active CETP mRNA. Furthermore, we found that even in this cell Line CETP mRNA alternative splicing occurs with deletion of exon 9 sequence. Densitometric analysis of the in vitro amplified fragments showed that under basal conditions about 60% of reverse transcribed CETP cDNA corresponds to exon 9-deleted transcripts. After challenge with 50 mu M sodium oleate, there is a similar to 2 fold increase in the transcription rate of the full-length CETP cDNA, as measured by competitive PCR, which is accompanied to an increased activity measured in the cell-conditioned medium. On the contrary, no significant change is seen in the amount of exon 9-deleted cDNA. Consequently, an inversion in the ratio of full-length and exon 9-deleted CETP cDNA is evident, suggesting that sodium oleate selectively enhances the expression of full-length CETP mRNA.

• 出版日期1997-12