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Department of Medicine II (S.N., C.S., M.U., S.T., M.E., H.M., N.Y., T.K.), Hokkaido University Graduate School of Medicine, Sapporo 060-8638, Japan; and Health Administration Center, Hokkaido University of Education (M.K.), Sapporo 002-8501, Japan
Address all correspondence and requests for reprints to: Chikara Shimizu, M.D., Ph.D, Department of Medicine II, Hokkaido University Graduate School of Medicine, N-15, W-7, Kita-ku, Sapporo 060-8638, Japan. E-mail: shimizch{at}med.hokudai.ac.jp.
Perilipin, a family of phosphoproteins located around lipid droplets in adipocytes, is essential for enlargement of lipid droplets and lipolytic reaction by hormone-sensitive lipase. Thiazolidinediones, peroxisome proliferator-activated receptor (PPAR) 
agonists, have been shown to increase perilipin expression in fully differentiated adipocytes. However, the precise mechanism of transcriptional regulation of murine perilipin gene heretofore remains unclear. We determined the transcription start site of murine perilipin gene by RNA ligase-mediated rapid amplification of the cDNA ends method. We generated luciferase reporter gene constructs containing various lengths of the 5'-flanking region of the murine perilipin gene and assayed promoter/enhancer activities using differentiated 3T3-L1 adipocytes. We identified a functional PPAR-responsive element (PPRE) in the murine perilipin promoter, and this was confirmed by gel EMSAs using nuclear extracts from differentiated 3T3-L1 adipocytes. Furthermore, point mutations of the identified functional PPRE markedly reduced both the reporter gene activity in differentiated 3T3-L1 adipocytes and PPAR/thiazolidinedione-induced transactivation in NIH-3T3 fibroblasts. Real-time RT-PCR revealed that thiazolidinedione up-regulates endogenous perilipin mRNA levels. We propose that PPAR plays a significant role in the transcriptional regulation of murine perilipin gene via the PPRE in its promoter.
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