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The Expression of GPIHBP1, an Endothelial Cell Binding Site for Lipoprotein Lipase and Chylomicrons, Is Induced by Peroxisome Proliferator-Activated Receptor-

Departments of Medicine (B.S.J.D., A.P.B., E.F., L.G.F., S.G.Y.), Pathology and Laboratory Medicine (H.W., D.C.W., P.T.), and Human Genetics (M.M.W., S.G.Y.), David Geffen School of Medicine, University of California, Los Angeles, California 90095; Howard Hughes Medical Institute (H.W., D.C.W., L.-J.T., R.M.E., P.T.) and Gene Expression Laboratory (L.-J.T., R.M.E.), Salk Institute for Biological Studies, La Jolla, California 92037; and Division of Endocrinology and Metabolism (L.-J.T.), Department of Medicine, University of California, San Diego, La Jolla, California 92093

Address all correspondence and requests for reprints to: Brandon S. J. Davies, 650 Charles E. Young Drive South, Los Angeles, California 90095. E-mail: bdavies{at}mednet.ucla.edu.

Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPIHBP1), a protein in the lymphocyte antigen 6 (Ly-6) family, plays a key role in the lipolytic processing of triglyceride-rich lipoproteins. GPIHBP1 binds lipoprotein lipase and chylomicrons and is expressed along the luminal surface of microvascular endothelial cells. Lipolysis is known to be regulated by metabolic factors and is controlled at multiple levels, including the number of LPL binding sites on capillaries. Here, we tested the possibility that GPIHBP1 expression could be regulated by dietary perturbations and by peroxisome proliferator-activated receptors (PPARs). Gpihbp1 transcript levels in the heart and in brown and white adipose tissue increased with fasting and returned toward baseline after refeeding. A PPAR agonist increased Gpihbp1 expression in adipose tissue, heart, and skeletal muscle, whereas PPAR and PPAR agonists had no effect. Gpihbp1 was expressed in endothelial cells of embryoid bodies generated from mouse embryonic stem cells, and Gpihbp1 expression in embryoid bodies was up-regulated by a PPAR agonist. Sequences upstream from exon 1 of Gpihbp1 contain a strong PPAR binding site, and that site exhibited activity in a luciferase reporter assay. Gpihbp1 transcript levels in brown and white adipose tissue were lower in endothelial cell PPAR knockout mice than in littermate control mice, suggesting that PPAR regulates Gpihbp1 expression in vivo. We conclude that GPIHBP1 is regulated by dietary factors and by PPAR.

NURSA Molecule Pages Link:

Nuclear Receptors:   PPARα  |  PPARγ  |  RXRα

Ligands:   Rosiglitazone

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