Peroxisome Proliferator-Activated Receptor γ Regulates the Expression of Lipid Phosphate Phosphohydrolase 1 in Human Vascular Endothelial Cells

Lipid phosphate phosphohydrolase 1 (LPP1), a membrane ectophosphohydrolase regulating the availability of bioactive lipid phosphates, plays important roles in cellular signaling and physiological processes such as angiogenesis and endothelial migration. However, the regulated expression of LPP1 rema...

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Main Authors: Yazi Huang, Beilei Zhao, Yahan Liu, Nanping Wang
Format: Article
Language:English
Published: Wiley 2014-01-01
Series:PPAR Research
Online Access:http://dx.doi.org/10.1155/2014/740121
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author Yazi Huang
Beilei Zhao
Yahan Liu
Nanping Wang
author_facet Yazi Huang
Beilei Zhao
Yahan Liu
Nanping Wang
author_sort Yazi Huang
collection DOAJ
description Lipid phosphate phosphohydrolase 1 (LPP1), a membrane ectophosphohydrolase regulating the availability of bioactive lipid phosphates, plays important roles in cellular signaling and physiological processes such as angiogenesis and endothelial migration. However, the regulated expression of LPP1 remains largely unknown. Here, we aimed to examine a role of peroxisome proliferator-activated receptor γ (PPARγ) in the transcriptional control of LPP1 gene expression. In human umbilical vein endothelial cells (HUVECs), quantitative reverse transcriptase polymerase chain reaction (qRT-PCR) demonstrated that activation of PPARγ increased the mRNA level of LPP1. Chromatin immunoprecipitation assay showed that PPARγ binds to the putative PPAR-responsive elements (PPREs) within the 5′-flanking region of the human LPP1 gene. Genomic fragment containing 1.7-kilobase of the promoter region was cloned by using PCR. The luciferase reporter assays demonstrated that overexpression of PPARγ and rosiglitazone, a specific ligand for PPARγ, could significantly upregulate the reporter activity. However, site-directed mutagenesis of the PPRE motif abolished the induction. In conclusion, our results demonstrated that PPARγ transcriptionally activated the expression of LPP1 gene in ECs, suggesting a potential role of PPARγ in the metabolism of phospholipids.
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issn 1687-4757
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publishDate 2014-01-01
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series PPAR Research
spelling doaj-art-0612630a498a4b3f925bdfb549c6a5302025-02-03T05:52:09ZengWileyPPAR Research1687-47571687-47652014-01-01201410.1155/2014/740121740121Peroxisome Proliferator-Activated Receptor γ Regulates the Expression of Lipid Phosphate Phosphohydrolase 1 in Human Vascular Endothelial CellsYazi Huang0Beilei Zhao1Yahan Liu2Nanping Wang3Institute of Cardiovascular Science, Peking University Health Science Center, Beijing 100191, ChinaInstitute of Cardiovascular Science, Peking University Health Science Center, Beijing 100191, ChinaInstitute of Cardiovascular Science, Peking University Health Science Center, Beijing 100191, ChinaInstitute of Cardiovascular Science, Peking University Health Science Center, Beijing 100191, ChinaLipid phosphate phosphohydrolase 1 (LPP1), a membrane ectophosphohydrolase regulating the availability of bioactive lipid phosphates, plays important roles in cellular signaling and physiological processes such as angiogenesis and endothelial migration. However, the regulated expression of LPP1 remains largely unknown. Here, we aimed to examine a role of peroxisome proliferator-activated receptor γ (PPARγ) in the transcriptional control of LPP1 gene expression. In human umbilical vein endothelial cells (HUVECs), quantitative reverse transcriptase polymerase chain reaction (qRT-PCR) demonstrated that activation of PPARγ increased the mRNA level of LPP1. Chromatin immunoprecipitation assay showed that PPARγ binds to the putative PPAR-responsive elements (PPREs) within the 5′-flanking region of the human LPP1 gene. Genomic fragment containing 1.7-kilobase of the promoter region was cloned by using PCR. The luciferase reporter assays demonstrated that overexpression of PPARγ and rosiglitazone, a specific ligand for PPARγ, could significantly upregulate the reporter activity. However, site-directed mutagenesis of the PPRE motif abolished the induction. In conclusion, our results demonstrated that PPARγ transcriptionally activated the expression of LPP1 gene in ECs, suggesting a potential role of PPARγ in the metabolism of phospholipids.http://dx.doi.org/10.1155/2014/740121
spellingShingle Yazi Huang
Beilei Zhao
Yahan Liu
Nanping Wang
Peroxisome Proliferator-Activated Receptor γ Regulates the Expression of Lipid Phosphate Phosphohydrolase 1 in Human Vascular Endothelial Cells
PPAR Research
title Peroxisome Proliferator-Activated Receptor γ Regulates the Expression of Lipid Phosphate Phosphohydrolase 1 in Human Vascular Endothelial Cells
title_full Peroxisome Proliferator-Activated Receptor γ Regulates the Expression of Lipid Phosphate Phosphohydrolase 1 in Human Vascular Endothelial Cells
title_fullStr Peroxisome Proliferator-Activated Receptor γ Regulates the Expression of Lipid Phosphate Phosphohydrolase 1 in Human Vascular Endothelial Cells
title_full_unstemmed Peroxisome Proliferator-Activated Receptor γ Regulates the Expression of Lipid Phosphate Phosphohydrolase 1 in Human Vascular Endothelial Cells
title_short Peroxisome Proliferator-Activated Receptor γ Regulates the Expression of Lipid Phosphate Phosphohydrolase 1 in Human Vascular Endothelial Cells
title_sort peroxisome proliferator activated receptor γ regulates the expression of lipid phosphate phosphohydrolase 1 in human vascular endothelial cells
url http://dx.doi.org/10.1155/2014/740121
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AT beileizhao peroxisomeproliferatoractivatedreceptorgregulatestheexpressionoflipidphosphatephosphohydrolase1inhumanvascularendothelialcells
AT yahanliu peroxisomeproliferatoractivatedreceptorgregulatestheexpressionoflipidphosphatephosphohydrolase1inhumanvascularendothelialcells
AT nanpingwang peroxisomeproliferatoractivatedreceptorgregulatestheexpressionoflipidphosphatephosphohydrolase1inhumanvascularendothelialcells