GPIHBP1, a GPI-anchored protein required for the lipolytic processing of triglyceride-rich lipoproteins
GPIHBP1, a small glycosylphosphatidylinositol-anchored glycoprotein, is required for the lipolytic processing of triglyceride-rich lipoproteins. GPIHBP1 knockout mice exhibit chylomicronemia, even on a low-fat diet, with plasma triglyceride levels of 3,500–5,000 mg/dl. GPIHBP1 is expressed highly in...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2009-01-01
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| Series: | Journal of Lipid Research |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S0022227520305873 |
| _version_ | 1818658439464747008 |
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| author | Anne P. Beigneux Brandon S.J. Davies André Bensadoun Loren G. Fong Stephen G. Young |
| author_facet | Anne P. Beigneux Brandon S.J. Davies André Bensadoun Loren G. Fong Stephen G. Young |
| author_sort | Anne P. Beigneux |
| collection | DOAJ |
| description | GPIHBP1, a small glycosylphosphatidylinositol-anchored glycoprotein, is required for the lipolytic processing of triglyceride-rich lipoproteins. GPIHBP1 knockout mice exhibit chylomicronemia, even on a low-fat diet, with plasma triglyceride levels of 3,500–5,000 mg/dl. GPIHBP1 is expressed highly in heart, adipose tissue, and skeletal muscle, the same tissues that express high levels of lipoprotein lipase (LPL). In each of these tissues, GPIHBP1 is located in capillary endothelial cells. Chinese hamster ovary (CHO) cells transfected with a GPIHBP1 expression vector bind LPL and chylomicrons avidly. The expression of GPIHBP1 in mice is modulated by fasting and refeeding and is also regulated by peroxisome proliferator-activated receptor (PPAR)γ agonists. Here, we review recent progress in understanding GPIHBP1 and discuss its role in lipolysis. |
| first_indexed | 2024-12-17T03:57:24Z |
| format | Article |
| id | doaj.art-fa4b643a615643da88f8268935399712 |
| institution | Directory Open Access Journal |
| issn | 0022-2275 |
| language | English |
| last_indexed | 2024-12-17T03:57:24Z |
| publishDate | 2009-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Lipid Research |
| spelling | doaj.art-fa4b643a615643da88f82689353997122022-12-21T22:04:35ZengElsevierJournal of Lipid Research0022-22752009-01-0150S57S62GPIHBP1, a GPI-anchored protein required for the lipolytic processing of triglyceride-rich lipoproteinsAnne P. Beigneux0Brandon S.J. Davies1André Bensadoun2Loren G. Fong3Stephen G. Young4To whom correspondence should be addressed; Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095; Department of Human Genetics, David Geffen School of Medicine, University of California, Los Angeles, CA 90095; Division of Nutritional Science, Cornell University, Ithaca, NY 14853Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095; Department of Human Genetics, David Geffen School of Medicine, University of California, Los Angeles, CA 90095; Division of Nutritional Science, Cornell University, Ithaca, NY 14853Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095; Department of Human Genetics, David Geffen School of Medicine, University of California, Los Angeles, CA 90095; Division of Nutritional Science, Cornell University, Ithaca, NY 14853To whom correspondence should be addressed; Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095; Department of Human Genetics, David Geffen School of Medicine, University of California, Los Angeles, CA 90095; Division of Nutritional Science, Cornell University, Ithaca, NY 14853To whom correspondence should be addressed; Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095; Department of Human Genetics, David Geffen School of Medicine, University of California, Los Angeles, CA 90095; Division of Nutritional Science, Cornell University, Ithaca, NY 14853GPIHBP1, a small glycosylphosphatidylinositol-anchored glycoprotein, is required for the lipolytic processing of triglyceride-rich lipoproteins. GPIHBP1 knockout mice exhibit chylomicronemia, even on a low-fat diet, with plasma triglyceride levels of 3,500–5,000 mg/dl. GPIHBP1 is expressed highly in heart, adipose tissue, and skeletal muscle, the same tissues that express high levels of lipoprotein lipase (LPL). In each of these tissues, GPIHBP1 is located in capillary endothelial cells. Chinese hamster ovary (CHO) cells transfected with a GPIHBP1 expression vector bind LPL and chylomicrons avidly. The expression of GPIHBP1 in mice is modulated by fasting and refeeding and is also regulated by peroxisome proliferator-activated receptor (PPAR)γ agonists. Here, we review recent progress in understanding GPIHBP1 and discuss its role in lipolysis.http://www.sciencedirect.com/science/article/pii/S0022227520305873chylomicronslipoprotein lipaseendothelialPPARγglycosylphosphatidylinositol |
| spellingShingle | Anne P. Beigneux Brandon S.J. Davies André Bensadoun Loren G. Fong Stephen G. Young GPIHBP1, a GPI-anchored protein required for the lipolytic processing of triglyceride-rich lipoproteins Journal of Lipid Research chylomicrons lipoprotein lipase endothelial PPARγ glycosylphosphatidylinositol |
| title | GPIHBP1, a GPI-anchored protein required for the lipolytic processing of triglyceride-rich lipoproteins |
| title_full | GPIHBP1, a GPI-anchored protein required for the lipolytic processing of triglyceride-rich lipoproteins |
| title_fullStr | GPIHBP1, a GPI-anchored protein required for the lipolytic processing of triglyceride-rich lipoproteins |
| title_full_unstemmed | GPIHBP1, a GPI-anchored protein required for the lipolytic processing of triglyceride-rich lipoproteins |
| title_short | GPIHBP1, a GPI-anchored protein required for the lipolytic processing of triglyceride-rich lipoproteins |
| title_sort | gpihbp1 a gpi anchored protein required for the lipolytic processing of triglyceride rich lipoproteins |
| topic | chylomicrons lipoprotein lipase endothelial PPARγ glycosylphosphatidylinositol |
| url | http://www.sciencedirect.com/science/article/pii/S0022227520305873 |
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