Journal article
GPIHBP1 Is Responsible for the Entry of Lipoprotein Lipase into Capillaries
Cell metabolism, Vol.12(1), pp.42-52
2010
DOI: 10.1016/j.cmet.2010.04.016
PMCID: PMC2913606
PMID: 20620994
Abstract
The lipolytic processing of triglyceride-rich lipoproteins by lipoprotein lipase (LPL) is the central event in plasma lipid metabolism, providing lipids for storage in adipose tissue and fuel for vital organs such as the heart. LPL is synthesized and secreted by myocytes and adipocytes, but then finds its way into the lumen of capillaries, where it hydrolyzes lipoprotein triglycerides. The mechanism by which LPL reaches the lumen of capillaries has remained an unresolved problem of plasma lipid metabolism. Here, we show that GPIHBP1 is responsible for the transport of LPL into capillaries. In
Gpihbp1-deficient mice, LPL is mislocalized to the interstitial spaces surrounding myocytes and adipocytes. Also, we show that GPIHBP1 is located at the basolateral surface of capillary endothelial cells and actively transports LPL across endothelial cells. Our experiments define the function of GPIHBP1 in triglyceride metabolism and provide a mechanism for the transport of LPL into capillaries.
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► GPIHBP1 is required for proper targeting of LPL to the lumen of capillaries ► GPIHBP1 is found on both the basolateral and apical surfaces of endothelial cells ► GPIHBP1 transports a GPIHBP1-specific monoclonal antibody across endothelial cells ► GPIHBP1 also transports LPL, providing a mechanism for LPL entry into capillaries
Details
- Title: Subtitle
- GPIHBP1 Is Responsible for the Entry of Lipoprotein Lipase into Capillaries
- Creators
- Brandon S.J Davies - Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USAAnne P Beigneux - Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USARichard H Barnes II - Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USAYiping Tu - Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USAPeter Gin - Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USAMichael M Weinstein - Department of Human Genetics, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USAChika Nobumori - Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USARakel Nyrén - Department of Medical Biosciences/Physiological Chemistry, Umeå University, S-901 87 Umeå, SwedenIra Goldberg - Department of Medicine, Columbia University College of Physicians and Surgeons, New York, NY 10032, USAGunilla Olivecrona - Department of Medical Biosciences/Physiological Chemistry, Umeå University, S-901 87 Umeå, SwedenAndré Bensadoun - Division of Nutritional Science, Cornell University, Ithaca, NY 14853, USAStephen G Young - Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USALoren G Fong - Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USA
- Resource Type
- Journal article
- Publication Details
- Cell metabolism, Vol.12(1), pp.42-52
- Publisher
- Elsevier Inc
- DOI
- 10.1016/j.cmet.2010.04.016
- PMID
- 20620994
- PMCID
- PMC2913606
- ISSN
- 1550-4131
- eISSN
- 1932-7420
- Language
- English
- Date published
- 2010
- Academic Unit
- Fraternal Order of Eagles Diabetes Research Center; Biochemistry and Molecular Biology
- Record Identifier
- 9984024412702771
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