GPIHBP1—an endothelial cell molecule important for the lipolytic processing of chylomicrons

Stephen G Young; Brandon S. J Davies; Loren G Fong; Peter Gin; Michael M Weinstein; André Bensadoun; Anne P Beigneux

doi:10.1097/MOL.0b013e3281527914

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GPIHBP1—an endothelial cell molecule important for the lipolytic processing of chylomicrons

Journal article

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GPIHBP1—an endothelial cell molecule important for the lipolytic processing of chylomicrons

Stephen G Young, Brandon S. J Davies, Loren G Fong, Peter Gin, Michael M Weinstein, André Bensadoun and Anne P Beigneux

Current opinion in lipidology, Vol.18(4), pp.389-396

08/2007

DOI: 10.1097/MOL.0b013e3281527914

PMCID: PMC2888298

PMID: 17620854

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https://www.ncbi.nlm.nih.gov/pmc/articles/2888298View

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Abstract

Purpose of review: To summarize recent data indicating that glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1) plays a key role in the lipolytic processing of chylomicrons. Recent findings: Lipoprotein lipase hydrolyses triglycerides in chylomicrons at the luminal surface of the capillaries in heart, adipose tissue, and skeletal muscle. The endothelial cell molecule that facilitates the lipolytic processing of chylomicrons has never been clearly defined. Mice lacking GPIHBP1 manifest chylomicronemia, with plasma triglyceride levels as high as 5000 mg/dl. In wild-type mice, GPIHBP1 is expressed on the luminal surface of capillaries in heart, adipose tissue, and skeletal muscle. Cells transfected with GPIHBP1 bind both chylomicrons and lipoprotein lipase avidly. Summary: The chylomicronemia in Gpihbp1-deficient mice, the fact that GPIHBP1 is located within the lumen of capillaries, and the fact that GPIHBP1 binds lipoprotein lipase and chylomicrons suggest that GPIHBP1 is a key platform for the lipolytic processing of triglyceride-rich lipoproteins.

Chylomicronemia

hypertriglyceridemia

GPI-anchored proteins

lipoprotein lipase

Details

Title: Subtitle: GPIHBP1—an endothelial cell molecule important for the lipolytic processing of chylomicrons
Creators: Stephen G Young - Department of Medicine/Division of Cardiology, David Geffen School of Medicine, University of California, Los Angeles, CA 90095
Brandon S. J Davies - Department of Medicine/Division of Cardiology, David Geffen School of Medicine, University of California, Los Angeles, CA 90095
Loren G Fong - Department of Medicine/Division of Cardiology, David Geffen School of Medicine, University of California, Los Angeles, CA 90095
Peter Gin - Department of Medicine/Division of Cardiology, David Geffen School of Medicine, University of California, Los Angeles, CA 90095
Michael M Weinstein - Department of Medicine/Division of Cardiology, David Geffen School of Medicine, University of California, Los Angeles, CA 90095
André Bensadoun - Division of Nutritional Sciences, Cornell University, Ithaca, NY 14853
Anne P Beigneux - Department of Medicine/Division of Cardiology, David Geffen School of Medicine, University of California, Los Angeles, CA 90095
Resource Type: Journal article
Publication Details: Current opinion in lipidology, Vol.18(4), pp.389-396
DOI: 10.1097/MOL.0b013e3281527914
PMID: 17620854
PMCID: PMC2888298
NLM abbreviation: Curr Opin Lipidol
ISSN: 0957-9672
eISSN: 1473-6535
Language: English
Date published: 08/2007
Academic Unit: Fraternal Order of Eagles Diabetes Research Center; Biochemistry and Molecular Biology
Record Identifier: 9984025271602771

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