title: GPIHBP1 and Plasma Triglyceride Metabolism.
abstract: GPIHBP1, a GPI-anchored protein in capillary endothelial cells, is crucial for the lipolytic processing of triglyceride-rich lipoproteins (TRLs). GPIHBP1 shuttles lipoprotein lipase (LPL) to its site of action in the capillary lumen and is essential for the margination of TRLs along capillaries - such that lipolytic processing can proceed. GPIHBP1 also reduces the unfolding of the LPL catalytic domain, thereby stabilizing LPL catalytic activity. Many different GPIHBP1 mutations have been identified in patients with severe hypertriglyceridemia (chylomicronemia), the majority of which interfere with folding of the protein and abolish its capacity to bind and transport LPL. The discovery of GPIHBP1 has substantially revised our understanding of intravascular triglyceride metabolism but has also raised many new questions for future research.
authors.affiliation: Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095, USA. Electronic address: lfong@mednet.ucla.edu.
authors.forename: Loren G
authors.initials: LG
authors.lastname: Fong
authors.affiliation: Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095, USA; Department of Human Genetics, David Geffen School of Medicine, University of California, Los Angeles, CA 90095, USA. Electronic address: sgyoung@mednet.ucla.edu.
authors.forename: Stephen G
authors.initials: SG
authors.lastname: Young
authors.affiliation: Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095, USA.
authors.forename: Anne P
authors.initials: AP
authors.lastname: Beigneux
authors.affiliation: Division of Nutritional Science, Cornell University, Ithaca, NY 14853, USA.
authors.forename: André
authors.initials: A
authors.lastname: Bensadoun
authors.affiliation: Institute of Molecular Biosciences, University of Graz and BioTechMed, Graz, Austria.
authors.forename: Monika
authors.initials: M
authors.lastname: Oberer
authors.affiliation: Centre for Microscopy, Characterisation, and Analysis, The University of Western Australia.
authors.forename: Haibo
authors.initials: H
authors.lastname: Jiang
authors.affiliation: Finsen Laboratory, Rigshospitalet, 2200 Copenhagen N, Denmark; Biotech Research and Innovation Centre (BRIC), University of Copenhagen, 220 Copenhagen N, Denmark. Electronic address: m-ploug@finsenlab.dk.
authors.forename: Michael
authors.initials: M
authors.lastname: Ploug
mesh_terms: D000818:Animals; D006801:Humans; D015228:Hypertriglyceridemia / Q000097:blood / Q000378:metabolism; D008071:Lipoprotein Lipase / Q000235:genetics / Q000378:metabolism; D018110:Receptors, Lipoprotein / Q000235:genetics / Q000378:metabolism*; D014280:Triglycerides / Q000097:blood* / Q000378:metabolism
chemical_list: C523701:GPIHBP1 protein, human; D018110:Receptors, Lipoprotein; D014280:Triglycerides; D008071:Lipoprotein Lipase
keywords: LU (Ly6/uPAR) protein family; chylomicronemia; endothelial cells; hypertriglyceridemia; lipid transport; lipoprotein lipase