Normal binding of lipoprotein lipase, chylomicrons, and apo-AV to GPIHBP1 containing a G56R amino acid substitution

Peter Gin; Anne P Beigneux; Brandon Davies; Madeline F Young; Robert O Ryan; André Bensadoun; Loren G Fong; Stephen G Young

doi:10.1016/j.bbalip.2007.10.005

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Normal binding of lipoprotein lipase, chylomicrons, and apo-AV to GPIHBP1 containing a G56R amino acid substitution

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Normal binding of lipoprotein lipase, chylomicrons, and apo-AV to GPIHBP1 containing a G56R amino acid substitution

Peter Gin, Anne P Beigneux, Brandon Davies, Madeline F Young, Robert O Ryan, André Bensadoun, Loren G Fong and Stephen G Young

Biochimica et biophysica acta. Molecular and cell biology of lipids, Vol.1771(12), pp.1464-1468

2007

DOI: 10.1016/j.bbalip.2007.10.005

PMCID: PMC2266775

PMID: 17997385

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https://www.ncbi.nlm.nih.gov/pmc/articles/2266775View

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Abstract

GPIHBP1 is an endothelial cell protein that serves as a platform for lipoprotein lipase-mediated processing of triglyceride-rich lipoproteins within the capillaries of heart, adipose tissue, and skeletal muscle. The absence of GPIHBP1 causes severe chylomicronemia. A hallmark of GPIHBP1 is the ability to bind lipoprotein lipase, chylomicrons, and apolipoprotein (apo-) AV. A homozygous G56R mutation in GPIHBP1 was recently identified in two siblings with chylomicronemia, and the authors of that study suggested that the G56R substitution was responsible for the hyperlipidemia. In this study, we created a human GPIHBP1 expression vector, introduced the G56R mutation, and tested the ability of the mutant GPIHBP1 to reach the cell surface and bind lipoprotein lipase, chylomicrons, and apo-AV. Our studies revealed that the G56R substitution did not affect the ability of GPIHBP1 to reach the cell surface, nor did the amino acid substitution have any discernible effect on the binding of lipoprotein lipase, chylomicrons, or apo-AV.

Chylomicronemia

Lipoprotein lipase

Hypertriglyceridemia

Apolipoprotein AV

GPIHBP1

Details

Title: Subtitle: Normal binding of lipoprotein lipase, chylomicrons, and apo-AV to GPIHBP1 containing a G56R amino acid substitution
Creators: Peter Gin - Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA, USA
Anne P Beigneux - Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA, USA
Brandon Davies - Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA, USA
Madeline F Young - Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA, USA
Robert O Ryan - Children’s Hospital Oakland Research Institute, Oakland, CA 94609, USA
André Bensadoun - Division of Nutritional Sciences, Cornell University, Ithaca, NY 14853, USA
Loren G Fong - Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA, USA
Stephen G Young - Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA, USA
Resource Type: Journal article
Publication Details: Biochimica et biophysica acta. Molecular and cell biology of lipids, Vol.1771(12), pp.1464-1468
DOI: 10.1016/j.bbalip.2007.10.005
PMID: 17997385
PMCID: PMC2266775
NLM abbreviation: Biochim Biophys Acta Mol Cell Biol Lipids
ISSN: 1388-1981
eISSN: 1879-2618
Publisher: Elsevier B.V
Language: English
Date published: 2007
Academic Unit: Fraternal Order of Eagles Diabetes Research Center; Biochemistry and Molecular Biology
Record Identifier: 9984025271302771

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