GPIHBP1 and Plasma Triglyceride Metabolism

Loren G Fong; Stephen G Young; Anne P Beigneux; André Bensadoun; Monika Oberer; Haibo Jiang; Michael Ploug

doi:10.1016/j.tem.2016.04.013

GPIHBP1 and Plasma Triglyceride Metabolism

Loren G Fong, Stephen G Young, Anne P Beigneux, André Bensadoun, Monika Oberer, Haibo Jiang, Michael Ploug

52 Citations (Scopus)

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.

Original language	English
Journal	Trends in Endocrinology and Metabolism
Volume	27
Issue number	7
Pages (from-to)	455-69
Number of pages	15
ISSN	1043-2760
DOIs	https://doi.org/10.1016/j.tem.2016.04.013
Publication status	Published - 1 Jul 2016

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Journal Article
Review

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10.1016/j.tem.2016.04.013

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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.",

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TY - JOUR

T1 - GPIHBP1 and Plasma Triglyceride Metabolism

AU - Fong, Loren G

AU - Young, Stephen G

AU - Beigneux, Anne P

AU - Bensadoun, André

AU - Oberer, Monika

AU - Jiang, Haibo

AU - Ploug, Michael

PY - 2016/7/1

Y1 - 2016/7/1

N2 - 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.

AB - 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.

KW - Journal Article

KW - Review

U2 - 10.1016/j.tem.2016.04.013

DO - 10.1016/j.tem.2016.04.013

M3 - Review

C2 - 27185325

SN - 1043-2760

VL - 27

SP - 455

EP - 469

JO - Trends in Endocrinology and Metabolism

JF - Trends in Endocrinology and Metabolism

IS - 7

ER -

GPIHBP1 and Plasma Triglyceride Metabolism

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