GPIHBP1 and Lipoprotein Lipase, Partners in Plasma Triglyceride Metabolism

Stephen G Young; Loren G Fong; Anne P Beigneux; Christopher M Allan; Cuiwen He; Haibo Jiang; Katsuyuki Nakajima; Muthuraman Meiyappan; Gabriel Birrane; Michael Ploug

doi:10.1016/j.cmet.2019.05.023

GPIHBP1 and Lipoprotein Lipase, Partners in Plasma Triglyceride Metabolism

Stephen G Young, Loren G Fong, Anne P Beigneux, Christopher M Allan, Cuiwen He, Haibo Jiang, Katsuyuki Nakajima, Muthuraman Meiyappan, Gabriel Birrane, Michael Ploug

23 Citations (Scopus)

Abstract

Lipoprotein lipase (LPL), identified in the 1950s, has been studied intensively by biochemists, physiologists, and clinical investigators. These efforts uncovered a central role for LPL in plasma triglyceride metabolism and identified LPL mutations as a cause of hypertriglyceridemia. By the 1990s, with an outline for plasma triglyceride metabolism established, interest in triglyceride metabolism waned. In recent years, however, interest in plasma triglyceride metabolism has awakened, in part because of the discovery of new molecules governing triglyceride metabolism. One such protein-and the focus of this review-is GPIHBP1, a protein of capillary endothelial cells. GPIHBP1 is LPL's essential partner: it binds LPL and transports it to the capillary lumen; it is essential for lipoprotein margination along capillaries, allowing lipolysis to proceed; and it preserves LPL's structure and activity. Recently, GPIHBP1 was the key to solving the structure of LPL. These developments have transformed the models for intravascular triglyceride metabolism.

Original language	English
Journal	Cell Metabolism
Volume	30
Issue number	1
Pages (from-to)	51-65
Number of pages	15
ISSN	1550-4131
DOIs	https://doi.org/10.1016/j.cmet.2019.05.023
Publication status	Published - 2 Jul 2019

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title = "GPIHBP1 and Lipoprotein Lipase, Partners in Plasma Triglyceride Metabolism",

abstract = "Lipoprotein lipase (LPL), identified in the 1950s, has been studied intensively by biochemists, physiologists, and clinical investigators. These efforts uncovered a central role for LPL in plasma triglyceride metabolism and identified LPL mutations as a cause of hypertriglyceridemia. By the 1990s, with an outline for plasma triglyceride metabolism established, interest in triglyceride metabolism waned. In recent years, however, interest in plasma triglyceride metabolism has awakened, in part because of the discovery of new molecules governing triglyceride metabolism. One such protein-and the focus of this review-is GPIHBP1, a protein of capillary endothelial cells. GPIHBP1 is LPL's essential partner: it binds LPL and transports it to the capillary lumen; it is essential for lipoprotein margination along capillaries, allowing lipolysis to proceed; and it preserves LPL's structure and activity. Recently, GPIHBP1 was the key to solving the structure of LPL. These developments have transformed the models for intravascular triglyceride metabolism.",

author = "Young, {Stephen G} and Fong, {Loren G} and Beigneux, {Anne P} and Allan, {Christopher M} and Cuiwen He and Haibo Jiang and Katsuyuki Nakajima and Muthuraman Meiyappan and Gabriel Birrane and Michael Ploug",

year = "2019",

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doi = "10.1016/j.cmet.2019.05.023",

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T1 - GPIHBP1 and Lipoprotein Lipase, Partners in Plasma Triglyceride Metabolism

AU - Young, Stephen G

AU - Fong, Loren G

AU - Beigneux, Anne P

AU - Allan, Christopher M

AU - He, Cuiwen

AU - Jiang, Haibo

AU - Nakajima, Katsuyuki

AU - Meiyappan, Muthuraman

AU - Birrane, Gabriel

AU - Ploug, Michael

PY - 2019/7/2

Y1 - 2019/7/2

N2 - Lipoprotein lipase (LPL), identified in the 1950s, has been studied intensively by biochemists, physiologists, and clinical investigators. These efforts uncovered a central role for LPL in plasma triglyceride metabolism and identified LPL mutations as a cause of hypertriglyceridemia. By the 1990s, with an outline for plasma triglyceride metabolism established, interest in triglyceride metabolism waned. In recent years, however, interest in plasma triglyceride metabolism has awakened, in part because of the discovery of new molecules governing triglyceride metabolism. One such protein-and the focus of this review-is GPIHBP1, a protein of capillary endothelial cells. GPIHBP1 is LPL's essential partner: it binds LPL and transports it to the capillary lumen; it is essential for lipoprotein margination along capillaries, allowing lipolysis to proceed; and it preserves LPL's structure and activity. Recently, GPIHBP1 was the key to solving the structure of LPL. These developments have transformed the models for intravascular triglyceride metabolism.

AB - Lipoprotein lipase (LPL), identified in the 1950s, has been studied intensively by biochemists, physiologists, and clinical investigators. These efforts uncovered a central role for LPL in plasma triglyceride metabolism and identified LPL mutations as a cause of hypertriglyceridemia. By the 1990s, with an outline for plasma triglyceride metabolism established, interest in triglyceride metabolism waned. In recent years, however, interest in plasma triglyceride metabolism has awakened, in part because of the discovery of new molecules governing triglyceride metabolism. One such protein-and the focus of this review-is GPIHBP1, a protein of capillary endothelial cells. GPIHBP1 is LPL's essential partner: it binds LPL and transports it to the capillary lumen; it is essential for lipoprotein margination along capillaries, allowing lipolysis to proceed; and it preserves LPL's structure and activity. Recently, GPIHBP1 was the key to solving the structure of LPL. These developments have transformed the models for intravascular triglyceride metabolism.

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DO - 10.1016/j.cmet.2019.05.023

M3 - Review

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SN - 1550-4131

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SP - 51

EP - 65

JO - Cell Metabolism

JF - Cell Metabolism

IS - 1

ER -

GPIHBP1 and Lipoprotein Lipase, Partners in Plasma Triglyceride Metabolism

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