TY - JOUR
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
N1 - Copyright © 2019 Elsevier Inc. All rights reserved.
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.
U2 - 10.1016/j.cmet.2019.05.023
DO - 10.1016/j.cmet.2019.05.023
M3 - Review
C2 - 31269429
SN - 1550-4131
VL - 30
SP - 51
EP - 65
JO - Cell Metabolism
JF - Cell Metabolism
IS - 1
ER -