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Review
. 2021 Jan;32(1):48-61.
doi: 10.1016/j.tem.2020.11.005. Epub 2020 Dec 1.

Lipoprotein Lipase and Its Regulators: An Unfolding Story

Shuangcheng Alivia Wu  1 , Sander Kersten  2 , Ling Qi  3
Affiliations
Review

Lipoprotein Lipase and Its Regulators: An Unfolding Story

Shuangcheng Alivia Wu et al. Trends Endocrinol Metab. 2021 Jan.

Abstract

Lipoprotein lipase (LPL) is one of the most important factors in systemic lipid partitioning and metabolism. It mediates intravascular hydrolysis of triglycerides packed in lipoproteins such as chylomicrons and very-low-density lipoprotein (VLDL). Since its initial discovery in the 1940s, its biology and pathophysiological significance have been well characterized. Nonetheless, several studies in the past decade, with recent delineation of LPL crystal structure and the discovery of several new regulators such as angiopoietin-like proteins (ANGPTLs), glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPIHBP1), lipase maturation factor 1 (LMF1) and Sel-1 suppressor of Lin-12-like 1 (SEL1L), have completely transformed our understanding of LPL biology.

Keywords: ANGPTL; GPIHBP1; LMF1; LPL; SEL1L; endoplasmic reticulum; endothelium; hyperlipidemia.

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Figures

Figure 1.
Figure 1.. Functional domains, post-translational modifications and disease mutants of LPL and its regulators.
Schematic diagrams of amino acid structure of LPL (a), GPIHBP1 (b), LMF1 (c), SEL1L (d), ANGPTL3 (e), ANGPTL4 (f) and ANGPTL8 (g). The cytosolic, transmembrane and luminal domain of LMF1 are colored with orange, purple and gray, respectively (c). The two cysteine residues of ANGPTL4, C76 and C80, are required for its oligomerization (f). Several human mutations of LPL (a), GPIHBP1 (b) and ANGPTL4 (f) are listed above the structure. SP: signal peptide; TM, transmembrane domain.
Figure I.
Figure I.. The maturation, secretion and function of LPL.
Abbreviation: ANGPTLs, angiopoietin-like proteins including angiopoietin-like proteins 3, 4, and 8. Apos: apolipoproteins including apolipoprotein-CI, -CII, -CIII, -AV and -E. CM, chylomicron. ER, endoplasmic reticulum. HSPG, heparan sulfate proteoglycan. LMF1, lipase maturation factor 1. SEL1L, Sel-1 suppressor of Lin-12-Like 1. VLDL, very low-density lipoproteins.
See this image and copyright information in PMC

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