Lipoprotein lipase and its regulators: an unfolding story
Open accessAbstract
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.
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Smaller VLDL2 is also made by the liver and can be delipidated to intermediate-density lipoprotein and low-density lipoprotein.
“Smaller VLDL2 is also made by the liver and can be delipidated to intermediate-density lipoprotein and low-density lipoprotein (for more detail see refs43–45).”
ANGPTL3 and ANGPTL8 inhibit lipoprotein lipase activity in skeletal muscle in the fed state, and ANGPTL4 inhibits lipoprotein lipase activity in white adipose tissue during fasting.
“In addition, ANGPTL3 and ANGPTL8 inhibit lipoprotein lipase activity in skeletal muscle in the fed state and ANGPTL4 inhibits lipoprotein lipase activity in white adipose tissue during fasting.45”
The primary role of triglyceride-rich lipoproteins is to transport triglyceride to adipose tissue for storage and to skeletal and cardiac muscle for energy production.
“The primary role of TRL is to transport TG to adipose tissue for storage and to skeletal and cardiac muscle for energy production.”
ANGPTL3, ANGPTL4, and ANGPTL8 are inhibitors of lipoprotein lipase and play important roles in targeting chylomicrons and VLDL to white adipose tissue or skeletal muscle, depending on nutritional and hormonal status.
“ANGPTL3, 4, and 8 are inhibitors of LpL and play important roles in targeting chylomicrons and VLDL to white adipose tissue or skeletal muscle, depending on nutritional and hormonal status at any time.45”
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References 134 · Cited by 225
Research works printed but not linked: 1
- [88]Georgiadi A,, Induction of cardiac Angptl4 by dietary fatty acids is mediated by PPARβ/δ and protects against oxidative stress: P18. European Journal of Clinical Nutrition, 2009. 63.
- Authors
- Wu, S. A., Kersten, S., & Qi, L.
- Affiliations
- University of Michigan (US)
- Wageningen University & Research (NL)
- Corresponding author
- Wu, Shuangcheng Alivia
- Qi, Ling
- Venue
- Trends in Endocrinology & Metabolism
- Publisher
- Elsevier BV
- Published
- 2021-01
- Volume
- 32
- Issue
- 1
- Pages
- 48-61
- ISSN
- 1043-2760 (ISSN-L)
- PMC
- PMC8627828
- OpenAlex
- W3109969586
- Cited by
- 225
- References
- 134
- Citations by year
- 2026: 30 · 2025: 59 · 2024: 54 · 2023: 44 · 2022: 21 · 2021: 17
- FWCI
- 3.48
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Trends in Endocrinology and Metabolism (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Socio-Environmental Systems Modeling (acceptedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases
- National Institute of General Medical Sciences
- Topics
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipid metabolism and disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
- Health Sciences › Medicine › Surgery › Lymphatic Disorders and Treatments
- Keywords
- lipoprotein lipase, lipolysis, lipid metabolism, chylomicrons, VLDL, angiopoietin-like proteins, GPIHBP1, LMF1, SEL1L, lipoprotein metabolism
- MeSH terms
- Animals, Endoplasmic Reticulum, Humans, Hyperlipidemias, Lipoprotein Lipase, Triglycerides, Receptors, Lipoprotein
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