Cited by 221Lipid metabolism and disordersLipoproteins and Cardiovascular HealthLipid metabolism and biosynthesis

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Angiopoietin-like 3 in lipoprotein metabolism

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Kersten, Sander·2017·Nature Reviews Endocrinology

DOI 10.1038/nrendo.2017.119

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Abstract

Triglycerides and cholesterol circulate in the bloodstream as part of various lipoprotein particles. Three members of the angiopoietin-like (ANGPTL) protein family - ANGPTL3, ANGPTL4 and ANGPTL8 - have emerged as important regulators of plasma lipoprotein levels by inhibiting the enzyme lipoprotein lipase. Here, I review the role of ANGPTL3 in lipoprotein metabolism. In contrast to ANGPTL4 and ANGPTL8, ANGPTL3 is exclusively produced in the liver and can therefore be classified as a true hepatokine. ANGPTL3 cooperates with ANGPTL8 to inhibit lipoprotein lipase and is mostly active after feeding, whereas ANGPTL4 is mostly active after fasting. Inactivation of ANGPTL3 in mice reduces plasma triglyceride and free fatty acid levels and suppresses atherosclerosis. In humans, homozygous loss-of-function mutations in ANGPTL3 lead to low plasma levels of low-density lipoproteins, high-density lipoproteins and triglycerides, a condition referred to as familial combined hypolipidaemia. Heterozygous carriers of loss-of-function mutations in ANGPTL3 have a lower risk of coronary artery disease than non-carriers. At present, researchers are investigating antisense oligonucleotide and monoclonal antibody-based inactivation of ANGPTL3 in human clinical trials for the therapeutic management of dyslipidaemia and atherosclerosis. Thus, ANGPTL3 is an important liver-derived regulator of lipoprotein metabolism that holds considerable promise as a target for atherosclerosis.

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Additional file 1 of ANGPTL3 impacts proteinuria and hyperlipidemia in primary nephrotic syndrome
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Additional file 2 of Familial hypertriglyceridemia: an entity with distinguishable features from other causes of hypertriglyceridemia
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Authors: Kersten, S.
Affiliations: Wageningen University & Research (NL)
Corresponding author: Kersten, Sander
ORCID: Kersten, Sander
Venue: Nature Reviews Endocrinology
Publisher: Springer Science and Business Media LLC
Published: 2017-10-06
Volume: 13
Issue: 12
Pages: 731-739
ISSN: 1759-5029 (ISSN-L)
1759-5037
DOI: 10.1038/nrendo.2017.119
OpenAlex: W2761312904
Semantic Scholar: de449b0f2ed915d896023302b106994d388fefb6
Cited by: 220
References: 80
Citations by year: 2026: 23 · 2025: 30 · 2024: 20 · 2023: 22 · 2022: 27 · 2021: 47 · 2020: 25 · 2019: 13 · 2018: 12 · 2017: 1
FWCI: 1.98
Type: journal article
Language: en
Open access: green
research.wur.nl
Licence: www.springer.com/tdm (tdm)
Locations: Nature Reviews Endocrinology (publishedVersion)
PubMed (publishedVersion)
Socio-Environmental Systems Modeling (acceptedVersion)
Data Archiving and Networked Services (DANS) (submittedVersion)
Funders: Fondation Leducq
Topics: Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipid metabolism and disorders
Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipoproteins and Cardiovascular Health
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
Keywords: ANGPTL3, angiopoietin-like proteins, lipoprotein lipase inhibition, lipoprotein metabolism, hepatokines, atherosclerosis, loss-of-function mutations, coronary artery disease, dyslipidemia, antisense oligonucleotides, monoclonal antibodies, triglycerides, free fatty acids, ANGPTL4, ANGPTL8
MeSH terms: Angiopoietin-like Proteins, Angiopoietin-Like Protein 3, Animals, Antibodies, Monoclonal, Fasting, Fatty Acids, Nonesterified, Food, Humans, Lipoprotein Lipase, Lipoproteins, Liver, Mutation, Triglycerides, Oligonucleotides, Antisense, Dyslipidemias, Atherosclerosis, Mice

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