The DOI matches its Crossref record; 80 of the 80 references it cites were found in a registry or an index.
Angiopoietin-like 3 in lipoprotein metabolism
Open accessAbstract
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“which codes for a glycoprotein with roles in angiogenesis, tissue remodeling, inflammation, and inhibition of lipoprotein lipase (LPL) catalytic activity [93–95]”
From Sterol and lipid analyses identifies hypolipidemia and apolipoprotein disorders in autism associated with adaptive functioning deficits (2021) · cites this paper as [95]
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
2 retracted
RETRACTED: Betatrophin: A Hormone that Controls Pancreatic β Cell Proliferation
Yi, P., Park, J.-S., & Melton, D. A. (2013) · Cell · doi:10.1016/j.cell.2013.04.008 · Cited by 449
RetractedRetraction Notice to: Betatrophin: A Hormone that Controls Pancreatic β Cell Proliferation
Peng, Y., Park, J.-S., & Melton, D. A. (2016) · Cell · doi:10.1016/j.cell.2016.12.017 · Cited by 49
RetractedBiological, clinical and population relevance of 95 loci for blood lipids
Teslovich, T. M., Musunuru, K., Smith, A. V., Edmondson, A. C., Stylianou, I. M., Koseki, M., Pirruccello, J. P., Ripatti, S., Chasman, D. I., Willer, C. J., et al. (2010) · Nature · doi:10.1038/nature09270 · Cited by 3,487
Newly identified loci that influence lipid concentrations and risk of coronary artery disease
Willer, C. J., Sanna, S., Jackson, A. U., Scuteri, A., Bonnycastle, L. L., Clarke, R., Heath, S. C., Timpson, N. J., Najjar, S. S., Stringham, H. M., et al. (2008) · Nature Genetics · doi:10.1038/ng.76 · Cited by 1,585
Kathiresan, S., Melander, O., Guiducci, C., Surti, A., Burtt, N. P., Rieder, M. J., Cooper, G. M., Roos, C., Voight, B. F., Havulinna, A. S., et al. (2008) · Nature Genetics · doi:10.1038/ng.75 · Cited by 1,386
Genetic and Pharmacologic Inactivation of ANGPTL3 and Cardiovascular Disease
Dewey, F. E., Gusarova, V., Dunbar, R. L., O’Dushlaine, C., Schurmann, C., Gottesman, O., McCarthy, S., Van Hout, C. V., Bruse, S., Dansky, H. M., et al. (2017) · New England Journal of Medicine · doi:10.1056/nejmoa1612790 · Cited by 885
Exome Sequencing, ANGPTL3 Mutations, and Familial Combined Hypolipidemia
Musunuru, K., Pirruccello, J. P., Do, R., Peloso, G. M., Guiducci, C., Sougnez, C., Garimella, K. V., Fisher, S., Abreu, J., Barry, A. J., et al. (2010) · New England Journal of Medicine · doi:10.1056/nejmoa1002926 · Cited by 754
Physiological regulation of lipoprotein lipase
Kersten, S. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2014.03.013 · Cited by 573
Self-citationCardiovascular and Metabolic Effects of ANGPTL3 Antisense Oligonucleotides
Graham, M. J., Lee, R. G., Brandt, T. A., Tai, L.-J., Fu, W., Peralta, R., Yu, R., Hurh, E., Paz, E., McEvoy, B. W., et al. (2017) · New England Journal of Medicine · doi:10.1056/nejmoa1701329 · Cited by 573
Kersten, S., Mandard, S., Tan, N. S., Escher, P., Metzger, D., Chambon, P., Gonzalez, F. J., Desvergne, B., & Wahli, W. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004029200 · Cited by 489
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Items 201–221 of 221
Cruz-Bautista, I., Huerta‐Chagoya, A., Moreno-Macías, H., Rodríguez-Guillén, R., Ordóñez-Sánchez, M. L., Segura-Kato, Y., Mehta, R., Almeda-Valdés, P., Gómez-Munguía, L., Chávez, X. R.-D., et al. (2021) · Figshare · doi:10.6084/m9.figshare.14037370
Sun, T., Zhan, W., Wei, L., Xu, Z., Fan, L., Zhuo, Y., Wang, C., & Zhang, J. (2021) · Figshare · doi:10.6084/m9.figshare.16944500
Foss-freitas, M. C., Akıncı, B., Neidert, A., Bartlett, V. J., Hurh, E., Karwatowska‐Prokopczuk, E., & Oral, E. A. (2021) · Figshare · doi:10.6084/m9.figshare.17127352
Wong Chong, E., Joncas, F.-H., Douville, P., Bachvarov, D. R., Diorio, C., Calon, F., Bergeron, A.-C., Blais, J., Leung, S. O., Seidah, N. G., et al. (2024) · Figshare · doi:10.6084/m9.figshare.25302989
Saalom King, J., Seena, T. X., Rojan, P. M., Kurian², E., Sumena, K. B., & Bindu, K. A. (2026) · SSRN Electronic Journal · doi:10.2139/ssrn.6145548
Wulff, A. B., Varbo, A., Nordestgaard, A. G., & Nordestgaard, B. G. (2026) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2026.2639678 · Cited by 2
Zhang, X., Han, Y., Zheng, L., He, X., Pu, Y., Wei, L., Wang, Y., & Xian, X. (2026) · Lipids in Health and Disease · doi:10.1186/s12944-026-02916-3
Abêta- et hypobêtalipoprotéinémies : diagnostic et prise en charge
Cariou, B. (2026) · Médecine des Maladies Métaboliques · doi:10.1016/j.mmm.2026.03.002
Xu, S., Wang, L., Dou, Z., Hu, X., Cao, Z., Zhang, Y., Jiang, X., Wu, T., Li, Z., Nan, Y., et al. (2026) · Inflammation Research · doi:10.1007/s00011-026-02218-5
Mabunda, C., Amadi-Echendu, A. P., & Ntoyanto-Tyatyantsi, N. (2026) · Journal of Transport and Supply Chain Management · doi:10.4102/jtscm.v20i0.1299 · Cited by 1
Long, L., Zhu, B. S., & Lv, T. (2026) · Journal of Cardiothoracic Surgery · doi:10.1186/s13019-026-04107-8
Deng, H., Shen, P., Li, G., Yin, Z., Zhou, L., Bai, Z., Zhang, P., Zhou, Y., Wang, N., Gao, Y., et al. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-026-02918-9
Angptl5 restricts primitive hematopoiesis by promoting retinoic acid signaling in zebrafish
Mo, J., Zhuo, D., Huang, Y., Cheng, T., Dong, Y., Dong, Y., Li, Y.-F., Jin, Z.-X., Liu, X., Zhao, G.-Q., et al. (2026) · PLoS Biology · doi:10.1371/journal.pbio.3003858
Jahromi, M., Al-Otaibi, T., Othman, N. F., Mahmoud, T. S. H., Nair, P., Halim, M. A., Jahrami, K., & Gheith, O. A. A. (2026) · Experimental and Clinical Transplantation · doi:10.6002/ect.mesot2025.p191
Blewusi, S., Afedzi, A. E. K., Poolsawat, T., Uan‐On, T., & Wanikorn, B. (2026) · Food Reviews International · doi:10.1080/87559129.2026.2704693
Adipokine in Metabolic Liver Disease: Adipo–Brain–Liver Cross talk
苏喻乐, Yang, Y., Sun, W., Yu, Z., Wang, Y., 刘世新, Chen, Z., Li, Y., Yang, X., Liu, J., et al. (2026) · International Journal of Endocrinology · doi:10.1155/ije/9009628
Pillai, S. S., Brar, P. C., & Ashraf, A. P. (2026) · Current Atherosclerosis Reports · doi:10.1007/s11883-026-01457-5
Yang, G., Zhang, D. Y., Fischman, C. J., Cuchel, M., Suszták, K., & Rader, D. J. (2026) · American Journal of Kidney Diseases · doi:10.1053/j.ajkd.2026.06.015
Hypertriglyceridemia: Causes, Consequences, Diagnosis, and Management
Qi, S., Chen, W., Chen, K., Yang, S., Wang, S., Ni, T., Xu, D., Mao, E., Chen, E., & Chen, Y. (2026) · MedComm · doi:10.1002/mco2.70956
A Nutrient-Dependent ANGPTL3–PCSK9-Containing Complex in HepG2 Cells and Human Plasma
Bini, S., Pecce, V., Grimaldos, A. P., Costanzo, A. D., Minicocci, I., Covino, S., Tramontano, D., Piconese, S., D’Erasmo, L., & Arca, M. (2026) · Biomolecules · doi:10.3390/biom16101531
Bolgova, O., Shypilova, I., Yaqinuddin, A., Omotayo, J., Stanek, A., Islam, Z. H., & Mavrych, V. (2026) · Current Issues in Molecular Biology · doi:10.3390/cimb48111122
Metadata
- Authors
- Kersten, S.
- Affiliations
- Wageningen University & Research (NL)
- Corresponding author
- Kersten, Sander
- ORCID
- Kersten, Sander
- Venue
- Nature Reviews Endocrinology
- Published
- 2017-10-06
- Volume
- 13
- Issue
- 12
- Pages
- 731-739
- ISSN
- 1759-5029 (ISSN-L)
- 1759-5037
- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review