Evidence map›Paper›PMID 32487544›Full record

ArticleJournal of lipid research2020

Angiopoietin-like protein 8 differentially regulates ANGPTL3 and ANGPTL4 during postprandial partitioning of fatty acids.

Yan Q Chen, Thomas G Pottanat, Robert W Siegel, Mariam Ehsani, Yue-Wei Qian, Eugene Y Zhen, Ajit Regmi, William C Roell, Haihong Guo, M Jane Luo and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
13.2field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

89 citing papers in PubMed, 144 citations in OpenAlex.

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  10. A neutralizing APOA5 monoclonal antibody reduces amounts of lipoprotein lipase in capillaries and triggers hypertriglyceridemia.Proceedings of the National Academy of Sciences of the United States of America · 2026
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29 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors at 2 institutions in 2 countries.

Yan Q ChenLilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN.
Thomas G PottanatLilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN.
Robert W SiegelLilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN.
Mariam EhsaniLilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN.
Yue-Wei QianLilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN.
Eugene Y ZhenLilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN.
Ajit RegmiLilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN.
William C RoellLilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN.
Haihong GuoLilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN.
M Jane LuoLilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN.
Ruth E GimenoLilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN.
Ferdinand Van't HooftDivision of Cardiovascular Medicine, Department of Medicine Solna, Karolinska Institutet Karolinska University Hospital Solna, Stockholm, Sweden.
Robert J KonradLilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN konrad_robert@lilly.com.
Eli Lilly (United States) · USKarolinska University Hospital · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Angiopoietin-like protein (ANGPTL)8 has been implicated in metabolic syndrome and reported to regulate adipose FA uptake through unknown mechanisms. Here, we studied how complex formation of ANGPTL8 with ANGPTL3 or ANGPTL4 varies with feeding to regulate LPL. In human serum, ANGPTL3/8 and ANGPTL4/8 complexes both increased postprandially, correlated negatively with HDL, and correlated positively with all other metabolic syndrome markers. ANGPTL3/8 also correlated positively with LDL-C and blocked LPL-facilitated hepatocyte VLDL-C uptake. LPL-inhibitory activity of ANGPTL3/8 was >100-fold more potent than that of ANGPTL3, and LPL-inhibitory activity of ANGPTL4/8 was >100-fold less potent than that of ANGPTL4. Quantitative analyses of inhibitory activities and competition experiments among the complexes suggested a model in which localized ANGPTL4/8 blocks the LPL-inhibitory activity of both circulating ANGPTL3/8 and localized ANGPTL4, allowing lipid sequestration into fat rather than muscle during the fed state. Supporting this model, insulin increased ANGPTL3/8 secretion from hepatocytes and ANGPTL4/8 secretion from adipocytes. These results suggest that low ANGPTL8 levels during fasting enable ANGPTL4-mediated LPL inhibition in fat tissue to minimize adipose FA uptake. During feeding, increased ANGPTL8 increases ANGPTL3 inhibition of LPL in muscle via circulating ANGPTL3/8, while decreasing ANGPTL4 inhibition of LPL in adipose tissue through localized ANGPTL4/8, thereby increasing FA uptake into adipose tissue. Excessive caloric intake may shift this system toward the latter conditions, possibly predisposing to metabolic syndrome.

Indexed as

Postprandial PeriodAngiopoietin-Like Protein 3Angiopoietin-Like Protein 4Angiopoietin-Like Protein 8Angiopoietin-like ProteinsBiomarkersFatty AcidsHumansPeptide HormonesAngiopoietin-Like Protein 3Angiopoietin-Like Protein 4Angiopoietin-Like Protein 8Angiopoietin-like ProteinsANGPTL3 protein, humanANGPTL8 protein, humanBiomarkersFatty AcidsPeptide Hormonesadipose tissueangiopoietin-like protein 3angiopoietin-like protein 4lipid metabolismlipoprotein lipasemetabolic syndromemuscleobesitypostprandial conditiontriglycerides

Identifiers

PMID32487544
PMCPMC7397750
OpenAlexW3032087370

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.