Evidence map›Paper›PMID 32999434›Full record

ArticleScientific reports2020

GALNT2 regulates ANGPTL3 cleavage in cells and in vivo of mice.

Xuedan Li, Yiliang Zhang, Minzhu Zhang, Yan Wang

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.1field-weighted citation impact, top 11% 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

16 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Article
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  9. Review
  10. Genes · 2022
    Article
  11. Article
  12. Role of GALNT2 on Insulin Sensitivity, Lipid Metabolism and Fat Homeostasis.International journal of molecular sciences · 2022
    Review
  13. Review
  14. PolypeptideMolecules (Basel, Switzerland) · 2021
    Review
  15. Review
  16. Review
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

4 authors at 1 institution in 1 country.

Xuedan LiHubei Key Laboratory of Cell Homeostasis, Department of Biochemistry, College of Life Sciences, Wuhan University, Wuhan, 430072, People's Republic of China.
Yiliang ZhangHubei Key Laboratory of Cell Homeostasis, Department of Biochemistry, College of Life Sciences, Wuhan University, Wuhan, 430072, People's Republic of China.
Minzhu ZhangHubei Key Laboratory of Cell Homeostasis, Department of Biochemistry, College of Life Sciences, Wuhan University, Wuhan, 430072, People's Republic of China.
Yan WangHubei Key Laboratory of Cell Homeostasis, Department of Biochemistry, College of Life Sciences, Wuhan University, Wuhan, 430072, People's Republic of China. Wang.y@whu.edu.cn.
Wuhan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Angiopoietin-like protein 3 (ANGPTL3) is an important inhibitor of lipoprotein lipase and endothelial lipase that plays critical roles in lipoprotein metabolism. It specifically expresses in the liver and undergoes proprotein convertase-mediated cleavage during secretion, which generates an N-terminal coiled-coil domain and C-terminal fibrinogen-like domain that has been considered as the activation step for its function. Previous studies have reported that the polypeptide GalNAc-transferase GALNT2 mediates the O-glycosylation of the ANGPTL3 near the cleavage site, which inhibits the proprotein convertase (PC)-mediated cleavage in vitro and in cultured cells. However, loss-of-function mutation for GALNT2 has no effect on ANGPTL3 cleavage in human. Thus whether GALNT2 regulates the cleavage of ANGPTL3 in vivo is unclear. In present study, we systematically characterized the cleavage of Angptl3 in cultured cells and in vivo of mice. We found that endogenous Angptl3 is cleaved in primary hepatocytes and in vivo of mice, and this cleavage can be blocked by Galnt2 overexpression or PC inhibition. Moreover, suppressing galnt2 expression increases the cleavage of Angptl3 in mice dramatically. Thus, our results support the conclusion that Galnt2 is a key endogenous regulator for Angptl3 cleavage both in vitro and in vivo.

Indexed as

Angiopoietin-Like Protein 3Angiopoietin-like ProteinsAnimalsGlycosylationHepatocytesLipoprotein LipaseLiverMiceN-AcetylgalactosaminyltransferasesPolypeptide N-acetylgalactosaminyltransferaseProprotein ConvertasesAngiopoietin-Like Protein 3Angiopoietin-like ProteinsAngptl3 protein, mouseLipoprotein LipaseN-AcetylgalactosaminyltransferasesPolypeptide N-acetylgalactosaminyltransferaseProprotein Convertases

Identifiers

PMID32999434
PMCPMC7527996
OpenAlexW3089741196

What OpenQuestion holds

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Registered trials

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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.