Evidence map›Paper›PMID 33955199›Full record

ArticleJournal of diabetes investigation2021

SIRT7 regulates lipogenesis in adipocytes through deacetylation of PPARγ2.

Fatema Akter, Tomonori Tsuyama, Tatsuya Yoshizawa, Shihab U Sobuz, Kazuya Yamagata

Open access · goldAbstract read
In one paragraph

Article in Journal of diabetes investigation, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

21 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Review
  3. The Sirtuin Network: Linking NADDiabetes/metabolism research and reviews · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Review
  16. Molecular and Cellular Mechanisms of Osteoporosis.International journal of molecular sciences · 2023
    Review
  17. Review
  18. Review
  19. Article
  20. SIRT7 in the aging process.Cellular and molecular life sciences : CMLS · 2022
    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

5 authors at 2 institutions in 1 country.

Fatema AkterDepartment of Medical Biochemistry, Faculty of Life Sciences, Kumamoto University, Kumamoto, Japan.
Tomonori TsuyamaCenter for Metabolic Regulation of Healthy Aging (CMHA), Faculty of Life Sciences, Kumamoto University, Kumamoto, Japan.
Tatsuya YoshizawaDepartment of Medical Biochemistry, Faculty of Life Sciences, Kumamoto University, Kumamoto, Japan.
Shihab U SobuzDepartment of Medical Biochemistry, Faculty of Life Sciences, Kumamoto University, Kumamoto, Japan.
Kazuya YamagataDepartment of Medical Biochemistry, Faculty of Life Sciences, Kumamoto University, Kumamoto, Japan.ORCID https://orcid.org/0000-0001-7564-7579
Kumamoto University · JPKumamoto Health Science University · JP

Funding

a Grant-in-Aid for Challenging Research (Exploratory) 19K22639a Grant-in-Aid for Scientific Research (B) 19H03711a Grant-in-Aid for Scientific Research (B) 20H04107MEXT Scientific Research on Innovative Areas "LipoQuality" 18H04676Naito FoundationTakeda Science Foundationthe Japan Agency for Medical Research and Development under Grant Number JP20gm5010002
6 · The paper itself

Abstract

AIMS/

introductionPeroxisome proliferator-activated receptor (PPAR)-γ2 is a transcription factor crucial for regulating adipogenesis and glucose/lipid metabolism, and synthetic PPARγ ligands, such as thiazolidinediones, are effective oral medication for type 2 diabetes. Sirtuin 7 (SIRT7), a nicotinamide adenine dinucleotide-dependent deacetylase, also controls metabolism. However, it is not known whether SIRT7 regulates the function of PPARγ2 by its deacetylation. MATERIALS AND

methodsPhysical interaction between SIRT7 and PPARγ2, the effect of SIRT7 on PPARγ2 acetylation, and the deacetylation residue targeted by SIRT7 were investigated. The effects of PPARγ2 K382 acetylation on lipid accumulation, gene expression in C3H10T1/2 cell-derived adipocytes, and ligand-dependent transactivation activity were also evaluated.

resultsWe demonstrated that SIRT7 binds to PPARγ2 and deacetylates PPARγ2 at K382. C3H10T1/2-derived adipocytes expressing PPARγ2

conclusionOur findings indicate that SIRT7-dependent PPARγ2 deacetylation at K382 controls lipogenesis in adipocytes.

Indexed as

LipogenesisAcetylationAdipocytesHEK293 CellsHumansPPAR gammaSirtuinsPPAR gammaSIRT7 protein, humanSirtuinsacetylationPPARγSIRT7

Identifiers

PMID33955199
PMCPMC8504911
OpenAlexW3157431409

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.