Evidence map›Paper›PMID 21176092›Full record

ArticleAging cell2011

A nutrient-sensitive interaction between Sirt1 and HNF-1α regulates Crp expression.

Andrew A Grimm, Cynthia S Brace, Ting Wang, Gary D Stormo, Shin-ichiro Imai

Open access · bronzeAbstract read
In one paragraph

Article in Aging cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.7field-weighted citation impact, top 27% 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

13 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. HNF1A Mutations and Beta Cell Dysfunction in Diabetes.International journal of molecular sciences · 2022
    Review
  3. Article
  4. Article
  5. Article
  6. Association study of HNF1A in women with polycystic ovary syndrome.Journal of assisted reproduction and genetics · 2017
    Article
  7. Article
  8. Sirtuins in epigenetic regulation.Chemical reviews · 2015
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
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 1 institution in 1 country.

Andrew A GrimmDepartment of Developmental Biology Department of Genetics, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.
Cynthia S Brace
Ting Wang
Gary D Stormo
Shin-ichiro Imai
Washington University in St. Louis · US

Funding

Washington University Nutrition Obesity Research CenterP30DK056341 · NIDDK · WASHINGTON UNIVERSITY · PI Jonathan R Brestoff · 1999 to 2026
$30.2M
DNA PATTERN IDENTIFICATION AND ANALYSISR01HG000249 · NHGRI · WASHINGTON UNIVERSITY · PI STORMO, GARY D · 1990 to 2017
$5.6M
MAMMALIAN SIR2 FUNCTION IN PANCREATIC BETA CELLSR01AG024150 · NIA · WASHINGTON UNIVERSITY · PI IMAI, SHIN-ICHIRO · 2004 to 2012
$2.7M
NHGRI NIH HHS HG00249NHGRI NIH HHS R01 HG000249NIA NIH HHS AG024150NIA NIH HHS R01 AG024150NIDDK NIH HHS P30 DK056341
6 · The paper itself

Abstract

Silent information regulator 2 (Sir2) orthologs are an evolutionarily conserved family of NAD-dependent protein deacetylases that regulate aging and longevity in model organisms. The mammalian Sir2 ortholog Sirt1 regulates metabolic and stress responses through the deacetylation of many transcriptional regulatory factors. To elucidate the mechanism by which Sirt1 controls gene expression in response to nutrient availability, we devised a bioinformatic screen combining gene expression analysis with phylogenetic footprinting to identify transcription factors as new candidate partners of Sirt1. One candidate target was HNF-1α, a homeodomain transcription factor that regulates pancreatic β-cell and hepatocyte functions and is commonly mutated in patients with maturity-onset diabetes of the young (MODY). Interestingly, Sirt1 physically interacts with HNF-1αin vitro but does so in vivo only in nutrient-restricting conditions. This interaction requires 12-24 h of nutrient restriction and is dependent on protein synthesis. Both nutrient restriction and Sirt1 suppress HNF-1α transcriptional activity and the expression of one of its target genes, C-reactive protein (Crp), in mouse primary hepatocytes. Pharmacological inhibition of Sirt1 blocks the suppression of Crp by nutrient restriction. Similarly, Crp expression is also suppressed in fasted and diet-restricted liver. Furthermore, Sirt1 and HNF-1α co-localize on two HNF-1α binding sites on the Crp promoter, leading to decreased acetylation of lysine 16 of histone H4 at these sites only in response to nutrient restriction. These findings reveal a novel nutrient-dependent interaction between Sirt1 and HNF-1α and provide important insight into the molecular mechanism by which Sirt1 mediates the anti-aging effects of diet restriction.

Indexed as

Nutritional StatusAnimalsBase SequenceBinding SitesComputational BiologyC-Reactive ProteinDietFastingGene ExpressionHepatocyte Nuclear Factor 1-alphaHumansMaleMiceMolecular Sequence DataPromoter Regions, GeneticRecombinant Fusion ProteinsC-Reactive ProteinHepatocyte Nuclear Factor 1-alphaRecombinant Fusion ProteinsSirt1 protein, mouseSirtuin 1Transcription Factors

Identifiers

PMID21176092
PMCPMC3079228
OpenAlexW1595347143

What OpenQuestion holds

Textmetadata
LicenceTDM
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.