Evidence map›Paper›PMID 21980057›Full record

ArticleJournal of lipid research2011

The polypyrimidine tract binding protein regulates desaturase alternative splicing and PUFA composition.

Holly T Reardon, Woo Jung Park, Jimmy Zhang, Peter Lawrence, Kumar S D Kothapalli, J Thomas Brenna

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

  1. Alternative Splicing Regulation in Metabolic Disorders.Obesity reviews : an official journal of the International Association for the Study of Obesity · 2025
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Fads3 modulates docosahexaenoic acid in liver and brain.Prostaglandins, leukotrienes, and essential fatty acids · 2017
    Article
  9. Review
  10. Desaturase and elongase-limiting endogenous long-chain polyunsaturated fatty acid biosynthesis.Current opinion in clinical nutrition and metabolic care · 2016
    Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. 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

6 authors at 1 institution in 1 country.

Holly T ReardonDivision of Nutritional Sciences, Cornell University, Ithaca, NY 14853.
Woo Jung ParkDivision of Nutritional Sciences, Cornell University, Ithaca, NY 14853.
Jimmy ZhangDivision of Nutritional Sciences, Cornell University, Ithaca, NY 14853.
Peter LawrenceDivision of Nutritional Sciences, Cornell University, Ithaca, NY 14853.
Kumar S D KothapalliDivision of Nutritional Sciences, Cornell University, Ithaca, NY 14853.
J Thomas BrennaDivision of Nutritional Sciences, Cornell University, Ithaca, NY 14853. Electronic address: jtb4@cornell.edu.
Cornell University · US

Funding

Reproductive Sciences and Genomics Training ProgramT32HD052471 · NICHD · CORNELL UNIVERSITY · PI ROBERSON, MARK S · 2007 to 2016
$2.0M
NICHD NIH HHS T32 HD052471NICHD NIH HHS T32HD052471
6 · The paper itself

Abstract

The Δ6 desaturase, encoded by FADS2, plays a crucial role in omega-3 and omega-6 fatty acid synthesis. These fatty acids are essential components of the central nervous system, and they act as precursors for eicosanoid signaling molecules and as direct modulators of gene expression. The polypyrimidine tract binding protein (PTB or hnRNP I) is a splicing factor that regulates alternative pre-mRNA splicing. Here, PTB is shown to bind an exonic splicing silencer element and repress alternative splicing of FADS2 into FADS2 AT1. PTB and FADS2AT1 were inversely correlated in neonatal baboon tissues, implicating PTB as a major regulator of tissue-specific FADS2 splicing. In HepG2 cells, PTB knockdown modulated alternative splicing of FADS2, as well as FADS3, a putative desaturase of unknown function. Omega-3 fatty acids decreased by nearly one half relative to omega-6 fatty acids in PTB knockdown cells compared with controls, with a particularly strong decrease in eicosapentaenoic acid (EPA) concentration and its ratio to arachidonic acid (ARA). This is a rare demonstration of a mechanism specifically altering the cellular omega-3 to omega-6 fatty acid ratio without any change in diet/media. These findings reveal a novel role for PTB, regulating availability of membrane components and eicosanoid precursors for cell signaling.

Indexed as

Alternative SplicingAnimalsExonsFatty Acid DesaturasesFatty Acids, Omega-3Fatty Acids, Omega-6Gene Knockdown TechniquesGene SilencingHep G2 CellsHeterogeneous-Nuclear RibonucleoproteinsHumansPapioPolypyrimidine Tract-Binding ProteinProtein BindingRNA, Small InterferingRNA Splice SitesFADS2 protein, humanFADS3 protein, humanFatty Acid DesaturasesFatty Acids, Omega-3Fatty Acids, Omega-6Heterogeneous-Nuclear RibonucleoproteinsPolypyrimidine Tract-Binding ProteinPTBP1 protein, humanRNA, Small InterferingRNA Splice Sites

Identifiers

PMID21980057
PMCPMC3220295
OpenAlexW2169356768

What OpenQuestion holds

Textmetadata
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.