Evidence map›Paper›PMID 26580610›Full record

ArticleInternational journal of molecular sciences2015

Three Peptides from Soy Glycinin Modulate Glucose Metabolism in Human Hepatic HepG2 Cells.

Carmen Lammi, Chiara Zanoni, Anna Arnoldi

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.2field-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

26 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Carob (Foods (Basel, Switzerland) · 2024
    Article
  6. Review
  7. Review
  8. Review
  9. Review
  10. Nutrients · 2022
    Article
  11. Article
  12. Characterisation of Endogenous Peptides Present in Virgin Olive Oil.International journal of molecular sciences · 2022
    Article
  13. Article
  14. Synthesis and evaluation ofIranian journal of basic medical sciences · 2021
    Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. 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

3 authors at 1 institution in 1 country.

Carmen LammiDepartment of Pharmaceutical Sciences, University of Milan, Mangiagalli Street 25, 20133 Milan, Italy. carmen.lammi@unimi.it.
Chiara ZanoniDepartment of Pharmaceutical Sciences, University of Milan, Mangiagalli Street 25, 20133 Milan, Italy. chiara.zanoni1@unimi.it.
Anna ArnoldiDepartment of Pharmaceutical Sciences, University of Milan, Mangiagalli Street 25, 20133 Milan, Italy. anna.arnoldi@unimi.it.
University of Milan · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ile-Ala-Val-Pro-Gly-Glu-Val-Ala (IAVPGEVA), Ile-Ala-Val-Pro-Thr-Gly-Val-Ala (IAVPTGVA) and Leu-Pro-Tyr-Pro (LPYP), three peptides deriving from soy glycinin hydrolysis, are known to regulate cholesterol metabolism in human hepatic HepG2 cells. We have recently demonstrated that the mechanism of action involves the activation of adenosine monophosphate-activated protein kinase (AMPK). This fact suggested a potential activity of the same peptides on glucose metabolism that prompted us to also investigate this aspect in the same cells. After treatment with IAVPGEVA, IAVPTGVA and LPYP, HepG2 cells were analyzed using a combination of molecular techniques, including western blot analysis, glucose uptake experiments and fluorescence microscopy evaluation. The results showed that these peptides are indeed able to enhance the capacity of HepG2 cells to uptake glucose, via glucose transporter 1 GLUT1 and glucose transporter 4 GLUT4 activation, through the stimulation of protein kinase B Akt and adenosine monophosphate-activated protein kinase AMPK pathways, both involved in glucose metabolism.

Indexed as

Carbohydrate MetabolismGlobulinsGlucoseGlucose Transport Proteins, FacilitativeGlycogen Synthase Kinase 3Hep G2 CellsHumansModels, BiologicalPeptide FragmentsProto-Oncogene Proteins c-aktSignal TransductionSoybean ProteinsGlobulinsGlucoseGlucose Transport Proteins, FacilitativeglycininGlycogen Synthase Kinase 3Peptide FragmentsProto-Oncogene Proteins c-aktSoybean Proteinsbioactive peptidesfunctional foodsglucose uptakeHepG2 cell lineplant proteins

Identifiers

PMID26580610
PMCPMC4661887
OpenAlexW2177186363

What OpenQuestion holds

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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.