Evidence map›Paper›PMID 32640594›Full record

ArticleBiomolecules2020

Aldose Reductase Differential Inhibitors in Green Tea.

Francesco Balestri, Giulio Poli, Carlotta Pineschi, Roberta Moschini, Mario Cappiello, Umberto Mura, Tiziano Tuccinardi, Antonella Del Corso

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2020. 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
1.2field-weighted citation impact, top 24% 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, 19 citations in OpenAlex.

  1. Review
  2. ExploringMolecules (Basel, Switzerland) · 2026
    Article
  3. Advances in pharmacological and pharmaceutical sciences · 2026
    Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
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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

8 authors at 1 institution in 1 country.

Francesco BalestriBiochemistry Unit, Department of Biology, University of Pisa, via S. Zeno, 51, 56123 Pisa, Italy.
Giulio PoliDepartment of Pharmacy, University of Pisa, via Bonanno 6, 56126 Pisa, Italy.
Carlotta PineschiBiochemistry Unit, Department of Biology, University of Pisa, via S. Zeno, 51, 56123 Pisa, Italy.
Roberta MoschiniBiochemistry Unit, Department of Biology, University of Pisa, via S. Zeno, 51, 56123 Pisa, Italy.
Mario CappielloBiochemistry Unit, Department of Biology, University of Pisa, via S. Zeno, 51, 56123 Pisa, Italy.
Umberto MuraBiochemistry Unit, Department of Biology, University of Pisa, via S. Zeno, 51, 56123 Pisa, Italy.
Tiziano TuccinardiDepartment of Pharmacy, University of Pisa, via Bonanno 6, 56126 Pisa, Italy.
Antonella Del CorsoBiochemistry Unit, Department of Biology, University of Pisa, via S. Zeno, 51, 56123 Pisa, Italy.
University of Pisa · IT

Funding

Aboca S.p.A. Società Agricola Research Contract with Department of Biology
6 · The paper itself

Abstract

Aldose reductase (AKR1B1), the first enzyme in the polyol pathway, is likely involved in the onset of diabetic complications. Differential inhibition of AKR1B1 has been proposed to counteract the damaging effects linked to the activity of the enzyme while preserving its detoxifying ability. Here, we show that epigallocatechin gallate (EGCG), one of the most representative catechins present in green tea, acts as a differential inhibitor of human recombinant AKR1B1. A kinetic analysis of EGCG, and of its components, gallic acid (GA) and epigallocatechin (EGC) as inhibitors of the reduction of L-idose, 4-hydroxy2,3-nonenal (HNE), and 3-glutathionyl l-4-dihydroxynonanal (GSHNE) revealed for the compounds a different model of inhibition toward the different substrates. While EGCG preferentially inhibited L-idose and GSHNE reduction with respect to HNE, gallic acid, which was still active in inhibiting the reduction of the sugar, was less active in inhibiting HNE and GSHNE reduction. EGC was found to be less efficient as an inhibitor of AKR1B1 and devoid of any differential inhibitory action. A computational study defined different interactive modes for the three substrates on the AKR1B1 active site and suggested a rationale for the observed differential inhibition. A chromatographic fractionation of an alcoholic green tea extract revealed that, besides EGCG and GA, other components may exhibit the differential inhibition of AKR1B1.

Indexed as

Aldehyde ReductaseCatalytic DomainCatechinEnzyme InhibitorsGallic AcidGlutathioneHexosesHumansModels, MolecularMolecular Docking SimulationMolecular Dynamics SimulationPlant ExtractsTea3-glutathionyl-4-hydroxynonanalAKR1B1 protein, humanAldehyde ReductaseCatechinEnzyme Inhibitorsepigallocatechin gallateGallic AcidgallocatecholGlutathioneHexosesidosePlant ExtractsTeaaldose reductaseARDIsdiabetic complicationsdifferential inhibitorsepigallocatechin gallategallic acidgreen tea

Identifiers

PMID32640594
PMCPMC7407822
OpenAlexW3039473905

What Socratic holds

Textmetadata
LicenceCC BY
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.