Evidence map›Paper›PMID 28487468›Full record

ArticleThe Journal of biological chemistry2017

Epigallocatechin gallate has pleiotropic effects on transmembrane signaling by altering the embedding of transmembrane domains.

Feng Ye, Chansik Yang, Jiyoon Kim, Christopher J MacNevin, Klaus M Hahn, Dongeun Park, Mark H Ginsberg, Chungho Kim

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

9 citing papers in PubMed, 13 citations in OpenAlex.

  1. Selective Inhibition of Integrin β3 Topology Provides a Safer Antithrombotic Strategy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. The Intrinsic Virtues of EGCG, anMolecules (Basel, Switzerland) · 2020
    Review
  8. Article
  9. 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

8 authors at 4 institutions in 2 countries.

Feng YeFrom the Department of Medicine, University of California San Diego School of Medicine, La Jolla, California 92093.
Chansik Yangthe Department of Life Sciences, Korea University, Seoul 136-701, Republic of Korea.
Jiyoon Kimthe Department of Life Sciences, Korea University, Seoul 136-701, Republic of Korea.
Christopher J MacNevinthe Department of Pharmacology and Lineberger Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599.
Klaus M Hahnthe Department of Pharmacology and Lineberger Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599.
Dongeun Parkthe School of Biological Sciences, Seoul National University, Seoul 151-747, Republic of Korea, and.
Mark H GinsbergFrom the Department of Medicine, University of California San Diego School of Medicine, La Jolla, California 92093, mhginsberg@ucsd.edu.
Chungho Kimthe Department of Life Sciences, Korea University, Seoul 136-701, Republic of Korea, chungho@korea.ac.kr.
Korea University · KRSeoul National University · KRUniversity of California, San Diego · USUniversity of North Carolina at Chapel Hill · US

Funding

The Interaction of TPO and Integrins in Hematopoiesis CellsP01HL078784 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GINSBERG, MARK HOWARD · 2005 to 2019
$28.3M
INTERACTIVE GRAPHICS FOR MOLECULAR STUDIES &MICROSCOPYP41EB002025 · NIBIB · UNIV OF NORTH CAROLINA CHAPEL HILL · PI SUPERFINE, RICHARD · 2003 to 2019
$16.9M
Somatic mutation(s) and cellular changes in CCM pathogenesisP01NS092521 · NINDS · DUKE UNIVERSITY · PI MARCHUK, DOUGLAS A. · 2015 to 2024
$12.9M
Mechanisms Of Cell Migration On 3D Aligned MatricesR01CA142833 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI FRIEDL, ANDREAS, HAHN, KLAUS M. · 2010 to 2020
$3.4M
Composition and Functions of the Integrin Activation ComplexR01HL117807 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GINSBERG, MARK HOWARD · 2014 to 2017
$1.5M
NCI NIH HHS R01 CA142833NHLBI NIH HHS P01 HL078784NHLBI NIH HHS R01 HL117807NIBIB NIH HHS P41 EB002025NINDS NIH HHS P01 NS092521
6 · The paper itself

Abstract

Epigallocatechin gallate (EGCG) is the principal bioactive ingredient in green tea and has been reported to have many health benefits. EGCG influences multiple signal transduction pathways related to human diseases, including redox, inflammation, cell cycle, and cell adhesion pathways. However, the molecular mechanisms of these varying effects are unclear, limiting further development and utilization of EGCG as a pharmaceutical compound. Here, we examined the effect of EGCG on two representative transmembrane signaling receptors, integrinαIIbβ3 and epidermal growth factor receptor (EGFR). We report that EGCG inhibits talin-induced integrin αIIbβ3 activation, but it activates αIIbβ3 in the absence of talin both in a purified system and in cells. This apparent paradox was explained by the fact that the activation state of αIIbβ3 is tightly regulated by the topology of β3 transmembrane domain (TMD); increases or decreases in TMD embedding can activate integrins. Talin increases the embedding of integrin β3 TMD, resulting in integrin activation, whereas we observed here that EGCG decreases the embedding, thus opposing talin-induced integrin activation. In the absence of talin, EGCG decreases the TMD embedding, which can also disrupt the integrin α-β TMD interaction, leading to integrin activation. EGCG exhibited similar paradoxical behavior in EGFR signaling. EGCG alters the topology of EGFR TMD and activates the receptor in the absence of EGF, but inhibits EGF-induced EGFR activation. Thus, this widely ingested polyphenol exhibits pleiotropic effects on transmembrane signaling by modifying the topology of TMDs.

Indexed as

Models, MolecularSignal TransductionAmino Acid SubstitutionAnimalsAntioxidantsCatechinCHO CellsCricetulusDietary SupplementsDimerizationErbB ReceptorsHumansIntegrin alpha2Integrin beta3LigandsLipid BilayersAntioxidantsCatechinEGFR protein, humanepigallocatechin gallateErbB ReceptorsIntegrin alpha2Integrin beta3ITGA2B protein, humanITGB3 protein, humanLigandsLipid BilayersPeptide FragmentsPlatelet Glycoprotein GPIIb-IIIa ComplexRecombinant Fusion ProteinsTalinepidermal growth factor receptor (EGFR)integrinpolyphenoltalintransmembrane domain

Identifiers

PMID28487468
PMCPMC5473239
OpenAlexW2612411634

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.