Related Experiment Video

Updated: Jun 20, 2026

Studying TGF-β Signaling and TGF-β-induced Epithelial-to-mesenchymal Transition in Breast Cancer and Normal Cells
06:54

Studying TGF-β Signaling and TGF-β-induced Epithelial-to-mesenchymal Transition in Breast Cancer and Normal Cells

Published on: October 27, 2020

Transforming growth factorbeta(1) transactivates EGFR via an H(2)O(2)-dependent mechanism in squamous carcinoma cell

EunAh Lee1, Jae Youn Yi, Eunkyung Chung

  • 1Department of Genetic Engineering, Musculoskeletal Bioorgan Center, Kyung Hee University, Yongin, Republic of Korea.

Cancer Letters
|September 16, 2009
PubMed

Insights

Transforming growth factor-beta 1 (TGFbeta1) activates the epidermal growth factor receptor (EGFR) through a hydrogen peroxide (H2O2)-dependent pathway. This mechanism involves H2O2 mediating the phosphorylation of EGFR, leading to downstream Erk1/2 activation.

Area of Science:

  • Cellular signaling pathways
  • Molecular biology
  • Cancer research

Background:

  • Transforming growth factor-beta (TGFbeta) is known to transactivate the epidermal growth factor receptor (EGFR).
  • The specific signaling molecules mediating this crosstalk remain largely uncharacterized.

Purpose of the Study:

  • To elucidate the signaling component involved in TGFbeta-induced EGFR transactivation.
  • To determine the role of reactive oxygen species in TGFbeta-mediated EGFR activation.

Main Methods:

  • Treatment of SCC13 and A431 cells with TGFbeta1.
  • Assessment of EGFR phosphorylation using EGF-neutralizing antibodies.
  • Measurement of hydrogen peroxide (H2O2) levels.
  • Inhibition studies using N-acetyl cysteine and catalase inhibitors.
  • Analysis of Erk1/2 activation.

Main Results:

  • TGFbeta1 induced dose-dependent phosphorylation of EGFR in SCC13 and A431 cells, independent of EGF.
  • TGFbeta1 treatment increased intracellular H2O2 levels with similar kinetics to EGFR activation.
  • N-acetyl cysteine pretreatment blocked TGFbeta1-induced H2O2 production and EGFR phosphorylation.
  • Direct H2O2 treatment phosphorylated EGFR, and catalase inhibition prolonged TGFbeta1-induced EGFR activation.
  • TGFbeta1-induced EGFR activation led to Erk1/2 activation.

Conclusions:

  • TGFbeta1 activates EGFR through an H2O2-dependent mechanism.
  • Hydrogen peroxide acts as a crucial mediator in the crosstalk between TGFbeta1 and EGFR signaling.
  • This pathway culminates in the activation of Erk1/2, suggesting a role in cellular processes like proliferation and survival.

More Related Videos

A Combined 3D Tissue Engineered In Vitro/In Silico Lung Tumor Model for Predicting Drug Effectiveness in Specific Mutational Backgrounds13:34

A Combined 3D Tissue Engineered In Vitro/In Silico Lung Tumor Model for Predicting Drug Effectiveness in Specific Mutational Backgrounds

Published on: April 6, 2016

Establishing Dual Resistance to EGFR-TKI and MET-TKI in Lung Adenocarcinoma Cells In Vitro with a 2-step Dose-escalation Procedure09:38

Establishing Dual Resistance to EGFR-TKI and MET-TKI in Lung Adenocarcinoma Cells In Vitro with a 2-step Dose-escalation Procedure

Published on: August 11, 2017

Related Concept Videos

Mitogens and the Cell Cycle02:38

Mitogens and the Cell Cycle

Mitogens and their receptors play a crucial role in controlling the progression of the cell cycle. However, the loss of mitogenic control over cell division leads to tumor formation. Therefore, mitogens and mitogen receptors play an important role in cancer research. For instance, the epidermal growth factor (EGF) - a type of mitogen and its transmembrane receptor (EGFR), decides the fate of the cell's proliferation. When EGF binds to EGFR, a member of the ErbB family of tyrosine kinase...
TGF - β Signaling Pathway01:16

TGF - β Signaling Pathway

The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors are of three kinds RI, RII, and RIII. The RI...
mTOR Signaling and Cancer Progression03:03

mTOR Signaling and Cancer Progression

The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
The mTOR pathway or the...
Regulation of Angiogenesis and Blood Supply01:24

Regulation of Angiogenesis and Blood Supply

Rapidly dividing tumors, embryos, and wounded tissues require more oxygen than usual, lowering the oxygen concentration in the blood. At low oxygen or hypoxic conditions, an oxygen-sensitive transcription factor called the hypoxia-inducible factor 1 or HIF1 is activated. HIF1 is a dimeric protein of alpha (ɑ) and beta (β) subunits.  Under optimal oxygen conditions, HIF1β is present in the nucleus while HIF1ɑ remains in the cytosol. HIF1ɑ is hydroxylated by prolyl hydroxylase and factor...
Abnormal Proliferation02:23

Abnormal Proliferation

Under normal conditions, most adult cells remain in a non-proliferative state unless stimulated by internal or external factors to replace lost cells. Abnormal cell proliferation is a condition in which the cell's growth exceeds and is uncoordinated with normal cells. In such situations, cell division persists in the same excessive manner even after cessation of the stimuli, leading to persistent tumors. The tumor arises from the damaged cells that replicate to pass the damage to the daughter...
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a rapamycin-insensitive companion...