Related Experiment Video
Updated: May 23, 2026

Studying TGF-β Signaling and TGF-β-induced Epithelial-to-mesenchymal Transition in Breast Cancer and Normal Cells
Published on: October 27, 2020
Human peroxiredoxin 1 modulates TGF-β1-induced epithelial-mesenchymal transition through its peroxidase activity
Bin Ha1, Eun-Kyung Kim, Ji-Hee Kim
1Lee Gil Ya Cancer and Diabetes Institute, Gachon University, Incheon 406-799, Republic of Korea.
Abstract:
The epithelial-to-mesenchymal transition (EMT), which is induced by transforming growth factor-β1 (TGF-β1), is an important event that allows cancer cells to obtain invasive and metastatic characteristics. Although human peroxiredoxin 1 (hPrx1) has been implicated in tumor progression (e.g., invasion and metastasis), little is known about the role of hPrx1 in the EMT process during tumorigenesis. Here, we investigated the regulatory effect of hPrx1 during TGF-β1-induced EMT in A549 lung adenocarcinoma cells. We observed that high hPrx1 levels downregulated E-cadherin expression, and low hPrx1 levels upregulated E-cadherin expression, suggesting that the hPrx1 level may be correlated with EMT. Knockdown of hPrx1 significantly inhibited TGF-β1-induced EMT and cell migration, whereas hPrx1 overexpression enhanced TGF-β1-induced EMT and cell migration. In contrast to wild-type hPrx1, a peroxidase-inactive hPrx1 mutant (hPrx1-C51S) resulted in markedly increased E-cadherin expression. Moreover, hPrx1 regulated the expression of two E-cadherin transcriptional repressors, Snail and Slug. These findings provide new insight into the role of hPrx1 in regulating TGF-β1-induced EMT.
More Related Videos
06:02Development of an In Vitro Assay to Evaluate Contractile Function of Mesenchymal Cells that Underwent Epithelial-Mesenchymal Transition
Published on: June 10, 2016
07:49Molecular Analysis of Endothelial-mesenchymal Transition Induced by Transforming Growth Factor-β Signaling
Published on: August 3, 2018
Related Concept Videos
TGF - β Signaling Pathway
Peroxisomes
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Protein Import into the Peroxisomes
Peroxisomal Protein Import:
Peroxisomes lack the genetic machinery required to code for their own proteins. Hence, most peroxisomal membrane, lumenal and transmembrane proteins are synthesized in the cytoplasm or ER and transported to the peroxisome...
Regulation of Angiogenesis and Blood Supply
Role of Matrix Metalloproteases in Degradation of ECM
A...