Related Experiment Video

Updated: May 12, 2026

Analysis of Oxidative Stress in Zebrafish Embryos
11:05

Analysis of Oxidative Stress in Zebrafish Embryos

Published on: July 7, 2014

37.2K

Biomarkers of NRF2 signalling: Current status and future challenges

Christina Morgenstern1, Isabel Lastres-Becker2, Birsen Can Demirdöğen3

  • 1Department of Otorhinolaryngology, Medical University of Vienna, General Hospital of Vienna, Waehringer Guertel 18-20, A-1090, Vienna, Austria; Institute of Molecular Biosciences, University of Graz, Humboldtstraße 50, A-8010, Graz, Austria.

Redox Biology
|April 21, 2024
PubMed

Insights

Identifying reliable biomarkers for Nuclear factor erythroid 2-related factor 2 (NRF2) signaling is crucial for disease research. This study proposes a robust panel of NRF2 target genes for accurate activity monitoring across various conditions.

Area of Science:

  • Molecular Biology
  • Cellular Signaling
  • Biochemistry

Background:

  • Nuclear factor erythroid 2-related factor 2 (NRF2) is a key regulator of cellular defense against oxidative stress and inflammation.
  • NRF2 signaling is a therapeutic target for diseases involving oxidative stress.
  • Accurate monitoring of NRF2 activity is essential for translational research.

Purpose of the Study:

  • To identify a consistent and reliable panel of NRF2 target genes for assessing NRF2 activity.
  • To evaluate the suitability of these markers in clinically relevant biofluids.
  • To address the lack of consensus on optimal NRF2 biomarkers.

Main Methods:

  • Comprehensive literature search using stringent criteria.
  • Identification and validation of direct NRF2 target genes.
  • Assessment of marker relevance in biofluids.

Main Results:

  • A robust panel of NRF2 target genes (GCLC, GCLM, HMOX1, NQO1, SRXN1, TXNRD1) was identified.
  • These markers are directly regulated by NRF2 across multiple cell and tissue types.
  • The relevance of these markers in human biofluids was assessed.

Conclusions:

  • The identified gene panel provides a reliable method for monitoring NRF2 activity.
  • Further research is needed to optimize NRF2 biomarker development for clinical applications.
  • This panel aids in understanding NRF2's role in disease and therapeutic interventions.
Keywords:
BiomarkerNRF2Oxidative stress responseTarget genesTranscription factor

More Related Videos

Measurements of Physiological Stress Responses in C. Elegans10:36

Measurements of Physiological Stress Responses in C. Elegans

Published on: May 21, 2020

13.9K
Quantification of Reactive Oxygen Species Using 2′,7′-Dichlorofluorescein Diacetate Probe and Flow-Cytometry in Müller Glial Cells14:25

Quantification of Reactive Oxygen Species Using 2′,7′-Dichlorofluorescein Diacetate Probe and Flow-Cytometry in Müller Glial Cells

Published on: May 13, 2022

6.7K

Related Concept Videos

Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

Proteins targeted to the nucleus carry short stretches of amino acid sequences called the nuclear localization signal or NLS. Classical nuclear localization signals are of two types: monopartite and bipartite NLS. Monopartite classical NLS (cNLS) consists of a single cluster of 4-8 amino acids. Bipartite cNLS consists of two clusters of  2-3 amino acids and a 9-12 residue long proline-rich linker bridging the two clusters. Signal clusters are rich in positively charged amino acids such as...
NF-κB-dependent Signaling Pathway02:26

NF-κB-dependent Signaling Pathway

The transcription factor NF-κB was discovered in 1986 in the lab of Nobel laureate Professor David Baltimore, for its interaction with the immunoglobulin light chain enhancer in B-cells. After more than three decades of study, it is now evident that NF-κB regulates the expression of over 100 genes. Most of these genes play an essential role in the innate and adaptive immune responses as well as the inflammatory responses of animals.
NF-κB-dependent Signaling Mechanism
The heterodimer of NF-κB...
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
NF-kB-dependent Signaling Pathway02:26

NF-kB-dependent Signaling Pathway

The transcription factor NF-κB was discovered in 1986 in the lab of Nobel laureate Professor David Baltimore, for its interaction with the immunoglobulin light chain enhancer in B-cells. After more than three decades of study, it is now evident that NF-κB regulates the expression of over 100 genes. Most of these genes play an essential role in the innate and adaptive immune responses as well as the inflammatory responses of animals.
NF-κB-dependent Signaling Mechanism
The heterodimer of NF-κB...
Signal Transduction: Overview01:26

Signal Transduction: Overview

Cells respond to many types of information, often through receptor proteins positioned on the membrane. They respond to chemical signals, such as hormones, neurotransmitters, and other signaling molecules, initiating a series of molecular reactions to produce an appropriate response. This is called signal transduction. Cells also coordinate different responses elicited by the same signaling molecule via mediators, allowing molecular cross-talk.
Typically, signal transduction involves three...
Transduction01:16

Transduction

Among the three main modes of HGT—transformation, conjugation, and transduction—transduction is unique in that it is mediated by bacteriophages, or bacterial viruses.Transduction occurs in two ways. Generalized transduction occurs during the lytic cycle of a bacteriophage infection. In this process, bacteriophages infect bacterial cells, replicate within them, and ultimately cause cell lysis, releasing newly assembled virions. Occasionally, random fragments of the bacterial genome are...