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Related Concept Videos

Peroxisomes01:24

Peroxisomes

Peroxisomes are specialized organelles present in fungi, plant, and animal cells. It can vary in number, size, morphology, and activity depending on the type of tissue and the nutritional state of the cell. For example, cells with active lipid metabolism, such as adipocytes, neurons, and hepatocytes, have more peroxisomes than other cells in the body. Besides their primary role in breaking down complex organic molecules, peroxisomes can also synthesize specific macromolecules and participate in...
Peroxisomes01:30

Peroxisomes

Peroxisomes and mitochondria are two important oxygen-utilizing organelles in eukaryotic cells. Mitochondria carry out cellular respiration—the process that converts energy from food into ATP. Peroxisomes carry out a variety of functions, primarily breaking down different substances, such as fatty acids.The peroxisome is a single membrane-bound cellular organelle that can perform several different functions, including lipid metabolism and chemical detoxification. The enzymes within peroxisomes...
Peroxisomes01:24

Peroxisomes

Peroxisomes are specialized organelles present in fungi, plant, and animal cells. It can vary in number, size, morphology, and activity depending on the type of tissue and the nutritional state of the cell. For example, cells with active lipid metabolism, such as adipocytes, neurons, and hepatocytes, have more peroxisomes than other cells in the body. Besides their primary role in breaking down complex organic molecules, peroxisomes can also synthesize specific macromolecules and participate in...
Protein Import into the Peroxisomes01:27

Protein Import into the Peroxisomes

Cells contain membrane-bound organelles called peroxisomes that oxidize organic molecules by transferring hydrogen atoms to oxygen, producing hydrogen peroxide. Peroxisomes enzymatically convert the released hydrogen peroxide into water and oxygen.
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...
Oxidation of Phenols to Quinones01:17

Oxidation of Phenols to Quinones

In the presence of oxidizing agents, phenols are oxidized to quinones. Quinones can be easily reduced back to phenols using mild reducing agents. The electron-donating hydroxyl group enhances the reactivity of the aromatic ring, enabling oxidation of the ring even in the absence of an α hydrogen.
o-hydroxy phenols are oxidized to o-quinones and p-hydroxy phenols to p-quinones. Such redox reactions involve the transfer of two electrons and two protons. The reversible redox property is crucial in...
Radical Autoxidation01:20

Radical Autoxidation

The oxidation of an organic compound in the presence of air or oxygen is called autoxidation. For example, cumene reacts with oxygen to form hydroperoxide. Autoxidation involves initiation, propagation, and termination steps. Many organic compounds are susceptible to autoxidation—especially ethers in the presence of oxygen, which form hydroperoxides. Even though this reaction is slow, old ether bottles contain small amounts of peroxide, which leads to laboratory explosions during ether...

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Related Experiment Video

Updated: Jul 9, 2026

Imaging Approaches to Assessments of Toxicological Oxidative Stress Using Genetically-encoded Fluorogenic Sensors
09:33

Imaging Approaches to Assessments of Toxicological Oxidative Stress Using Genetically-encoded Fluorogenic Sensors

Published on: February 7, 2018

Stress-induced peroxiredoxins.

Tetsuro Ishii1, Toru Yanagawa

  • 1Graduate School of Comprehensive Human Sciences, University of Tsukuba, Tsukuba, Ibaraki, 305-8575 Japan.

Sub-Cellular Biochemistry
|December 19, 2007
PubMed
Summary

Prx proteins, including Prx I, II, and III, are upregulated under cellular stress. This antioxidant response, involving Nrf2 and Keap1, helps cells recover from oxidative damage.

Area of Science:

  • Biochemistry
  • Cellular Biology
  • Molecular Biology

Background:

  • The Peroxiredoxin (Prx) protein family plays a crucial role in cellular defense mechanisms.
  • Certain Prx members, particularly Prx I, are known to be upregulated in response to various cellular stress conditions.
  • Prx I functions as a major cytoplasmic antioxidant enzyme, with its gene expression activated by diverse stress agents.

Purpose of the Study:

  • To investigate the stress-induced upregulation of Prx I, II, and III.
  • To elucidate the molecular mechanisms underlying the regulation of Prx gene expression under stress.
  • To understand the role of Prx proteins in cellular recovery from oxidative damage.

Main Methods:

  • Analysis of gene expression patterns under various stress conditions.

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Monitoring Stub1-Mediated Pexophagy
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Monitoring Stub1-Mediated Pexophagy

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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

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Last Updated: Jul 9, 2026

Imaging Approaches to Assessments of Toxicological Oxidative Stress Using Genetically-encoded Fluorogenic Sensors
09:33

Imaging Approaches to Assessments of Toxicological Oxidative Stress Using Genetically-encoded Fluorogenic Sensors

Published on: February 7, 2018

Monitoring Stub1-Mediated Pexophagy
08:26

Monitoring Stub1-Mediated Pexophagy

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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

  • Investigation of the roles of transcription factors Nrf2 and Keap1 in Prx I regulation via the antioxidant/electrophile response element (ARE/EpRE).
  • Examination of Prx I and II gene activation by X-ray irradiation in testicular tissues.
  • Assessment of mitochondrial Prx III upregulation by stress agents in cellular and animal models.
  • Main Results:

    • Prx I, II, and III expression levels increase under stress conditions.
    • The transcription factor Nrf2 and its inhibitor Keap1 are essential for stress-induced Prx I gene activation through the ARE/EpRE.
    • X-ray irradiation activates the gene expression of Prx I and II in the testis.
    • Mitochondrial Prx III is upregulated by stress agents in both cultured cells and experimental animals.

    Conclusions:

    • The upregulation of Prx proteins (Prx I, II, and III) is a significant cellular response to oxidative stress.
    • The Nrf2-Keap1 pathway is critical for regulating the antioxidant response of Prx I.
    • Prx upregulation contributes to cellular recovery mechanisms following oxidative damage.