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Related Concept Videos

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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...
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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...
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During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
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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.
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The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
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Caveolae and the oxidative stress response.

Yeping Wu1, Ye-Wheen Lim1, Robert G Parton1,2

  • 1The University of Queensland, Institute for Molecular Bioscience, 4072 Brisbane, Australia.

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|May 30, 2023
PubMed
Summary

Caveolae disassembly during oxidative stress releases proteins that regulate the master redox controller, nuclear factor erythroid 2-related factor 2, impacting cell death and homeostasis.

Keywords:
Cavin1NRF2caveolaecell deathlipid peroxidationoxidative stress

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Area of Science:

  • Cellular biology
  • Oxidative stress research
  • Molecular mechanisms of cell death

Background:

  • Oxidative stress is implicated in numerous diseases.
  • Cells possess intricate mechanisms to counteract oxidative stress.
  • Ferroptosis is an iron-dependent cell death pathway activated by lipid peroxidation.

Purpose of the Study:

  • To explore the connection between caveolae and cellular oxidative stress response.
  • To elucidate the role of caveolae disassembly in regulating cellular redox homeostasis.

Main Methods:

  • Analysis of recent studies in cultured cells.
  • Investigation using an in vivo model.
  • Examination of lipid peroxidation effects on caveolae structure and protein release.

Main Results:

  • Oxidative stress-induced lipid peroxidation leads to caveolae disassembly.
  • Released caveola proteins modulate nuclear factor erythroid 2-related factor 2 (NRF2).
  • Caveolae appear to maintain cellular susceptibility to oxidative stress-induced death.

Conclusions:

  • Caveolae play a significant role in cellular homeostasis.
  • Caveolae are involved in the cellular response to oxidative stress and wounding.
  • Caveolae disassembly is a key event in the cellular oxidative stress response pathway.