Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Mitochondrial Membranes01:45

Mitochondrial Membranes

A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
Cellular Injury I: Introduction01:00

Cellular Injury I: Introduction

Cellular injury occurs when a cell cannot maintain homeostasis or adapt to stressors such as hypoxia, toxins, or trauma. Depending on severity and duration, injury may be reversible, allowing recovery, or irreversible, leading to cell death.General Mechanisms of Cell InjuryAlthough causes vary, most cellular injuries arise from a few key mechanisms that disrupt essential functions and often amplify one another. Cell survival depends on the extent and balance of these disturbances.ATP depletion...
Cellular Injury IV: Necrosis01:16

Cellular Injury IV: Necrosis

Necrosis is a form of irreversible cell death caused by severe injury such as ischemia, toxins, or trauma. Unlike programmed cell death, it is an uncontrolled, pathological process that typically provokes inflammation in surrounding tissues.Pathophysiologic ChangesNecrosis begins when cells sustain critical damage, leading to swelling of organelles, particularly mitochondria, and rapid ATP depletion. As energy levels decline, membrane ion pumps fail, leading to calcium influx and eventually,...
Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

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...
Mitochondria01:37

Mitochondria

Mitochondria are eukaryotic cellular organelles that are known to produce energy through a process called oxidative phosphorylation. Besides their primary function, mitochondria are involved in various cellular processes, including cell growth, differentiation, signaling, metabolism, and senescence. Age-related changes cause a decline in mitochondrial quality and integrity due to increased mitochondrial mutations and oxidative damage. Thus, aging can severely impact mitochondrial functions,...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Mutation of a single cysteine in CaMKIIδ protects the heart from ischemia-reperfusion Injury.

bioRxiv : the preprint server for biology·2026
Same author

CD83 suppresses endogenous March-I-dependent MHC class II ubiquitination, endocytosis, and degradation.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

Double alkylation with maleimide-PEG-biotin: An enrichment method for cysteine redox states.

Analytical biochemistry·2025
Same author

Metabolic dependency mapping identifies Peroxiredoxin 1 as a driver of resistance to ATM inhibition.

Redox biology·2025
Same author

Oxidation of CaMKIIα cysteines inhibits autonomous activation induced by phosphorylation.

Archives of biochemistry and biophysics·2024
Same author

Corrigendum to "Loss of methionine sulfoxide reductases increases resistance to oxidative stress" [Free Radic. Biol. Med. 145 (2019) 374-384].

Free radical biology & medicine·2024

Related Experiment Video

Updated: Jun 16, 2026

Cellular Redox Profiling Using High-content Microscopy
11:37

Cellular Redox Profiling Using High-content Microscopy

Published on: May 14, 2017

Oxidative stress causes reversible changes in mitochondrial permeability and structure.

Nelson B Cole1, Mathew P Daniels, Rodney L Levine

  • 1Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, Bethesda, MD 20892-8012, USA. ncole@nhlbi.nih.gov

Experimental Gerontology
|January 26, 2010
PubMed
Summary

Reactive oxygen species alter mitochondrial permeability, making matrix proteins detectable. This rapid, reversible change suggests a role in cell communication.

More Related Videos

Assessment of Open Probability of the Mitochondrial Permeability Transition Pore in the Setting of Coenzyme Q Excess
07:35

Assessment of Open Probability of the Mitochondrial Permeability Transition Pore in the Setting of Coenzyme Q Excess

Published on: June 1, 2022

Confocal Imaging of Single Mitochondrial Superoxide Flashes in Intact Heart or In Vivo
12:06

Confocal Imaging of Single Mitochondrial Superoxide Flashes in Intact Heart or In Vivo

Published on: November 5, 2013

Related Experiment Videos

Last Updated: Jun 16, 2026

Cellular Redox Profiling Using High-content Microscopy
11:37

Cellular Redox Profiling Using High-content Microscopy

Published on: May 14, 2017

Assessment of Open Probability of the Mitochondrial Permeability Transition Pore in the Setting of Coenzyme Q Excess
07:35

Assessment of Open Probability of the Mitochondrial Permeability Transition Pore in the Setting of Coenzyme Q Excess

Published on: June 1, 2022

Confocal Imaging of Single Mitochondrial Superoxide Flashes in Intact Heart or In Vivo
12:06

Confocal Imaging of Single Mitochondrial Superoxide Flashes in Intact Heart or In Vivo

Published on: November 5, 2013

Area of Science:

  • Cell Biology
  • Mitochondrial Research
  • Oxidative Stress

Background:

  • Mitochondria are central players in cellular reactive oxygen species (ROS) production and are also targets of ROS.
  • Mitochondrial matrix proteins are typically inaccessible to antibodies in fixed cells.

Purpose of the Study:

  • To investigate the effect of oxidative stress on mitochondrial permeability and protein accessibility.
  • To explore the structural and permeability changes in mitochondria induced by ROS.

Main Methods:

  • Immunofluorescence microscopy was used to detect mitochondrial matrix proteins.
  • Cells were subjected to oxidative stress before fixation and permeabilization with saponin.
  • Electron microscopy was employed to examine mitochondrial structure.

Main Results:

  • Oxidative stress rendered normally undetectable mitochondrial matrix proteins accessible.
  • Electron microscopy showed loss of matrix density and disorganized inner membrane cristae upon oxidative stress.
  • These structural and permeability changes were rapidly reversible upon removal of oxidative stress.

Conclusions:

  • Reactive oxygen species can reversibly alter mitochondrial membrane permeability.
  • This reversible permeability change may serve as a communication mechanism within the cell, potentially linking nuclear and mitochondrial functions.