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Related Concept Videos

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,...
Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...

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Related Experiment Video

Updated: Jul 15, 2026

Ratiometric Biosensors that Measure Mitochondrial Redox State and ATP in Living Yeast Cells
12:22

Ratiometric Biosensors that Measure Mitochondrial Redox State and ATP in Living Yeast Cells

Published on: July 22, 2013

Proteome alterations in rat mitochondria caused by aging.

Norbert A Dencher1, Monika Frenzel, Nicole H Reifschneider

  • 1Physical Biochemistry, Department of Chemistry, Darmstadt University of Technology, Petersenstr., 22, D-64287 Darmstadt, Germany. nad@pop.tu-darmstadt.de

Annals of the New York Academy of Sciences
|April 27, 2007
PubMed
Summary

Mitochondrial protein changes during aging, particularly in the inner membrane, offer insights into aging and related diseases. Alterations in ATP synthase and OXPHOS supercomplexes in rat brains link respiration to longevity and ROS production.

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Area of Science:

  • Mitochondrial biology
  • Aging research
  • Proteomics

Background:

  • Mitochondrial protein analysis is key to understanding aging and age-related diseases.
  • The inner mitochondrial membrane proteome, including respiratory chain complexes, is crucial for life-span control.
  • Age-dependent variations in mitochondrial proteins are examined in various rat tissues.

Purpose of the Study:

  • To investigate age-dependent variations in the mammalian mitochondrial membrane proteome.
  • To explore the role of mitochondrial proteins and their supramolecular organization in aging.
  • To identify age-related changes in protein abundance, composition, structure, and activity.

Main Methods:

  • Native polyacrylamide gel electrophoresis (native PAGE) to separate proteins and supercomplexes in their native state.
  • MALDI-TOF mass spectrometry for protein identification and quantification.
  • Analysis of protein variations in rat brain cortex during aging.

Main Results:

  • Detected age-modulated differences in mitochondrial and non-mitochondrial proteins (e.g., Na,K-ATPase, HSP60, aconitase-2, V-type ATPase, ATP synthase, OXPHOS complexes I-IV) in rat brain.
  • Observed a decrease in intact MF(o)F(1) ATP synthase during aging in the cortex.
  • Found age-related alterations in the oligomerization of MF(o)F(1) ATP synthase and the abundance of OXPHOS supercomplexes.

Conclusions:

  • Age-related changes in MF(o)F(1) ATP synthase oligomerization may link respiration to longevity.
  • Alterations in the supramolecular architecture of OXPHOS complexes could explain age-related changes in ROS production.
  • Mitochondrial proteome analysis provides insights into aging mechanisms and potential therapeutic targets.