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Lysosomal ROS formation.

Hans Nohl1, Lars Gille

  • 1Research Institute for Biochemical Pharmacology and Toxicology, University of Veterinary Medicine Vienna, Vienna, Austria. hans.nohl@vu-wien.ac.at

Redox Report : Communications in Free Radical Research
|November 2, 2005
PubMed
Summary

Lysosomes utilize a novel redox chain involving ubiquinone to pump protons, contributing to lysosomal acidification. This process, linked to NADH and oxygen, generates hydrogen peroxide radicals.

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Area of Science:

  • Cellular Biology
  • Biochemistry
  • Organelle Function

Background:

  • Ubiquinone (coenzyme Q) is found in various cellular membranes, including mitochondria, Golgi vesicles, and lysosomes.
  • Lysosomes maintain a low internal pH crucial for hydrolytic enzyme activity.
  • Ubiquinone's redox cycling is linked to proton transport, suggesting a role in proton distribution.

Purpose of the Study:

  • To investigate the role of ubiquinone in lysosomal proton distribution and acidification.
  • To identify the components of a potential lysosomal redox chain involved in proton translocation.

Main Methods:

  • Analysis of lysosomal ubiquinone reduction states.
  • Investigating ubiquinone reduction by NADH and identifying involved enzymes.
  • Studying the effect of oxygen as a terminal electron acceptor.

Main Results:

  • Lysosomes contain high levels of ubiquinone, with ~70% in a reduced state.
  • A novel lysosomal redox chain, including an FAD-containing NADH dehydrogenase and a b-type cytochrome, reduces ubiquinone.
  • This redox chain translocates protons into the lysosome, contributing to acidification and producing HO radicals via oxygen reduction.

Conclusions:

  • A novel proton-pumping redox chain exists in lysosomes, utilizing ubiquinone to regulate internal pH.
  • Oxygen acts as the terminal electron acceptor, leading to ROS formation and lysosomal acidification.
  • The precise function and significance of this redox chain and ROS production require further investigation.

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