About the dangers, costs and benefits of living an aerobic lifestyle

Daniela Knoefler, Lars I.O. Leichert, Maike Thamsen, Claudia M. Cremers, Dana Reichmann, Michael J. Gray, Wei Yun Wholey, Ursula Jakob*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

The era in which ROS (reactive oxygen species) were simply the 'bad boys of biology' is clearly over. High levels of ROS are still rightfully considered to be toxic to many cellular processes and, as such, contribute to disease conditions and cell death. However, the high toxicity of ROS is also extremely beneficial, particularly as it is used to kill invading micro-organisms during mammalian host defence. Moreover, a transient, often more localized, increase in ROS levels appears to play a major role in signal transduction processes and positively affects cell growth, development and differentiation. At the heart of all these processes are redox-regulated proteins, which use oxidation-sensitive cysteine residues to control their function and by extension the function of the pathways that they are part of. Our work has contributed to changing the view about ROS through: (i) our characterization of Hsp33 (heat-shock protein 33), one of the first redox-regulated proteins identified, whose function is specifically activated by ROS, (ii) the development of quantitative tools that reveal extensive redox-sensitive processes in bacteria and eukaryotes, and (iii) the discovery of a link between early exposure to oxidants and aging. Our future research programme aims to generate an integrated and system-wide view of the beneficial and deleterious effects of ROS with the central goal to develop more effective antioxidant strategies and more powerful antimicrobial agents.

Original languageEnglish
Pages (from-to)917-921
Number of pages5
JournalBiochemical Society Transactions
Volume42
Issue number4
DOIs
StatePublished - Aug 2014

Keywords

  • Aging
  • Chaperone
  • Host defence
  • Oxidative stress
  • Protein unfolding

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