The peroxiredoxin repair proteins.
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Sulfiredoxin and sestrin are cysteine sulfinic acid reductases that selectively reduce or repair the hyperoxidized forms of typical 2-Cys peroxiredoxins within eukaryotes.Abstract:
Sulfiredoxin and sestrin are cysteine sulfinic acid reductases that selectively reduce or repair the hyperoxidized forms of typical 2-Cys peroxiredoxins within eukaryotes. As such these enzymes play key roles in the modulation of peroxide-mediated cell signaling and cellular defense mechanisms. The unique structure of sulfiredoxin facilitates access to the peroxiredoxin active site and novel sulfur chemistryread more
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Typical 2-Cys Peroxiredoxins: Structures, mechanisms and functions
TL;DR: This review summarizes recent progress in understanding of the catalytic and regulatory mechanisms of ‘typical 2‐Cys’ peroxiredoxins and of the biological roles played by these important enzymes in oxidative stress and nonstress‐related cellular signaling.
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Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins.
TL;DR: Strict conservation of the peroxidatic active site along with the variation in structural transitions provides a fascinating picture of how the diverse Prxs function to break down peroxide substrates rapidly.
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Glutathione peroxidases in different stages of carcinogenesis
TL;DR: GPx-mediated regulation of COX/LOX activities may be relevant to early stages of inflammation-mediated carcinogenesis, and GPxs prevent cancer initiation by removing hydroperoxides.
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An adult tissue-specific stem cell in its niche: a gene profiling analysis of in vivo quiescent and activated muscle satellite cells.
Giorgia Pallafacchina,Stéphanie François,Béatrice Regnault,Bertrand Czarny,Vincent Dive,Ana Cumano,Didier Montarras,Margaret Buckingham +7 more
TL;DR: It is demonstrated that metalloproteinase function is required for efficient regeneration in vivo, and revealed how the satellite cell protects itself from damage and maintains quiescence, while being primed for activation on receipt of the appropriate signal.
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The cysteine proteome.
TL;DR: The need for atlases of Cys modifications to develop systems biology models for integrative studies linking the Cys proteome to imaging and other omics platforms, providing a basis for improved redox-based therapeutics is focused on.
References
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REACTIVE OXYGEN SPECIES: Metabolism, Oxidative Stress, and Signal Transduction
Klaus Apel,Heribert Hirt +1 more
TL;DR: The mechanisms of ROS generation and removal in plants during development and under biotic and abiotic stress conditions are described and the possible functions and mechanisms for ROS sensing and signaling in plants are compared with those in animals and yeast.
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Structure, mechanism and regulation of peroxiredoxins
TL;DR: Using crystal structures, a detailed catalytic cycle has been derived for typical 2-Cys Prxs, including a model for the redox-regulated oligomeric state proposed to control enzyme activity.
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H2O2, a necessary evil for cell signaling
TL;DR: Once considered lethal to cells, reactive oxygen species are now known to be involved in redox signaling pathways that may contribute to normal cell function as well as disease progression.
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Peroxiredoxin Evolution and the Regulation of Hydrogen Peroxide Signaling
TL;DR: It is suggested that this adaptation allows 2-Cys Prxs to act as floodgates, keeping resting levels of hydrogen peroxide low, while permitting higher levels during signal transduction, and is proposed to be the structural origins of sensitivity.