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Quantitative biology of hydrogen peroxide signaling

Hydrogen peroxide (H(2)O(2)) controls signaling pathways in cells by oxidative modulation of the activity of redox sensitive proteins denominated redox switches. Here, quantitative biology concepts are applied to review how H(2)O(2) fulfills a key role in information transmission. Equations describe...

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Detalles Bibliográficos
Autores principales: Antunes, Fernando, Brito, Paula Matos
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5436100/
https://www.ncbi.nlm.nih.gov/pubmed/28528123
http://dx.doi.org/10.1016/j.redox.2017.04.039
Descripción
Sumario:Hydrogen peroxide (H(2)O(2)) controls signaling pathways in cells by oxidative modulation of the activity of redox sensitive proteins denominated redox switches. Here, quantitative biology concepts are applied to review how H(2)O(2) fulfills a key role in information transmission. Equations described lay the foundation of H(2)O(2) signaling, give new insights on H(2)O(2) signaling mechanisms, and help to learn new information from common redox signaling experiments. A key characteristic of H(2)O(2) signaling is that the ratio between reduction and oxidation of redox switches determines the range of H(2)O(2) concentrations to which they respond. Thus, a redox switch with low H(2)O(2)-dependent oxidability and slow reduction rate responds to the same range of H(2)O(2) concentrations as a redox switch with high H(2)O(2)-dependent oxidability, but that is rapidly reduced. Yet, in the first case the response time is slow while in the second case is rapid. H(2)O(2) sensing and transmission of information can be done directly or by complex mechanisms in which oxidation is relayed between proteins before oxidizing the final regulatory redox target. In spite of being a very simple molecule, H(2)O(2) has a key role in cellular signaling, with the reliability of the information transmitted depending on the inherent chemical reactivity of redox switches, on the presence of localized H(2)O(2) pools, and on the molecular recognition between redox switches and their partners.