Tracking reactive oxygen species (ROS) and in particular hydrogen peroxyde (H2O2) is particularly relevant for studying oxidative stress (involved in the development of a wide variety of pathologies, including malignant diseases, diabetes mellitus, atherosclerosis, chronic inflammatory processes, ischemia and reperfusion injury, and some neurodegenerative diseases). H2O2 has also a role of intracellular second messenger, controlling signaling cascades by selective oxidation of redox active thiolates in proteins.
The first genetically-encoded fluorescent indicators of redox changes were reduction-oxidation-sensitive GFPs (roGFPs). This family of indicators was created in 2004 by substitution of surface-exposed residues on the Aequorea victoria green fluorescent protein (GFP) with cysteines in appropriate positions to form disulfide bonds [2, 3]. roGFPs have two fluorescence excitation maxima at about 400 and 490 nm and display rapid and reversible ratiometric changes in fluorescence in response to changes in ambient redox potential in vitro and in vivo. These probes are ratiometric because of the presence of these two excitation peaks: ratios of fluorescence from excitation at 400 and 490 nm indicate the extent of oxidation (and thus the redox potential) while canceling out the amount of indicator and the absolute optical sensitivity.
In 2006, a specific H2O2 indicator, called HyPer, was designed in the laboratory of Sergey A. Lukyanov . HyPer consists of a circularly permuted yellow fluorescent protein (cpYFP) inserted into the regulatory domain of the prokaryotic H2O2-sensing protein, OxyR . HyPer2, an improved version of the probe, was generated by a single point mutation A406V from HyPer corresponding to A233V in wild type OxyR .
Summary of available sensors
|Acronym||Full Name||Description||Accession #||Refs|
|roGFP1||reduction-oxydation-sensitive GFP 1||[2, 3]|
|roGFP2||reduction-oxydation-sensitive GFP 2||[2, 3]|
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