Formation of long-lived reactive species of blood serum proteins by the action of heat

Abstract

It has been previously established that heat induces the formation of reactive oxygen species (ROS) in aqueous solutions. In biological systems, ROS cause oxidative damage predominantly to proteins due to their abundance and sensitivity to oxidation. Proteins oxidized by the action of X-rays represent long-lived reactive species, which trigger the secondary generation of ROS (Bruskov et al. (2012) [25]). Here we studied the possibility of formation of long-lived species of the blood serum proteins bovine serum albumin and bovine gamma-globulin in air-saturated solutions under the action of heat. It is shown that heat induces the generation of long-lived protein species, which in turn generate ROS ((1)О2, (·)O2(-), (·)OН, and H2O2). The formation of the long-lived reactive species of BSA and BGG with a half-life of about 4h induced by moderate hyperthermia was revealed using the chemiluminescence of protein solutions. It was found that long-lived reactive species of BSA and BGG cause prolonged generation of H2O2. The results obtained suggest that H2O2 produced by proteins after heating represents a messenger in signaling pathways and produces therapeutic effects in living organisms.

Keywords: Action of heat; BGG; BSA; CCA; Hydrogen peroxide; LRPS; Long-lived reactive protein species; PBS; Protein oxidation; ROS; Reactive oxygen species; SOD; bovine gamma-globulin; bovine serum albumin; coumarin-3-carboxylic acid; long-lived reactive protein species; phosphate-buffered saline; reactive oxygen species; superoxide dismutase.