Type of document : Magazine article Edition cipher : Author(s) : Rakhmetov A. D., Lee Sang Pil, Ostapchenko L. I., Chae Title : Prx II and CKBB proteins interaction under physiological and thermal stress conditions in A549 and HeLa cells Parallel titles :Взаємодія протеїнів Prx II та CKBB за умов теплового стресу в клітинах A549 та HeLa Place of publication : Український біохімічний журнал. - 2016. - Т. 88, № 1. - С. 61-68 (Cipher УУ1/2016/88/1) Notes : Бібліогр.: в кінці ст. MeSH-main: ПЕРОКСИРЕДОКСИНЫ -- PEROXIREDOXINS ТЕПЛОВОГО СТРЕССА СИНДРОМЫ -- HEAT STRESS DISORDERS КРЕАТИНКИНАЗА -- CREATINE KINASE ВЕСТЕРН-БЛОТТИНГ -- BLOTTING, WESTERN Annotation: Peroxiredoxins (Prxs) are versatile enzymes that demonstrate various cell functions as peroxidases, protein chaperones, functions of signal modulators and binding partners. It is well established that Prxs can interact with multiple proteins in cells, such as ASK1, Cdk5-p35, JNK, MIF, PDGF, TKR4 and others. In this study, we attempted to evaluate a possible association between ubiquitous Prx II and ATP/ADP buffering enzyme - brain-type creatine kinase (CKBB). Our co-immunoprecipitation (Co-IP) results from the A549 and HeLa cell lysates with overexpressed HA-Prx II and Flag-CKBB have demonstrated strong association between two proteins under non-stressed conditions. This protein interaction was enhanced by the heat treatment with further HA-Prx IIprecipitation to the immobilized Flag-CKBB depending on the temperature increase. Temperature induced oligomerization of Prx II may contribute to the formation of Prx II conglomerates, which in turn, can associate with CKBB and increase signal intensities on the blotted membranes. Thus, such association and oligomerization of Prx II could take part in recovery and protection of the CKBB enzyme activity from inactivation during heat-induced stress Additional Access Points: Rakhmetov, A. D. Lee, Sang Pil Ostapchenko, L. I. Chae