| Autor: |
Petrushanko IY; Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Street 32, 119991 Moscow, Russia., Lobachev VM; Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Street 32, 119991 Moscow, Russia., Kononikhin AS; Moscow Institute of Physics and Technology, 141700 Dolgoprudnyi, Moscow Region, Russia., Makarov AA; Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Street 32, 119991 Moscow, Russia., Devred F; Aix-Marseille University, Inserm, CRO2 UMR_S 911, Faculté de Pharmacie, 13385 Marseille, France., Kovacic H; Aix-Marseille University, Inserm, CRO2 UMR_S 911, Faculté de Pharmacie, 13385 Marseille, France., Kubatiev AA; Institute of General Pathology and Pathophysiology, RAMS, 125315, Moscow, Russian Federation., Tsvetkov PO; Aix-Marseille University, Inserm, CRO2 UMR_S 911, Faculté de Pharmacie, 13385 Marseille, France.; Institute of General Pathology and Pathophysiology, RAMS, 125315, Moscow, Russian Federation. |
| Abstrakt: |
NOX5 protein, one of the most active generators of reactive oxygen species (ROS), plays an important role in many processes, including regulation of cell growth, death and differentiation. Because of its central role in ROS generation, it needs to be tightly regulated to guarantee cellular homeostasis. Contrary to other members of NADPH-oxidases family, NOX5 has its own regulatory calcium-binding domain and thus could be activated directly by calcium ions. While several mechanisms of activation have been described, very little is known about the mechanisms that could prevent the overproduction of ROS by NOX5. In the present study using calorimetric methods and circular dichroism we found that oxidation of cysteine and methionine residues of NOX5 decreases binding of Ca2+ ions and perturbs both secondary and tertiary structure of protein. Our data strongly suggest that oxidation of calcium-binding domain of NOX5 could be implicated in its inactivation, serving as a possible defense mechanism against oxidative stress. |
