- SIRT5 desuccinylates and activates SOD1 to eliminate ROS.
SIRT5 desuccinylates and activates SOD1 to eliminate ROS.
Biochemical and biophysical research communications (2013-10-22)
Zhi-Feng Lin, Hong-Bing Xu, Jian-Yun Wang, Qiang Lin, Zhen Ruan, Fa-Bing Liu, Wang Jin, Hai-Hua Huang, Xi Chen
PMID24140062
ABSTRACT
Cu/Zn superoxide dismutase (SOD1) is a key antioxidant enzyme. Deficiency of SOD1 is associated with various human diseases, including cancer. Here, we report that SOD1 is succinylated and that succinylation decreases its activity. SIRT5 binds to, desuccinylates and activates SOD1. SOD1-mediated ROS reduction is increased when SIRT5 is co-expressed. Furthermore, mutation of the SOD1 succinylation site inhibits the growth of lung tumor cells. These results reveal a novel post-translational regulation of SOD1 by means of succinylation and SIRT5-dependent desuccinylation, which is important for the growth of lung tumor cells.
MATERIALS
Product Number
Brand
Product Description
Sigma-Aldrich
L-Lysine monohydrochloride, from non-animal source, meets EP, JP, USP testing specifications, suitable for cell culture, 98.5-101.0%
Supelco
L-Lysine monohydrochloride, certified reference material, TraceCERT®, Manufactured by: Sigma-Aldrich Production GmbH, Switzerland
Supelco
L-Lysine monohydrochloride, Pharmaceutical Secondary Standard; Certified Reference Material