Carbonic Anhydrase III S-Glutathionylation Is Necessary for Anti-Oxidant Activity  

作　　者：P. Roy M. Ireland S. Roy J. Craft C. Bartholomew 

机构地区：[1]Department of Biological & Biomedical Sciences, School of Health & Life Sciences, Glasgow Caledonian University, City Campus, Glasgow, UK

出　　处：《Yangtze Medicine》2018年第4期244-254,共11页长江医药（英文）

摘　　要：Carbonic anhydrase isozyme CA3 protects cells against oxidative stress. Ectopic expression of murine Ca3, but not Ca2, protects proto-oncogene Evi1 expressing Rat1 fibroblast cells (ca3low) against hydrogen peroxide (H2O2) induced stress. Ca3 is S-glutathionylated via glutathione adducts with cysteines 181 and 186. Substitution of both Ca3 cysteines with serine fails to protect cells from oxidative stress. Insertion of cysteine at 181 and 186 in Ca2 is insufficient for conferring efficient anti-oxidant activity. This shows for the first time that S-glutathionylation of cys181 and cys186 residues is required for Ca3 anti-oxidant activity but that additional factors are also required.Carbonic anhydrase isozyme CA3 protects cells against oxidative stress. Ectopic expression of murine Ca3, but not Ca2, protects proto-oncogene Evi1 expressing Rat1 fibroblast cells (ca3low) against hydrogen peroxide (H2O2) induced stress. Ca3 is S-glutathionylated via glutathione adducts with cysteines 181 and 186. Substitution of both Ca3 cysteines with serine fails to protect cells from oxidative stress. Insertion of cysteine at 181 and 186 in Ca2 is insufficient for conferring efficient anti-oxidant activity. This shows for the first time that S-glutathionylation of cys181 and cys186 residues is required for Ca3 anti-oxidant activity but that additional factors are also required.

关 键 词：CA3 CAIII Carbonic ANHYDRASE III S-GLUTATHIONYLATION APOPTOSIS ANTI-OXIDANT 

分 类 号：R73[医药卫生—肿瘤]