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   Functional heterogeneity of Nadph oxidases in atherosclerotic and aneurysmal diseases  
   
نویسنده kigawa y. ,miyazaki t. ,lei x.-f. ,kim-kaneyama j.-r. ,miyazaki a.
منبع journal of atherosclerosis and thrombosis - 2017 - دوره : 24 - شماره : 1 - صفحه:1 -13
چکیده    Nadph oxidases (nox) are enzymes that catalyze the production of reactive oxygen species (ros). four species of nox catalytic homologs (nox1,nox2,nox4,and nox5) are reportedly expressed in vascular tissues. the pro-atherogenic roles of nox1,nox2,and their organizer protein p47ph°x were manifested,and it was noted that the hydrogen peroxide-generating enzyme nox4 possesses atheroprotective effects. loss of nox1 or p47ph°x appears to ameliorate murine aortic dissection and subsequent aneurysmal diseases; in contrast,the ablation of nox2 exacerbates the aneurysmal diseases. it is possible that the loss of nox2 activates inflammatory cascades in macrophages in the lesions. roles of nox5 in vascular functions are currently undetermined,owing to the absence of this enzyme in rodents and the limitation of the experimental procedure. thus,it is possible that the nox family of enzymes exhibits heterogeneity in the atherosclerotic diseases. in this aspect,subtype- selective nox inhibitor may be promising when nox systems serve as a molecular target for atherosclerotic and aneurysmal diseases. © 2017 japan atherosclerosis society.
کلیدواژه Abdominal aortic aneurysm; Aortic dissection; Atherosclerosis; Nadph oxidase
آدرس division of endocrinology and metabolism,showa university fujigaoka hospital,yokohama, Japan, department of biochemistry,showa university school of medicine,tokyo, Japan, department of biochemistry,showa university school of medicine,tokyo, Japan, department of biochemistry,showa university school of medicine,tokyo, Japan, department of biochemistry,showa university school of medicine,tokyo, Japan
 
     
   
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