Extracellular Superoxide Dismutase with Vaccinia Virus Anti-inflammatory Protein 35K or Tissue Inhibitor of Metalloproteinase-1: Combination Gene Therapy in the Treatment of Vein Graft Stenosis in Rabbits

2006 ◽  
Vol 17 (4) ◽  
pp. 405-414 ◽  
Author(s):  
Päivi Turunen ◽  
Hanna L. Puhakka ◽  
Tommi Heikura ◽  
Elina Romppanen ◽  
Matias Inkala ◽  
...  
Circulation ◽  
2000 ◽  
Vol 101 (3) ◽  
pp. 296-304 ◽  
Author(s):  
Sarah J. George ◽  
Clinton T. Lloyd ◽  
Gianni D. Angelini ◽  
Andrew C. Newby ◽  
Andrew H. Baker

2012 ◽  
Vol 2012 ◽  
pp. 1-9 ◽  
Author(s):  
Tiina Kelkka ◽  
Juha Petteri Laurila ◽  
Outi Sareila ◽  
Peter Olofsson ◽  
Mikko Olavi Laukkanen ◽  
...  

Extracellular superoxide dismutase (SOD3), an enzyme mediating dismutation of superoxide into hydrogen peroxide, has been shown to reduce inflammation by inhibiting macrophage migration into injured tissues. In inflamed tissues, superoxide is produced by the phagocytic NOX2 complex, which consists of the catalytic subunit NOX2 and several regulatory subunits (e.g., NCF1). To analyze whether SOD3 can regulate inflammation in the absence of functional NOX2 complex, we injected an adenoviral vector overexpressing SOD3 directly into the arthritic paws ofNcf1*/*mice with collagen-induced arthritis. SOD3 reduced arthritis severity in both oxidative burst-deficientNcf1*/*mice and also in wild-type mice. The NOX2 complex independent anti-inflammatory effect of SOD3 was further characterized in peritonitis, and SOD3 was found to reduce macrophage infiltration independently of NOX2 complex functionality. We conclude that the SOD3-mediated anti-inflammatory effect on arthritis and peritonitis operates independently of NOX2 complex derived oxidative burst.


Circulation ◽  
2001 ◽  
Vol 103 (14) ◽  
pp. 1893-1898 ◽  
Author(s):  
Qianhong Li ◽  
Roberto Bolli ◽  
Yumin Qiu ◽  
Xian-Liang Tang ◽  
Yiru Guo ◽  
...  

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