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JCI table of contents: Jan. 24, 2008
Date:1/24/2008

x known as Rac1, as concentrations of superoxide and the product to which it is converted, hydrogen peroxide, increased SOD1 dissociated from Rac1 and Nox stopped making superoxide. However, mutant forms of SOD1 found in individuals with ALS never dissociated from Rac1 and so Nox never stopped making superoxide. Treating mice that develop an ALS-like disease because they have been engineered to express an ALS-associated mutant form of SOD1 with the inhibitor of Nox apocynin decreased disease and increased their lifespan. However, as discussed in an accompanying commentary by Sverine Boille and Don Cleveland from the University of California at San Diego, there are several questions that need to be addressed before the potential of apocynin as a human therapeutic can be determined.

TITLE: SOD1 mutations disrupt redox-sensitive Rac regulation of NADPH oxidase in a familial ALS model

AUTHOR CONTACT:
John F. Engelhardt
Carver College of Medicine, University of Iowa, Iowa City, Iowa, USA.
Phone: (319) 335-7744; Fax: (319) 335-6581; E-mail: john-engelhardt@uiowa.edu.

MEDIA CONTACT:
Jennifer Brown
Health Science Relations, University of Iowa, Iowa City, Iowa, USA.
Phone: (319) 335-9917; Fax: (319) 384-4638; E-mail: jennifer-l-brown@uiowa.edu.

View the PDF of this article at: https://www.the-jci.org/article.php?id=34060

ACCOMPANYING COMMENTARY TITLE: Revisiting oxidative damage in ALS: microglia, Nox, and mutant SOD1

AUTHOR CONTACT:
Don W. Cleveland
University of California at San Diego, La Jolla, California, USA.
Phone: (858) 534-7811; Fax: (858) 534-7659; E-mail: dcleveland@ucsd.edu.

View the PDF of this article at: htt
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Contact: Karen Honey
press_releases@the-jci.org
215-573-1850
Journal of Clinical Investigation
Source:Eurekalert

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