Overexpressed mutant G93A superoxide dismutase protects calcineurin from inactivation.
Previous studies have claimed that there is a failure of a mutant form of superoxide dismutase (mSOD) to protect the protein phosphatase, calcineurin (CN), against inactivation in the pathogenesis of amyotrophic lateral sclerosis (ALS), as determined in a murine model of ALS resulting from overexpression of mSOD (G93A). In contrast to previous studies, we find that mice overexpressing G93A mSOD have no statistically significant differences in the expression, or activity, of CN. However, CN from G93A mSOD overexpressing mice is significantly more protected against inactivation than non-transgenic mice that do not overexpress SOD. This reduced inactivation of CN is a consequence of increased expression of G93A mSOD. Thus, like wild-type SOD, G93A mSOD protects CN against inactivation.
Li
Shipeng
S
Laboratory of Biochemistry, National Cancer Institute, NIH, Bethesda, MD 20892-4255, USA.
Wang
Xutong
X
Klee
Claude B
CB
Krieger
Charles
C
D000690:Amyotrophic Lateral Sclerosis / Q000235:genetics / Q000378:metabolism* / Q000503:physiopathology; D000818:Animals; D019703:Calcineurin / Q000378:metabolism*; D006801:Humans; D051379:Mice; D008822:Mice, Transgenic; D017354:Point Mutation; D013482:Superoxide Dismutase / Q000235:genetics* / Q000378:metabolism*
D013482:Superoxide Dismutase; D019703:Calcineurin