Superoxide dismutase-1 and other proteins in inclusions from transgenic amyotrophic lateral sclerosis model mice
Article first published online: 19 APR 2010
© 2010 The Authors. Journal Compilation © 2010 International Society for Neurochemistry
Journal of Neurochemistry
Volume 114, Issue 2, pages 408–418, July 2010
How to Cite
Bergemalm, D., Forsberg, K., Srivastava, V., Graffmo, K. S., Andersen, P. M., Brännström, T., Wingsle, G. and Marklund, S. L. (2010), Superoxide dismutase-1 and other proteins in inclusions from transgenic amyotrophic lateral sclerosis model mice. Journal of Neurochemistry, 114: 408–418. doi: 10.1111/j.1471-4159.2010.06753.x
- Issue published online: 22 JUN 2010
- Article first published online: 19 APR 2010
- Received December 21, 2009; revised manuscript received March 13, 2010; accepted April 12, 2010.
Appendix S1. Supplementary Materials and methods.
Figure S1. Human SOD1-immunoreactive inclusions. Human SOD1 inclusions in spinal ventral horns from an ALS patient and a transgenic mouse carrying the G127X mutation are here shown as examples. *denotes nuclei in motor neurons with abundant hSOD1 inclusions. The streaks of dots represent inclusions in axons and dendrites. The abundance of inclusions in the neuropil (area outside cell bodies: interstitium, neurites and glial processes) is generally greater in transgenic mice than in human ALS cases. The G127X patient was described in Jonsson et al. Ann. Neurol. 63, 2008, 675. The scale bars indicate 20 μm.
Figure S2. A spinal cord homogenate from a pre-symptomatic D90A (100 days) transgenic mouse was subjected to density-gradient ultracentrifugation. Mutant hSOD1 was detected by immunoblotting (IB). For detection of mutant hSOD1 aggregates, fractions were filter-trapped in a dot-blot apparatus. For discrimination between C57-C146 disulfide-oxidized (arrow) and reduced hSOD1 (arrowhead), reducing agent was omitted from the immunoblot sample buffer. SE = short exposure of the blot.
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