Research articleUbiquitin-positive inclusion in anterior horn cells in subgroups of motor neuron diseases: A comparative study of adult-onset amyotrophic lateral sclerosis, juvenile amyotrophic lateral sclerosis and werdnig-hoffmann disease
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Lactate dyscrasia: A novel explanation for amyotrophic lateral sclerosis
2012, Neurobiology of AgingCitation Excerpt :In addition to the loss of neurons, various types of inclusion bodies have been identified in degenerating neurons and surrounding reactive astrocytes and are well demonstrated hallmarks of ALS (Barbeito et al., 2004). Ubiquitinated inclusions found in lower motoneurons of the spinal cord and brainstem are the most common and specific type of inclusion in ALS (Matsumoto et al., 1993) and in corticospinal upper motoneurons (Sasaki and Maruyama, 1994). The exact composition of such inclusions, classified as “Lewy body-like inclusions”, “Skein-like inclusions” (He and Hays, 2004; Kawashima et al., 1998), and Bunina bodies (Wada et al., 1999) is not known.
The ubiquitin proteasome system in neurodegenerative diseases: Culprit, accomplice or victim?
2012, Progress in NeurobiologyCitation Excerpt :Disease progression is rapid since life expectancy is only 2–3 years after diagnosis. In the brain, ubiquitin-positive skein-like inclusions can be observed (Matsumoto et al., 1993). Despite of the fact that different brain areas are affected ALS shows many similarities with spectrum of FTD.
Chapter 5 Cytopathology of the motor neuron
2007, Handbook of Clinical NeurologyAlsin, the Product of ALS2 Gene, Suppresses SOD1 Mutant Neurotoxicity through RhoGEF Domain by Interacting with SOD1 Mutants
2004, Journal of Biological ChemistryCitation Excerpt :Alsin LF Does Not Affect Ubiquitination of Mutant SOD1—One of the pathological hallmarks of ALS is the presence of the inclusion bodies, which consist of aggregated, ubiquitinated proteins, in surviving motor neurons in both sporadic and familial ALS (28). It has been reported that when wtSOD1 or mutant SOD1 is transiently overexpressed with ubiquitin, only mutant SOD1 is co-immunoprecipitated with poly-ubiquitin (29). In addition, a novel centrosomal ring finger protein, Dorfin (double ring-finger protein), which exhibits ubiquitin-protein isopeptide ligase activity, ubiquitinates mutant SOD1 and reduces mutant SOD1 neurotoxicity (5, 23).
Aberrant glycosylation/phosphorylation in chromatolytic motoneurons of Werdnig-Hoffmann disease
1997, Journal of the Neurological Sciences