Proteasomes remain intact, but show early focal alteration in their composition in a mouse model of amyotrophic lateral sclerosis

In amyotrophic lateral sclerosis caused by mutations in Cu/Zn-superoxide dismutase (SOD1), altered solubility and aggregation of the mutant protein implicates failure of pathways for detecting and catabolizing misfolded proteins. Our previous studies demonstrated early reduction of proteasome-mediat...

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Veröffentlicht in:	Journal of neurochemistry 2008-06, Vol.105 (6), p.2353-2366
Hauptverfasser:	Kabashi, Edor, Agar, Jeffrey N, Hong, Yu, Taylor, David M, Minotti, Sandra, Figlewicz, Denise A, Durham, Heather D
Format:	Artikel
Sprache:	eng
Schlagworte:	Alanine - genetics Amyotrophic lateral sclerosis Amyotrophic Lateral Sclerosis - enzymology Amyotrophic Lateral Sclerosis - genetics Amyotrophic Lateral Sclerosis - pathology Animals Biochemistry Biological and medical sciences Cerebrospinal fluid. Meninges. Spinal cord Cu/Zn-superoxide dismutase Cu/Zn-superoxide dismutase 1 Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases Disease Models, Animal Glycine - genetics Humans Medical sciences Mice Mice, Transgenic motor neuron disease Mutation Nervous system (semeiology, syndromes) Neurology Proteasome Endopeptidase Complex - genetics Proteasome Endopeptidase Complex - metabolism protein aggregates protein aggregation Protein folding proteolysis Rodents Spinal Cord - enzymology Spinal Cord - pathology Superoxide Dismutase - genetics Superoxide Dismutase - metabolism ubiquitin-proteasome pathway Ubiquitination
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