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Familial ALS-superoxide dismutases associate with mitochondria and shift their redox potentials

Ferri, Alberto and Cozzolino, Mauro and Crosio, Claudia and Nencini, Monica and Casciati, Arianna and Butler Gralla, Edith and Rotilio, Giuseppe and Valentine, Joan Selverstone and Carrì, Maria Teresa (2006) Familial ALS-superoxide dismutases associate with mitochondria and shift their redox potentials. Proceedings of The National Academy of Sciences, Vol. 103 (37), p. 13860-13865. eISSN 1091-6490. Article.

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DOI: 10.1073/pnas.0605814103


Recent studies suggest that the toxicity of familial amyotrophic lateral sclerosis mutant Cu, Zn superoxide dismutase (SOD1) arises from its selective recruitment to mitochondria. Here we demonstrate that each of 12 different familial ALS-mutant SOD1s with widely differing biophysical properties are associated with mitochondria of motoneuronal cells to a much greater extent than wild-type SOD1, and that this effect may depend on the oxidation of Cys residues. We demonstrate further that mutant SOD1 proteins associated with the mitochondria tend to form cross-linked oligomers and that their presence causes a shift in the redox state of these organelles and results in impairment of respiratory complexes. The observation that such a diverse set of mutant SOD1 proteins behave so similarly in mitochondria of motoneuronal cells and so differently from wild-type SOD1 suggests that this behavior may explain the toxicity of ALS-mutant SOD1 proteins, which causes motor neurons to die.

Item Type:Article
ID Code:1094
Uncontrolled Keywords:Motor neuron, neurodegeneration, amyotrophic lateral sclerosis
Subjects:Area 05 - Scienze biologiche > BIO/11 Biologia molecolare
Divisions:001 Università di Sassari > 01 Dipartimenti > Scienze fisiologiche, biochimiche e cellulari
Publisher:The National Academy of Sciences of the USA
Publisher Policy:Depositato per gentile concessione dell'Editore. È vietato duplicare e postare il PDF. E' consentito l'uso a solo scopo di studio e di ricerca.
Additional Information:Pubblicato online il 30 agosto 2006.
Deposited On:18 Aug 2009 10:04

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