Mitochondrial dysfunction due to mutant copper/zinc superoxide dismutase associated with familial amyotrophic lateral sclerosis is reversed by n-acetyl-cysteine (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Mitochondrial dysfunction due to mutant copper/zinc superoxide dismutase associated with familial amyotrophic lateral sclerosis is reversed by n-acetyl-cysteine (Articolo in rivista) (literal)

Anno

• 2003-01-01T00:00:00+01:00 (literal)

Alternative label

• Beretta S., Sala G., Mattavelli L., Ceresa C., Casciati A., Ferri A., Carrì M.T. and Ferrarese C. (2003)
  Mitochondrial dysfunction due to mutant copper/zinc superoxide dismutase associated with familial amyotrophic lateral sclerosis is reversed by n-acetyl-cysteine
  in Neurobiology of disease
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Beretta S., Sala G., Mattavelli L., Ceresa C., Casciati A., Ferri A., Carrì M.T. and Ferrarese C. (literal)

Pagina inizio

• 213 (literal)

Pagina fine

• 221 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 13 (literal)

Rivista

• Neurobiology of disease (Rivista)

Note

• ISI Web of Science (WOS) (literal)

Titolo

• Mitochondrial dysfunction due to mutant copper/zinc superoxide dismutase associated with familial amyotrophic lateral sclerosis is reversed by n-acetyl-cysteine (literal)

Abstract

• We report that the expression of mutant G93A copper/zinc superoxide dismutase (SOD1), associated with familial amyotrophic lateral sclerosis, specifically causes a decrease in MTT reduction rate and ATP levels and an increase in both cytosolic and mitochondrial reactive oxygen species (ROS) production in human neuroblastoma SH-SY5Y cells compared to cells overexpressing wild-type SOD1 and untransfected cells. Exposure to N-acetylcysteine lowers ROS production and returns mitochondrial functional assays to control levels. No large aggregates of human SOD1 are detectable under basal growth conditions in any of the investigated cell lines. After proteasome activity inhibition, SOD1 aggregates can be detected exclusively in G93A-SOD1 cells, even though they do not per se enhance cell death compared to control cell lines. Our findings indicate that mitochondrial homeostasis is affected by mutant SOD1-generated ROS independently from the formation of aggregates and that this alteration is reversed by antioxidants. (literal)

Prodotto di

• Institute of neuroscience (IN) (Istituto)

Incoming links:

Prodotto

• Institute of neuroscience (IN) (Istituto)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Neurobiology of disease (Rivista)