Several point mutations in the gene coding for human Cu,Zn superoxide dismutase have been reported as being responsible for familial amyotrophic lateral sclerosis (FALS). However, no direct demonstration has been provided for a correlation between total superoxide dismutase activity and severity of the FALS pathology. In order to get a better insight into the mechanism(s) underlying the FALS phenotype, we have investigated the activity and the copper binding properties of the single mutant H46R, which is associated with a Japanese form of FALS. We have shown that this mutant is structurally stable but lacks significant enzyme activity and has impaired capability of binding catalytic copper. The mutant protein can be fully reconstituted with copper in vitro but its ESR spectrum displays an axial shape quite different from that of the wild-type.

Carri', M.t., Battistoni, A., Polizio, F., Desideri, A., Rotilio, G. (1994). Impaired copper binding by the H46R mutant of human Cu,Zn superoxide dismutase, involved in amyotrophic lateral sclerosis. FEBS LETTERS, 356, 314-316 [10.1016/0014-5793(94)01295-4].

Impaired copper binding by the H46R mutant of human Cu,Zn superoxide dismutase, involved in amyotrophic lateral sclerosis

CARRI', MARIA TERESA;BATTISTONI, ANDREA;POLIZIO, FRANCESCA;DESIDERI, ALESSANDRO;ROTILIO, GIUSEPPE
1994-01-01

Abstract

Several point mutations in the gene coding for human Cu,Zn superoxide dismutase have been reported as being responsible for familial amyotrophic lateral sclerosis (FALS). However, no direct demonstration has been provided for a correlation between total superoxide dismutase activity and severity of the FALS pathology. In order to get a better insight into the mechanism(s) underlying the FALS phenotype, we have investigated the activity and the copper binding properties of the single mutant H46R, which is associated with a Japanese form of FALS. We have shown that this mutant is structurally stable but lacks significant enzyme activity and has impaired capability of binding catalytic copper. The mutant protein can be fully reconstituted with copper in vitro but its ESR spectrum displays an axial shape quite different from that of the wild-type.
1994
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/10 - BIOCHIMICA
English
Con Impact Factor ISI
Amyotrophic lateral sclerosis; Cu,Zn superoxide dismutase; Oxidative damage
Carri', M.t., Battistoni, A., Polizio, F., Desideri, A., Rotilio, G. (1994). Impaired copper binding by the H46R mutant of human Cu,Zn superoxide dismutase, involved in amyotrophic lateral sclerosis. FEBS LETTERS, 356, 314-316 [10.1016/0014-5793(94)01295-4].
Carri', Mt; Battistoni, A; Polizio, F; Desideri, A; Rotilio, G
Articolo su rivista
File in questo prodotto:
File Dimensione Formato  
Febs 1994 Carri.pdf

solo utenti autorizzati

Licenza: Creative commons
Dimensione 437.66 kB
Formato Adobe PDF
437.66 kB Adobe PDF   Visualizza/Apri   Richiedi una copia

Questo articolo è pubblicato sotto una Licenza Licenza Creative Commons Creative Commons

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/55157
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 78
  • ???jsp.display-item.citation.isi??? 80
social impact