http://www.cnr.it/ontology/cnr/individuo/prodotto/ID175838
The reaction of alpha-synuclein with tyrosinase: possible implications for Parkinson disease (Articolo in rivista)
- Type
- Label
- The reaction of alpha-synuclein with tyrosinase: possible implications for Parkinson disease (Articolo in rivista) (literal)
- Anno
- 2008-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1074/jbc.M709014200 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Isabella Tessari; (1) Marco Bisaglia (1); Francesco Valle (2); Bruno Samorì (2); Elisabetta Bergantino (1); Stefano Mammi (3); Luigi Bubacco (1) (literal)
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- Rivista
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- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- (1) Dipartimento di Biologia, Università di Padova
(2) Dipartimento di Biochimica, Università di Bologna \"Alma Mater Studiorum\"
(3) Dipartimento di Scienze Chimiche, Università di Padova (literal)
- Titolo
- The reaction of alpha-synuclein with tyrosinase: possible implications for Parkinson disease (literal)
- Abstract
- Oxidative stress appears to be directly involved in the pathogenesis of Parkinson disease. Several different pathways have been identified for the production of oxidative stress conditions in nigral dopaminergic neurons, including a pathological accumulation of cytosolic dopamine with the subsequent production of toxic reactive oxygen species or the formation of highly reactive quinone species. On these premises, tyrosinase, a key copper enzyme known for its role in the synthesis of melanin in skin and hair, has been proposed to take part in the oxidative chemistry related to Parkinson disease. A study is herein presented of the in vitro reactivity of tyrosinase with ?-synuclein, aimed at defining the molecular basis of their synergistic toxic effect. The results presented here indicate that, in conformity with the stringent specificity of tyrosinase, the exposed tyrosine side-chains are the reactive centers of ?-synuclein. The reactivity of ?-synuclein depends on whether it is free or membrane bound, and the chemical modifications on the tyrosinase-treated ?-synuclein strongly influence its aggregation properties. On the basis of our results, we propose a cytotoxic model which includes a possible new toxic role for ?-synuclein exacerbated by its direct chemical modification by tyrosinase. (literal)
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