title: α-Synuclein-mediated defense against oxidative stress via modulation of glutathione peroxidase.
abstract: In this report, mutual effect of α-synuclein and GPX-1 is investigated to unveil their involvement in the PD pathogenesis in terms of cellular defense mechanism against oxidative stress. Biochemical and immunocytochemical studies showed that α-synuclein enhanced the GPX-1 activity with Kd of 17.3nM and the enzyme in turn markedly enhanced in vitro fibrillation of α-synuclein. Transmission electron microscopy revealed the fibrillar meshwork of α-synuclein containing GPX-1 located in locally concentrated islets. The entrapped enzyme was demonstrated to be protected in a latent form and its activity was fully recovered as released from the matrix. Therefore, novel defensive roles of α-synuclein and its amyloid fibrils against oxidative stress are suggested as the GPX-1 stimulator and the active depot for the enzyme, respectively.
authors.affiliation: School of Chemical and Biological Engineering, Seoul National University, Seoul, Republic of Korea.
authors.forename: Hee Jung
authors.initials: HJ
authors.lastname: Koo
authors.forename: Jee Eun
authors.initials: JE
authors.lastname: Yang
authors.forename: Jae Hyung
authors.initials: JH
authors.lastname: Park
authors.forename: Daekyun
authors.initials: D
authors.lastname: Lee
authors.forename: Seung R
authors.initials: SR
authors.lastname: Paik
mesh_terms: D000682:Amyloid / Q000378:metabolism; D000818:Animals; D000975:Antioxidants / Q000378:metabolism; D002417:Cattle; D005979:Glutathione Peroxidase / Q000378:metabolism*; D006801:Humans; D018384:Oxidative Stress / Q000502:physiology*; D010300:Parkinson Disease / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D051844:alpha-Synuclein / Q000378:metabolism*; D000094765:Glutathione Peroxidase GPX1
chemical_list: D000682:Amyloid; D000975:Antioxidants; D011994:Recombinant Proteins; D051844:alpha-Synuclein; D005979:Glutathione Peroxidase; D000094765:Glutathione Peroxidase GPX1