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Novel Alpha-Synuclein Oligomers Formed with the Aminochrome-Glutathione Conjugate Are Not Neurotoxic
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.ORCID-id: 0000-0002-6416-064X
Rekke forfattare: 42019 (engelsk)Inngår i: Neurotoxicity research, ISSN 1029-8428, E-ISSN 1476-3524, Vol. 35, nr 2, s. 432-440Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Aminochrome induces neurotoxic alpha-synuclein oligomer formation relevant to the etiology of Parkinson's disease. Oxidative stress produces aminochrome from dopamine, but conjugation with glutathione catalyzed by glutathione transferase M2-2 significantly decreases aminochrome-induced toxicity and alpha-synuclein oligomer formation. Notably, in the presence of the aminochrome-glutathione conjugate, previously unknown species of alpha-synuclein oligomers are formed. These aminochrome-glutathione oligomers of alpha-synuclein differ from formerly characterized oligomers and (i) have high molecular weight, and are stable and SDS-resistant, as determined by the Western blot method, (ii) show positive NBT-quinone-protein staining, which indicates the formation of alpha-synuclein adducts containing aminochrome. Furthermore, aminochrome-glutathione alpha-synuclein oligomers (iii) have distinctive shape and size, as determined by transmission electron microscopy, and (iv) are not toxic in U373MG cells. In conclusion, glutathione conjugated with aminochrome induces a new type of alpha-synuclein oligomers of a different size and shape, which have no demonstrable toxicity.

sted, utgiver, år, opplag, sider
2019. Vol. 35, nr 2, s. 432-440
Emneord [en]
Alpha-synuclein, Parkinson's disease, Glutathione, Glutathione transferase, Dopamine, Aminochrome, Oligomers
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Identifikatorer
URN: urn:nbn:se:su:diva-165639DOI: 10.1007/s12640-018-9969-0ISI: 000455660400014PubMedID: 30343424OAI: oai:DiVA.org:su-165639DiVA, id: diva2:1287039
Tilgjengelig fra: 2019-02-08 Laget: 2019-02-08 Sist oppdatert: 2019-12-12bibliografisk kontrollert

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