DJ-1 can form β-sheet structured aggregates that co-localize with pathological amyloid deposits | Zendy

Katalin Solti | Zendy; WeiLi Kuan | Zendy; Balázs Fórizs | Zendy; Gergely Kustos | Zendy; Judith Mihály | Zendy; Zoltán Varga | Zendy; Balàzs Herberth | Zendy; Éva Moravcsik | Zendy; Róbert Kiss | Zendy; Manuéla Kárpáti | Zendy; A Mikeś | Zendy; Yanyan Zhao | Zendy; Tímea Imre | Zendy; JeanChristophe Rochet | Zendy; Franklin I. Aigbirhio | Zendy; Caroline H. WilliamsGray | Zendy; Roger A. Barker | Zendy; Gergely Tóth | Zendy

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DJ-1 can form β-sheet structured aggregates that co-localize with pathological amyloid deposits

Author(s) -

Katalin Solti,

WeiLi Kuan,

Balázs Fórizs,

Gergely Kustos,

Judith Mihály,

Zoltán Varga,

Balàzs Herberth,

Éva Moravcsik,

Róbert Kiss,

Manuéla Kárpáti,

A Mikeś,

Yanyan Zhao,

Tímea Imre,

JeanChristophe Rochet,

Franklin I. Aigbirhio,

Caroline H. WilliamsGray,

Roger A. Barker,

Gergely Tóth

Publication year - 2019

Publication title -

neurobiology of disease

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.205

H-Index - 166

eISSN - 1095-953X

pISSN - 0969-9961

DOI - 10.1016/j.nbd.2019.104629

Subject(s) - protein aggregation , chemistry , pathological , loss function , amyloid (mycology) , parkinson's disease , pathology , microbiology and biotechnology , neuroscience , biophysics , disease , medicine , biology , biochemistry , phenotype , gene

The loss of native function of the DJ-1 protein has been linked to the development of Parkinson's (PD) and other neurodegenerative diseases. Here we show that DJ-1 aggregates into β-sheet structured soluble and fibrillar aggregates in vitro under physiological conditions and that this process is promoted by the oxidation of its catalytic Cys106 residue. This aggregation resulted in the loss of its native biochemical glyoxalase function and in addition oxidized DJ-1 aggregates were observed to localize within Lewy bodies, neurofibrillary tangles and amyloid plaques in human PD and Alzheimer's (AD) patients' post-mortem brain tissue. These findings suggest that the aggregation of DJ-1 may be a critical player in the development of the pathology of PD and AD and demonstrate that loss of DJ-1 function can happen through DJ-1 aggregation. This could then contribute to AD and PD disease onset and progression. ABBREVIATIONS.

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