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Acetylation of tau protein at Lys274 in argyrophilic grain disease and Alzheimer’s disease


Šimić, Goran; Babić Leko, Mirjana; Bažadona, Danira; Benković, Vesna; Boban, Mirta; Borovečki, Fran; Čirko, Antonela; Đikić, Domagoj; Jazvinšćak-Jembrek, Maja; Klepac, Nataša et al.
Acetylation of tau protein at Lys274 in argyrophilic grain disease and Alzheimer’s disease // Book of abstracts of the 10th FENS Forum of Neuroscience
Kopenhagen, Danska, 2016. str. 231-231 (poster, međunarodna recenzija, sažetak, znanstveni)


Naslov
Acetylation of tau protein at Lys274 in argyrophilic grain disease and Alzheimer’s disease

Autori
Šimić, Goran ; Babić Leko, Mirjana ; Bažadona, Danira ; Benković, Vesna ; Boban, Mirta ; Borovečki, Fran ; Čirko, Antonela ; Đikić, Domagoj ; Jazvinšćak-Jembrek, Maja ; Klepac, Nataša ; Oršolić, Nada ; Petelin Gadže, Željka ; Hof, Patrick R.

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
Book of abstracts of the 10th FENS Forum of Neuroscience / - , 2016, 231-231

Skup
10th FENS Forum of Neuroscience

Mjesto i datum
Kopenhagen, Danska, 02-06.07.2016

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
Argyrophilic grain disease ; Alzheimer’s disease ; tau acetylation

Sažetak
Argyrophilic grain disease (AGD) is a common sporadic 4R tauopathy. The term ‘argyrophilic grains’ is derived from their strong staining with the Gallyas silver iodide method, although not all silver methods permit their visualization. In combination with Alzheimer’s disease (AD) or alone, AGD significantly contributes to dementia in older age subjects and alone accounts for about 5% of all dementia cases. By using a novel monoclonal antibody specifically immunoreactive to acetylated tau at Lys274 (MAb 359), it has been shown that acetylation of tau protein is an early change in AD brains, which occurs even before tangles are detectable. Interestingly, AGD differs from AD and other tauopathies by lacking tau acetylation at Lys274. By using MAb 359 developed to detect acetylation at Lys274 (a gift from Dr. Li Gan, Gladstone Institute of Neurological Disease, UCSF) we compared immunohistochemically temporal and entorhinal cortex and the hippocampal formation in an AD brain, a brain with pathological changes of AD and AGD, and a brain with AGD alone. Our detailed analysis confirms and expands previous findings and supports further investigations of tau acetylation as a potential new therapeutic target in AD, AGD, and other tauopathies.

Izvorni jezik
Engleski

Znanstvena područja
Temeljne medicinske znanosti