Български
Albanian
Arabic
Armenian
Azerbaijani
Belarusian
Bengali
Bosnian
Catalan
Czech
Danish
Deutsch
Dutch
English
Estonian
Finnish
Français
Greek
Haitian Creole
Hebrew
Hindi
Hungarian
Icelandic
Indonesian
Irish
Italian
Japanese
Korean
Latvian
Lithuanian
Macedonian
Mongolian
Norwegian
Persian
Polish
Portuguese
Romanian
Russian
Serbian
Slovak
Slovenian
Spanish
Swahili
Swedish
Turkish
Ukrainian
Vietnamese
Български
中文(简体)
中文(繁體)
European Journal of Neuroscience 2007-Aug

Oxidative stress-induced phosphorylation, degradation and aggregation of alpha-synuclein are linked to upregulated CK2 and cathepsin D.

Само регистрирани потребители могат да превеждат статии
Вход / Регистрация
Линкът е запазен в клипборда
Makio Takahashi
Li-wen Ko
Jayanarayan Kulathingal
Peizhou Jiang
Daniel Sevlever
Shu-Hui C Yen

Ключови думи

Резюме

Intracellular accumulation of alpha-synuclein (alpha-Syn) as filamentous aggregates is a pathological feature shared by Parkinson's disease, dementia with Lewy bodies and multiple system atrophy, referred to as synucleinopathies. To understand the mechanisms underlying alpha-Syn aggregation, we established a tetracycline-off inducible transfectant (3D5) of neuronal lineage overexpressing human wild-type alpha-Syn. Alpha-Syn aggregation was initiated by exposure of 3D5 cells to FeCl2. The exposure led to formation of alpha-Syn inclusions and oligomers of 34, 54, 68 kDa and higher molecular weights. The oligomers displayed immunoreactivity with antibodies to the amino-, but not to the carboxyl (C)-, terminus of alpha-Syn, indicating that C-terminally truncated alpha-Syn is a major component of oligomers. FeCl2 exposure also promoted accumulation of S129 phosphorylated monomeric alpha-Syn (P alpha-Syn) and casein kinase 2 (CK2); however, G-protein-coupled receptor kinase 2 was reduced. Treatment of FeCl2-exposed cells with CK2 inhibitors (DRB or TBB) led to decreased formation of alpha-Syn inclusions, oligomers and P alpha-Syn. FeCl2 exposure also enhanced the activity/level of cathepsin D. Treatment of the FeCl2-exposed cells with pepstatin A or NH4Cl led to reduced formation of oligomers/inclusions as well as of approximately 10 and 12 kDa truncated alpha-Syn. Our results indicate that alpha-Syn phosphorylation caused by FeCl2 is due to CK2 upregulation, and that lysosomal proteases may have a role in producing truncated alpha-Syn for oligomer assembly.

Присъединете се към нашата
страница във facebook

Най-пълната база данни за лечебни билки, подкрепена от науката

  • Работи на 55 езика
  • Билкови лекове, подкрепени от науката
  • Разпознаване на билки по изображение
  • Интерактивна GPS карта - маркирайте билките на място (очаквайте скоро)
  • Прочетете научни публикации, свързани с вашето търсене
  • Търсете лечебни билки по техните ефекти
  • Организирайте вашите интереси и бъдете в крак с научните статии, клиничните изследвания и патентите

Въведете симптом или болест и прочетете за билките, които биха могли да помогнат, напишете билка и вижте болестите и симптомите, срещу които се използва.
* Цялата информация се базира на публикувани научни изследвания

Google Play badgeApp Store badge