| 1. |
|
|
| 2. |
- Ulusoy, Ayse, et al.
(author)
-
Co-expression of C-terminal truncated alpha-synuclein enhances full-length alpha-synuclein-induced pathology.
- 2010
-
In: European Journal of Neuroscience. - : Wiley. - 1460-9568 .- 0953-816X. ; 32:3, s. 409-422
-
Journal article (peer-reviewed)abstract
- Lewy bodies, which are a pathological hallmark of Parkinson's disease, contain insoluble polymers of alpha-synuclein (alphasyn). Among the different modifications that can promote the formation of toxic alphasyn species, C-terminal truncation is among the most abundant alterations in patients with Parkinson's disease. In vitro, C-terminal truncated alphasyn aggregates faster and sub-stoichiometric amounts of C-terminal truncated alphasyn promote aggregation of the full-length alphasyn (alphasynFL) and induce neuronal toxicity. To address in vivo the putative stimulation of alphasyn-induced pathology by the presence of truncated alphasyn, we used recombinant adeno-associated virus to express either alphasynFL or a C-terminal truncated alphasyn (1-110) in rats. We adjusted the recombinant adeno-associated virus vector concentrations so that either protein alone led to only mild to moderate axonal pathology in the terminals of nigrostriatal dopamine neurons without frank cell loss. When these two forms of alphasyn were co-expressed at these pre-determined levels, it resulted in a more aggressive pathology in fiber terminals as well as dopaminergic cell loss in the substantia nigra. Using an antibody that did not detect the C-terminal truncated alphasyn (1-110) but only alphasynFL, we demonstrated that the co-expressed truncated protein promoted the progressive accumulation of alphasynFL and formation of larger pathological accumulations. Moreover, in the co-expression group, three of the eight animals showed apomorphine-induced turning, suggesting prominent post-synaptic alterations due to impairments in the dopamine release, whereas the mild pathology induced by either form alone did not cause motor abnormalities. Taken together these data suggest that C-terminal truncated alphasyn can interact with and exacerbate the formation of pathological accumulations containing alphasynFL in vivo.
|
|
| 3. |
- Ulusoy, Inan, et al.
(author)
-
Multisource geophysical investigation of the Acıgöl caldera structure (central Turkey): preliminary results
- 2009
-
In: ; , s. 7746-7746
-
Conference paper (peer-reviewed)abstract
- Neogene and Quaternary volcanic activity formed the large volume ignimbritic units (about 10 different units, namely Cappadocian ignimbritic field) around Nevşehir, Derinkuyu and Acıgöl districts. These large volume ignimbrites are mostly caldera-related products but the calderas are partially or totally buried by later pyroclastic and sedimentary cover. Source estimations for the caldera-related pyroclastics in Nevşehir plateau indicate that the calderas concentrate around Derinkuyu and Acıgöl plains. Geophysical methods (resistivity imaging, self-potential, TDEM and magnetic surveys) were applied around Acıgöl plain and Mt. Erdaş to reveal out the near-surface structural elements related to the Acıgöl caldera system. Additionally, remote sensing coupled with morphology was used. Preliminary results show that the Acıgöl caldera complex may have an elongated shape. Possible structural models for the caldera system/complex are explained. Future geophysical studies and a detailed study of the geological relationship between the caldera-related products are necessary to better understand the Acıgöl caldera system.
|
|
