Salem, Sultan A and Allsop, David and Mann, David M A and Tokuda, Takahiko and El-Agnaf, Omar M A (2007) An investigation into the lipid-binding properties of α-, β- and γ-synucleins in human brain and cerebrospinal fluid. Experimental Brain Research, 1170. pp. 103-111.
Full text not available from this repository.Abstract
Parkinson's disease (PD) and dementia with Lewy bodies (DLB) are both characterized by the formation and intraneuronal accumulation of fibrillar aggregates of alpha-synuclein (alpha-syn) protein in affected brain regions. alpha-Syn has biochemical properties and a structural motif characteristic of fatty acid binding proteins. Using the fatty acid binding resin Lipidex-1000, we investigated the capture of alpha-, beta-, and gamma-syn proteins as lipid-associated proteins from normal and DLB brain lysates, and from normal human cerebrospinal fluid (CSF). These were eluted from Lipidex-1000 and analyzed by SDS-NuPAGE followed by Western blotting. Using this methodology, we have been able to extract full-length and truncated forms of alpha-syn from brain lysates. We also extracted low levels of beta-syn from DLB brains, but failed to extract any gamma-syn. We were able to capture only full-length monomeric alpha-syn from normal human CSF. Our data confirm the fatty acid binding properties of alpha-syn, and to a lesser extent beta-syn, but suggest that gamma-syn does not share this same characteristic.
| Item Type: | Article |
|---|---|
| Journal or Publication Title: | Experimental Brain Research |
| Uncontrolled Keywords: | Binding, Competitive ; Brain ; Brain Chemistry ; Cerebrospinal Fluid ; Dextrans ; Electrophoresis, Polyacrylamide Gel ; Humans ; Lewy Body Disease ; Membrane Lipids ; Synucleins ; alpha-Synuclein ; beta-Synuclein ; gamma-Synuclein |
| Subjects: | UNSPECIFIED |
| Departments: | Faculty of Health and Medicine > Biomedical & Life Sciences |
| ID Code: | 50813 |
| Deposited By: | ep_importer_pure |
| Deposited On: | 07 Nov 2011 10:17 |
| Refereed?: | Yes |
| Published?: | Published |
| Last Modified: | 26 Jul 2012 19:43 |
| Identification Number: | |
| URI: | http://eprints.lancs.ac.uk/id/eprint/50813 |
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