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When α-synuclein meets its antibody……

Lin Zheng

Antibodies can recognize their respective proteins. Can antibodies also work as inhibitors to restrain the aggregation of abnormally folded proteins into harmful forms?

In this project, I tried to test this immunotherapy hypothesis on the protein α-synuclein, which plays a principle role in Parkinson’s disease and. It has been shown that the accumulation and aggregation of α-synuclein in these neurodegenerative disorders lead to neurodegeneration of the dopamine (a neuron transmitter) producing system leading to loss of muscle control and problems related to the process of thought.

In this study, I investigated the capacity of an antibody specific for α-synuclein, SC-211, to affect α-synuclein levels in a cellular model and tried to understand the molecular mechanism behind this event. I treated cells that overexpressed wild-type human α-synuclein with the antibody SC-211 for 24 hours, and then analyzed the levels of α-synuclein both in the medium and in the cells. Increased α-synuclein levels were observed in antibody treated cells, whereas lower levels were detected in the cell medium under the same treatment conditions. To further understand the mechanisms of immunotherapy, antibodies were visualized when its fluorescent secondary antibody bind on, but unfortunately the results were somewhat inconclusive and I was not able to determine whether the antibody was taken up into cells.

This study will help me to understand more how α-synuclein behaves in the cells and in cell medium, and figure out how α-synuclein antibodies may affect this protein.

Although I can not exactly explain the observed events, the antibody treatment against α-synuclein may provide a new exciting treatment scheme.

Degree project in biology, Master of Science (2 years), 2010 Examensarbete i biologi 30 hp till masterexamen, 2010

Biology Education Center and Molecular Geriatric Department, Uppsala University Supervisors: Charlotte Sahlin, Joakim Bergström

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