Title : Role of protein aggregation in neurodegenerative diseases; Investigating cellular mechanism of Parkinson’s disease in iPSC model
Abstract:
Misfolding and aggregation of proteins such as amyloid-β (Aβ), tau and alpha-synuclein (?-syn) is the predominant pathology underlying the neurodegenerative disorders, Alzheimer’s disease (AD) and Parkinson’s disease (PD). Although end stage insoluble products of aggregates are the key pathological hallmark of the diseases, there is accumulating evidence that the soluble oligomeric forms of aggregates may be the key toxic species involved in disease. However, the initial triggers to form the early aggregates inside cells are unknown due to the inability to detect the soluble intermediates (oligomers) within the cells. Here we are able to trace the dynamic process of aggregation in human iPSC derived neurons by utilizing Foster Resonance Energy Transfer (FRET) based method that enables to visualize the kinetics of intracellular oligomerization track.
Audience Take Away:
- Explain how the audience will be able to use what they learn?
- How will this help the audience in their job? Is this research that other faculty could use to expand their research or teaching? Does this provide a practical solution to a problem that could simplify or make a designer’s job more efficient? Will it improve the accuracy of a design, or provide new information to assist in a design problem? List all other benefits.
- I will introduce a new method/technology to trace protein aggregation in cells so audience can adapt the methods for their research. I will also tell about human cell model of neurodegenerative disease and how to study by using it. Taken together, audience will learn new method to study progress of protein aggregation in neurodegenerative diseases molecular mechanism of Parkinson’s disease and Lewybody dementia and human iPSC derived cell model (astrocytes, neurons).
