Milly Rao
About the Students
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Training
| Degree: | BSc. in Biology |
| Institution: | University of Washington, Seattle, USA |
Current Position
| Position: | MSc. in Dr. Marzban’s lab in the Faculty of Pharmaceutical Sciences at the University of British Columbia |
Scholarships + Awards
| Name: | CIHR Training Program In Transplantation |
| Period: | 2009-2011 |
| Name: | Graduate Entrance Scholarship |
| Period: | 2009 |
| Name: | Faculty of Pharmaceutical Sciences Graduate Award |
| Period: | 2009 |
| Name: | International Partial Tuition Scholarship |
| Period: | 2009 |
| Name: | Summer Studentship |
| Period: | June 2009-August 2009 |
About The Research
Research of Interest
Progressive beta-cell dysfunction and death result in insulin deficiency in type 2 diabetes (T2D). Islet amyloid, formed by fibrillogenesis of a small peptide named islet amyloid polypeptide (IAPP) has been shown to contribute to the progressive beta-cell death in T2D. Amyloid formation is not only found in T2D but also in cultured and transplanted islets into type 1 diabetes (T1D) patients.
Growing evidence suggests that amyloid fibrils kill beta-cells by triggering the apoptotic pathway(s). Caspase (casp)-3 is a major downstream enzyme in the two major apoptotic pathways named extrinsic and intrinsic pathways. Fas is an upstream transmembrane cell death receptor in the extrinsic apoptotic pathway which activates downstream caspases to fulfill programmed cell death through interaction with its ligand. In the extrinsic pathway casp-3 is activated by the upstream enzyme casp-8 whereas in the intrinsic pathway casp-3 is activated by the upstream enzyme casp-9. Studies have shown that in certain conditions there is an overlap between these two pathways through the activation of casp-9 by casp-8.
Thus, we think that both pathways may be involved in hIAPP-induced apoptosis. For the MSc. project, I will be using transformed beta-cell lines and isolated mouse islets to examine the role of Fas-associated (extrinsic) and intrinsic apoptotic pathways in mediating the amyloid-induced beta-cell death in conditions associated with islet amyloid formation.
Publications + Presentations
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