Rammohan Rao, PhD
Associate Research Professor
Misfolded Proteins and ER stress-induced cell death
Mechanisms of neurodegenerative disease
I am an Associate Research Professor collaborating with Drs. Dale Bredesen and David Greenberg on: Endoplasmic Reticulum stress and neuronal cell death and mechanisms of age-associated neurodegenerative diseases.
Neurodegenerative disorders such as Alzheimer's disease, Parkinson's disease, Huntington's disease, Amyotrophic Lateral Sclerosis (ALS) and prion protein diseases all feature misfolded proteins and their aggregates that appear to play a role in disease pathogenesis. However the mechanism and pathways by which misfolded proteins induce cellular stress response ultimately leading to neuronal cell death is poorly understood. Accumulation of misfolded proteins whether in the cytosol or the endoplasmic reticulum (ER), elicits cellular stress responses that protect cells against toxic buildup of misfolded proteins. Prolonged stress leads to organelle damage and dysfunction and ultimately leads to cell death.
We have been investigating the biochemical pathways that couple misfolded proteins to the cell death programs. These studies have led to the identification of several new proteins that function in this link that therefore represent potential therapeutic targets.
1. Rao RV, Bredesen DE. (2007) Tumor Necrosis Factor (TNF) and Neurodegeneration, 47-65; In: Khare S, Ed. TNF Superfamily. Georgetown: Landes Bioscience/Eurekah.com; New York: Kluwer Academic/Plenum Publishers.
2. Bredesen DE, Rao RV, Mehlen P. (2007) Programmed Cell Death and Its Role in Neurological Disease, 125-144; In: Waxman SG, Ed. Molecular Neurology: Elsevier Academic Press.