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2008 Grants - Iijima
Mechanisms of Tau Phosphorylation and Toxicity Induced by Abeta42 In Vivo
Koichi Iijima, Ph.D.
Thomas Jefferson University
2008 New investigator Research Grant
The protein tau and the protein fragment beta-amyloid (also known as Abeta) are at the focus of research on Alzheimer's disease. Tau normally helps support cell structures, but tau that has undergone abnormal chemical modification by the addition of phosphate groups (phosphorylation) is the main constituent of neurofibrillary tangles, one of the hallmark features of Alzheimer pathology. Beta-amyloid aggregates into amyloid plaque, the other hallmark of Alzheimer pathology. The molecular mechanisms that link production of beta-amyloid to phosphorylation of tau are not well understood.
Koichi Iijima, Ph.D., and colleagues are studying the links between beta-amyloid and tau phosphorylation. Their model system is the fruit fly Drosophila, which is a commonly used model for genetic studies. Dr. Iijima and colleagues have genetically engineered flies that express beta-amyloid and tau. In this model system, they have observed that expression of beta-amyloid leads to phosphorylation of tau.
Using their genetically modified model system, the researchers plan to identify the enzymes responsible for beta-amyloid-stimulated phosphorylation of tau. They also plan to study how such phosphorylation may cause tau to become toxic to nerve cells. These studies may reveal some of the most fundamental mechanisms causing neurodegeneration in Alzheimer's disease and potential targets for the development of new therapies for the disease.