Title

Contribution of GSK3 Phosphorylation towards Tau Protein Aggregation

Presenter Information

Katie Czeschin

Department

Chemistry

Major

Biochemistry

Research Advisor

Forciniti, Daniel

Advisor's Department

Chemical and Biochemical Engineering

Funding Source

Missouri S&T Opportunities for Undergraduate Experience Program (OURE)

Abstract

Tau microtubule associated protein is one of the many factors responsible for neuronal structure. When the failure of tau compromises structural integrity, the conditions are referred to as “tauopathies,” resulting in neurodegeneration. This is caused by the hyperphosphorylation and subsequent aggregation of tau, which collapses the scaffold required for microtubule assembly. This research investigated a potential cause of Alzheimer’s disease, a widely recognized tauopathy. Afflicted individuals have been shown to have an overabundance of GSK3 phosphorylating kinase in cerebrospinal fluid, and so it was devised to test the contribution of this kinase activity towards tau aggregation. This would be done by varying environmental factors in vitro, such as oxidation and acetylation. For this OURE, the focus was on isolating tau protein for further study. Tau was extracted from bovine brain, and centrifuged in varying cocktails of microtubule-forming stimulants. Further fractionation was performed on microtubule samples, monitored via BCA assay. The presence of tau could be confirmed by SDS-PAGE, and research continues for final purification.

Biography

Katie is currently a senior in the Chemistry/Biochemistry emphasis program at Missouri S&T. She splits her free time between the research lab, Cycling Club, and her position as Music Director and DJ at KMNR. After harboring the idea for Alzheimer’s research since her freshmen year, she is grateful for the continuing opportunities provided by Missouri S&T and Dr. Daniel Forciniti.

Research Category

Sciences

Presentation Type

Poster Presentation

Document Type

Poster

Location

Upper Atrium/Hall

Presentation Date

16 Apr 2014, 9:00 am - 11:45 am

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Apr 16th, 9:00 AM Apr 16th, 11:45 AM

Contribution of GSK3 Phosphorylation towards Tau Protein Aggregation

Upper Atrium/Hall

Tau microtubule associated protein is one of the many factors responsible for neuronal structure. When the failure of tau compromises structural integrity, the conditions are referred to as “tauopathies,” resulting in neurodegeneration. This is caused by the hyperphosphorylation and subsequent aggregation of tau, which collapses the scaffold required for microtubule assembly. This research investigated a potential cause of Alzheimer’s disease, a widely recognized tauopathy. Afflicted individuals have been shown to have an overabundance of GSK3 phosphorylating kinase in cerebrospinal fluid, and so it was devised to test the contribution of this kinase activity towards tau aggregation. This would be done by varying environmental factors in vitro, such as oxidation and acetylation. For this OURE, the focus was on isolating tau protein for further study. Tau was extracted from bovine brain, and centrifuged in varying cocktails of microtubule-forming stimulants. Further fractionation was performed on microtubule samples, monitored via BCA assay. The presence of tau could be confirmed by SDS-PAGE, and research continues for final purification.