Kinetics of GSK3 Phosphorylation of Tau Protein
Department
Chemistry
Major
Biochemistry
Research Advisor
Forciniti, Daniel
Advisor's Department
Chemical and Biochemical Engineering
Funding Source
Missouri S& T Opportunities for Undergraduate Research Experiences (OURE) Program
Abstract
Tau microtubule associated protein is one of many factors responsible for neuronal structure. When the failure of tau compromises this 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 will investigate the causes of one of the most widely recognized tauopathies: Alzheimer's disease. Afflicted individuals have an abundance of GSK3, a phosphorylating kinase, in cerebrospinal fluid. It was therefore devised to test the kinetics of phosphorylation with respect to oxidative stress, acetylation, incubation, and time. For this particular OURE, the first stages of what is intended to be a continuing project will be undertaken. Tau will first be extracted from homogenized bovine brain, then separated out via ammonium sulfate fractionation. TEM and SOS-PAGE will be performed to verify the presence of microtubules and tau, respectively.
Biography
Katie is currently a junior in the Chemistry/Biochemistry emphasis program at Missouri University of Science and Technology. She splits her time between the research lab, Cycling Club, Climbing Club, General Delegation of Independents, and her position as Assistant Music Director and DJ at KMNR. After harboring this 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
Oral Presentation
Document Type
Presentation
Award
Sciences poster session, Second place
Location
Upper Atrium/Hallway
Presentation Date
03 Apr 2013, 9:00 am - 11:45 am
Kinetics of GSK3 Phosphorylation of Tau Protein
Upper Atrium/Hallway
Tau microtubule associated protein is one of many factors responsible for neuronal structure. When the failure of tau compromises this 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 will investigate the causes of one of the most widely recognized tauopathies: Alzheimer's disease. Afflicted individuals have an abundance of GSK3, a phosphorylating kinase, in cerebrospinal fluid. It was therefore devised to test the kinetics of phosphorylation with respect to oxidative stress, acetylation, incubation, and time. For this particular OURE, the first stages of what is intended to be a continuing project will be undertaken. Tau will first be extracted from homogenized bovine brain, then separated out via ammonium sulfate fractionation. TEM and SOS-PAGE will be performed to verify the presence of microtubules and tau, respectively.
