"By applying to the University of Scholars Program I hoped to gain a deeper understanding of basic translational science and the research process. Over the next year my goals are to present my research at a professional conference and to complete my senior thesis. Furthermore I hope to learn skills that will prepare me to conduct research during medical school."
Molecular biology, biochemistry, and muscle atrophy.
Academic and Other Awards
- University Scholars Program Scholarship (2011-2012)
- Anderson Scholar of High Distinction
- Phi Delta Theta
- Student Senate
Camp Boggy Creek, TopSoccer, and Shands Hospital Ronald McDonald House.
Hobbies and Interests
- Playing basketball, golfing, experiencing new things, and socializing.
Effect of Hsp70 on Muscle Atrophy
Heat shock protein (Hsp70) belongs to a family of proteins called heat shock proteins and is found in virtually all cells of all living animals. Hsp70 is a cytoprotective protein whose expression is directly related to an increase in temperature as well as a variety of other stressors. Hsp70 is dramatically up regulated in response to stressors and has been shown to protect cells during these periods of strain. However, Hsp70 is actually down regulated in skeletal muscle during periods of inactivity, or disuse. Consequently, scientists have hypothesized that this down regulation may contribute to the muscle atrophy associated with muscle disuse. However, no work has directly tested this hypothesis. Under the guidance of Dr. Judge and his lab I will compare the size of muscle cells from “normal” control mice to the size of muscle cells from Hsp70 knockout mice. If the muscle cells are smaller in the Hsp70 knockout mice this would be clear evidence that a lack of Hsp70 causes muscle atrophy. I will also subject control and Hsp70 knockout mice to a period of muscle disuse to determine whether a lack of Hsp70 potentiates disuse muscle atrophy. To do this I will place a plaster cast around the hind limbs of mice for 7 days, which Dr. Judge’s lab has shown causes an approximate 35% decrease in muscle cell size in control mice. If the decrease in muscle cell size is greater in the Hsp70 knockout mice this will be evidence that a lack of Hsp70 potentiates disuse muscle atrophy. This work is important because if I identify that Hsp70 directly regulates muscle size then specific drugs that target Hsp70 can be tested as therapeutic countermeasures to muscle atrophy.