UTHSCSA Faculty Profiles v1.0

Pierce, Anson P

Graduate School of Biomedical Sciences
Barshop Institute
(210) 562-6016

Proteins play an essential role in carrying out almost every function within a cell or tissue, and are able to carry out these functions based on their unique three dimensional structures. During disease conditions, protein structures can be altered in multiple ways, which can cause them to lose their function or impart them with toxic properties. In order to keep proteins folded in their proper structures, the cell produces heat shock proteins which can recognize misfolded proteins and properly fold them or direct them to proteolytic pathways. The major transcription factors responsible for expression of chaperones are heat shock factor 1 (HSF1) and HSF2. When levels of unfolded proteins rise in the cell caused by heat or oxidative stress, HSFs become activated and lead to production of more heat shock proteins. Protein unfolding and aggregation are common features of Lou Gehrig`s Disease or amyotrophic lateral sclerosis (ALS) and other neurodegenerative diseases. ALS is characterized by a progressive
loss of
motorneurons and muscle atrophy, which eventually leads to paralysis and death. There is no known cure for this disease, and its cause is unknown. Using mice that overexpress HSFs, I am interested in understanding more about the role of chaperones in ALS and other protein unfolding diseases, and learning more about their role in protecting protein structure.

1/2009 - Present Research Assistant Professor University of Texas Health Science Center at San Antonio, Cellular & Structural Biology, San Antonio, TX
5/2008 - Present Research Health Scientist South Texas Veterans Healthcare System, Research, San Antonio, TX