University of Maryland, Baltimore County
Volunteer for Chinmaya Organization for Rural Development (CORD), volunteer for Females Excelling More in Mathematics Engineering and Science (FEMMES) capstone, participant in Women In Science and Engineering (WISE), participant and former executive board member of Association for Women In Science (AWIS), Michigan DNA Day pharmacogenomics lecture.
Our lab tests whether phosphorylation of the cardiac contractile apparatus acts as both an accelerator and a brake for pump performance and whether chronic phosphorylation contributes to heart failure. These ideas are tested using mouse models expressing either a phospho-mimetic or –null substitution at specific phosphorylation sites within contractile proteins. Both structural remodeling and functional performance are studied to determine the impact of these substitutions. Recent work led to a focus on sarcomere- mitochondrial communication and the contribution mitochondrial reactive oxygen species to the development and progression of heart failure caused by a phospho-mimetic substitution in a molecular switch contractile protein. The rationale for this idea is that a critical component of the cardiac contractile apparatus, myosin, uses the majority of mitochondria-derived ATP to drive cardiac pump function. Intuitively, then, impairments in mitochondrial function and subsequent output of reactive oxygen species may play a role in development and progression of heart failure. Indeed, alterations in mitochondrial function (specifically overproduction of reactive oxygen species) are linked to many cardiovascular diseases, including heart failure. Our lab aims to develop a clear understanding of how changes in a sarcomeric protein can trigger changes in mitochondrial redox to potentially cause heart failure.