Our laboratory develops mass spectrometry and computational techniques to understand the mechanisms driving disease progression in humans. Our current research focuses include protein dynamics, protein alternative isoform, and protein annotation methods.
ER STRESS IN CARDIAC REMODELING
The integrity of cellular proteins must be constantly regulated to maintain cellular functions. Endoplasmic reticulum (ER) stress occurs when protein homeostasis is disrupted, and induces potent response pathways to restore protein folding and homeostasis. Evidence now implicates ER stress as a central feature in diseases including cardiac hypertrophy and failure, but details of how ER stress quantitatively impacts on protein expression, dynamics, and signaling are poorly understood. Our laboratory employs multidimensional proteomics techniques to define the global proteostatic landscape of the cardiac proteome and how they are dysregulated during ER stress in diseases.
DIFFERENTIAL ALTERNATIV?E ISOFORM IN THE CARDIAC PROTEOME
Alternative splicing allows eukaryotes to produce a diverse proteome from a genome of limited size, by enabling multiple protein isoforms to be encoded in a single gene. Differential expression of alternative isoforms is common in human diseases from cancer to heart failure. Current knowledge remains poor on the functional consequences of alternative protein isoforms. Our goal is to develop new multi-omics strategies by integrating RNA-seq and shotgun proteomics approaches to determine the differential expression in the cardiac proteome.