Established in 1993, my lab is interested in the regulation and structure-function relationships of contractile and cytoskeleton proteins.
Muscle (cardiac, skeletal and smooth) contraction and non-muscle cell motility play vital roles in physiological activities and pathological conditions. Our research is focused on actin thin filament-associated regulatory proteins: troponin and calponin, to study their regulation and structure-function relationships. Molecular biology and genetic approaches are used to investigate protein isoform evolution and expression as well as to provide engineered protein constructs for functional characterization. Biochemical, biophysical and immunochemical methods are used in studying protein structure and function. Cell culture systems and transgenic/gene knock-out/knock-in mouse models are developed for integrative functional characterizations at cellular, organ and whole animal levels.
On going projects:
a) Regulation and function of troponin T isoforms: Biochemical and biophysical studies are performed to investigate the functional significance of various troponin T isoforms in the Ca2+-regulation of cardiac and skeletal muscle contraction and diseases. The studies are focused on the abnormal cardiac troponin T splicing variants found in dilated cardiomyopathy and a slow skeletal muscle troponin T mutation that causes a lethal type of nemaline myopathy. This line of study is currently funded by NIH grants R01HL078773 and R01AR048816.
b) Post-translational regulation of troponin during muscle adaptation and diseases: Proteolytic modification of troponin I and troponin T is studied for functional significance and therapeutic values in the Ca2+-regulation of myocardial contraction in adaptation to hemodynamic stresses, myocardial ischemia-reperfusion injury, heart failure, and skeletal muscle fatigue. This line of study is currently funded by NIH grant R01HL098945 and a Group Incubator Grant from WSU Office of Vice President for Research.
c) Mechanical tension regulation and function of calponin: To study calponin's function as a troponin analog in smooth muscle and non-muscle cells, we are investigating their role in the fine-tuning of smooth muscle contractility, non-muscle motility, and the function of actin cytoskeleton during development, tissue remodeling and cytokinesis. The study is focused on mechanical tension regulated calponin gene expression and protein degradation in epithelial, endothelial, fibroblast, macrophages and smooth muscle cells. This line of study is currently funded by NIH grant R01HL086720.