Dr. Samantha Harris received her PhD from the University of Michigan, Department of Physiology, in 1995 where she studied epithelial ion transport in the laboratory of Dr. David C. Dawson. She then went on to do a postdoc at the University of Wisconsin, Madison, where she studied muscle physiology in the laboratory of Dr. Richard L. Moss. It was in Dr. Moss’ lab that she began her career-long fascination with the muscle regulatory protein, cardiac myosin binding protein-C (cMyBP-C), and where she characterized the first knockout mouse model of cMyBP-C. Dr. Harris then began her independent career in the Department of Bioengineering at the University of Washington before moving to the University of California, Davis, and finally to the University of Arizona in 2013.

Throughout this time the major research focus of Dr. Harris’ lab has been on how cMyBP-C regulates cardiac contraction during healthy conditions and how mutations in cMyBP-C cause hypertrophic cardiomyopathy (HCM), a disease affecting 1 in 250-500 people that can lead to heart failure or sudden cardiac death.  Recently, mutations in the 2 skeletal muscle paralogs of MyBP-C, expressed predominantly in slow and fast twitch muscles, have also been linked to inherited diseases including distal limb contractures (arthrogryposes) and muscle tremors.

To study cardiac and skeletal MyBP-C Dr. Harris uses a wide variety of approaches ranging from single molecule biophysical and biochemical methods to whole animal models of disease. Methods include atomic force microscopy, biochemical binding and motility assays, ex vivo force measurements in permeabilized contracting muscle, and measurement of whole heart cardiac function in engineered rodent models of disease and in a naturally occurring feline model of HCM with a genetic mutation in cMyBP-C.  Recently Dr. Harris’ lab pioneered a new “cut and paste” approach for replacing MyBP-C in sarcomeres in situ in permeabilized myocytes from gene-edited “Spy-C” mice. The method revealed an unexpected role for MyBP-C in dampening oscillatory contractions that originate from sarcomeres. The discovery has implications for the mechanisms by which cMyBP-C regulates relaxation and potentially for arrhythmogenesis in patients with atrial fibrillation, heart failure or cardiac diseases where cMyBP-C expression is reduced.