Dr. Kamm’s research at UT Southwestern involves aspects of muscle biology and cell motility. In studies of vascular, airway and visceral smooth muscle she has concentrated on relating mechanical events of contraction and relaxation to the generation of biochemical intermediates that regulate contractility. Smooth muscle contraction and aspects of cell motility such as cytokinesis and locomotion result from the action of the motor protein myosin II on the actin cytoskeleton. Smooth and non-muscle isoforms of myosin II are regulated by phosphorylation of their regulatory light chains, owing in part or whole to the activity of calcium/calmodulin-dependent myosin light chain kinase (MLCK). The activation of MLCK by binding of calcium/calmodulin is assessed by fluorescence resonance energy transfer in tissues from transgenic mice expressing chimeric constructs of MLCK labeled with variants of green fluorescent protein. To determine which aspects of actomyosin-dependent contraction and cell motility require MLCK activity, targeted gene ablation approaches are used. These studies of smooth muscle contraction bear on the pathophysiology of hypertension, asthma and premature labor. In addition, studies of cell migration and division elucidate aspects of the coronary vascular response to injury that leads to restenosis following angioplasty.
