\u201cMutations in titin are responsible for many cardiac diseases such as cardiomyopathy and muscle diseases such as muscular dystrophy, yet the underlying causes of these mutations remain largely unexplained,\u201d Nishikawa said. \u201cTitin is the largest known protein, but it\u2019s a very compliant spring-like protein. For titin to contribute to active force production, a mechanism is needed to increase titin stiffness. Our studies suggest that calcium-dependent binding of titin to actin provides the mechanism.\u201d<\/p>\n
Using an atomic force microscope, dynamic force spectroscopy, co-sedimentation assays and\u00a0in vitro<\/em> motility assays, Nishikawa and her team\u2014including associate professor of mechanical engineering Brent Nelson<\/strong>, postdoctoral scholar Samrat Dutta<\/strong> and collaborators at the University of Massachusetts Lowell\u2014conducted multiple experiments to determine how titin interacts with actin when calcium is present and how this interaction might contribute to muscle elasticity. As a result of this study, they believe titin plays a regulatory role in muscle contraction.<\/p>\n Nishikawa\u2019s research is supported by the W. M. Keck Foundation and the Technology Research Initiative Fund at NAU. Awarded a highly prestigious $1 million grant by the Keck Foundation in 2014\u2014one of only six medical research grants awarded that year\u2014Nishikawa leads the Muscle and Motor Control Laboratory, a transdisciplinary group of scientists and engineers who study muscles from molecules to movement. The team has produced many new and exciting ideas about the fundamental principles of muscle physiology and applied these ideas to the control of wearable assistive devices, including prostheses and exoskeletons.<\/p>\n <\/p>\n
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