Key result
Active muscle exhibits time-dependent spring properties explained by interactions between spring elements and cycling cross bridges, with a potential role for the giant protein titin.
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Design
Review
Informs models of muscle elasticity in exercise; leaves open titin modulation for cardiac therapies pending validation.
During active lengthening and shortening, muscles exhibit a variety of time-dependent spring properties, including load-dependent and nonlinear stiffness. These properties can be explained as interactions between a spring element and cycling cross bridges within muscle sarcomeres. Several lines of evidence suggest a role for the giant protein titin in active muscle, but specific mechanisms remain to be elucidated.
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Monroy et al. (2007) reported a review. Active muscle exhibits time-dependent spring properties explained by interactions between spring elements and cycling cross bridges, with a potential role for the giant protein titin.
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