Rapid unloading experiments from Ttn112-158 muscles

Evidence suggests that the giant muscle protein, titin, functions as a tunable spring in active muscle. However, the mechanisms for increasing titin stiffness with activation are not well understood. Previous studies have suggested that during muscle activation, titin binds to actin which engages the PEVK region of titin thereby increasing titin stiffness. In this study, we investigated the role of PEVK titin in active muscle stiffness during rapid unloading. We measured elastic recoil of active and passive soleus muscles from Ttn112-158 mice characterized by a 75% deletion of PEVK titin and increased passive stiffness. We hypothesized that activated Ttn112-158 muscles are stiffer than wild-type muscles as a result of the increased stiffness of PEVK titin. Using a servomotor force lever, we compared the stress-strain relationships of elastic elements in active and passive muscles during rapid unloading and quantified the change in stiffness upon activation. The results show that the ela...