title: Effects of muscle length on the response to unloading.
abstract: Muscle mass, distribution of fiber types, fiber cross-sectional areas (CSA) and selected enzyme activities were determined in rats hindlimb-suspended free of immobilization (Susp-Free), suspended with the ankle dorsiflexed (Susp-DF, soleus stretched) or plantarflexed (Susp-PF, soleus shortened) for 10 days and compared to cage-control (Con) rats. Reduction of muscle weight associated with suspension was prevented in Susp-DF rats. The mean CSAs of slow fibers were Con = Susp-DF > Susp > PF > Susp-Free and of fast and intermediate fiber tended to be Susp-DF > Con > Susp-PF = Susp-Free. Mean activities of succinate dehydrogenase (SDH), alpha-glycerophosphate dehydrogenase (GPD) and myofibrillar adenosine triphosphatase (mATPase) in slow and fast fibers were similar in Con and Susp-Free rats. Mean SDH activity in slow fibers was higher in Susp-DF and Susp-PF than in Con and Susp-Free. No significant differences in SDH activities of fast fibers were observed among groups. GPD activity was higher in slow fibers of Susp-DF and Susp-PF compared to Con. The mATPase activity was higher in slow fibers of Susp-DF compared to Con and Susp-Free rats and lower in fast fibers of Susp-DF compared to Con rats. Thus, when compared to control, the patterns of adaptation were more similar in the Susp-DF and Susp-PF than in the Susp-Free. Although these results are consistent with previous studies demonstrating that the load placed on a muscle can affect protein metabolism, the direction and magnitude of the adaptive responses observed in the present study were closely associated with the chronically imposed changes in muscle length, i.e. fixed at either a shortened or a lengthened position.
authors.affiliation: Department of Physiology and Biomechanics, National Institute of Fitness and Sports, Kanoya City, Japan. ohira@nifs-k.ac.jp
authors.forename: Y
authors.initials: Y
authors.lastname: Ohira
authors.forename: W
authors.initials: W
authors.lastname: Yasui
authors.forename: R R
authors.initials: RR
authors.lastname: Roy
authors.forename: V R
authors.initials: VR
authors.lastname: Edgerton
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D001696:Biomechanical Phenomena; D005993:Glycerolphosphate Dehydrogenase / Q000378:metabolism; D006614:Hindlimb; D007103:Immobilization; D008297:Male; D018485:Muscle Fibers, Skeletal / Q000648:ultrastructure*; D009132:Muscles / Q000033:anatomy & histology* / Q000201:enzymology / Q000502:physiology*; D009210:Myofibrils / Q000201:enzymology; D009929:Organ Size; D051381:Rats; D017208:Rats, Wistar; D013385:Succinate Dehydrogenase / Q000378:metabolism; D016474:Weight-Bearing / Q000502:physiology*
chemical_list: D005993:Glycerolphosphate Dehydrogenase; D013385:Succinate Dehydrogenase; D000251:Adenosine Triphosphatases