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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Udaka, Jun Terui, Takako Ohtsuki, Iwao Marumo, Keishi Ishiwata, Shin'ichi Kurihara, Satoshi Fukuda, Norio |
| Description | Country affiliation: Japan Author Affiliation: Udaka J ( Department of Cell Physiology, The Jikei University School of Medicine, Tokyo, Japan.) |
| Abstract | Long-term disuse results in atrophy in skeletal muscle, which is characterized by reduced functional capability, impaired locomotor condition, and reduced resistance to fatigue. Here we show how long-term disuse affects contractility and fatigue resistance in single fibers of soleus muscle taken from the hindlimb immobilization model of the rat. We found that long-term disuse results in depression of caffeine-induced transient contractions in saponin-treated single fibers. However, when normalized to maximal Ca(2+)-activated force, the magnitude of the transient contractions became similar to that in control fibers. Control experiments indicated that the active force depression in disused muscle is not coupled with isoform switching of myosin heavy chain or troponin, or with disruptions of sarcomere structure or excessive internal sarcomere shortening during contraction. In contrast, our electronmicroscopic observation supported our earlier observation that interfilament lattice spacing is expanded after disuse. Then, to investigate the molecular mechanism of the reduced fatigue resistance in disused muscle, we compared the inhibitory effects of inorganic phosphate (Pi) on maximal Ca(2+)-activated force in control vs. disused fibers. The effect of Pi was more pronounced in disused fibers, and it approached that observed in control fibers after osmotic compression. These results suggest that contractile depression in disuse results from the lowering of myofibrillar force-generating capacity, rather than from defective Ca(2+) mobilization, and the reduced resistance to fatigue is from an enhanced inhibitory effect of Pi coupled with a decrease in the number of attached cross bridges, presumably due to lattice spacing expansion. |
| File Format | HTM / HTML |
| ISSN | 87507587 |
| e-ISSN | 15221601 |
| Journal | Journal of Applied Physiology |
| Issue Number | 4 |
| Volume Number | 111 |
| Language | English |
| Publisher | American Physiological Society |
| Publisher Date | 2011-10-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Discipline Physiology Fatigue Physiopathology Muscle Contraction Physiology Muscle Fibers, Skeletal Muscular Disorders, Atrophic Myofibrils Animals Caffeine Pharmacology Calcium Metabolism Hindlimb Suspension Drug Effects Myosin Heavy Chains Osmotic Pressure Phosphates Rats, Wistar Saponins Sarcomeres Troponin Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Physiology Physiology (medical) Sports Science |
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