Structural changes in the muscle thin filament during contractions caused by single and double electrical pulses.
In order to investigate the structural changes of the myofilaments involved in the phenomenon of summation in skeletal muscle contraction, we studied small-angle x-ray intensity changes during twitches of frog skeletal muscle elicited by either a single or a double stimulus at 16 degrees C. The separation of the pulses in the double-pulse stimulation was either 15 or 30 ms. The peak tension was more than doubled by the second stimulus. The equatorial (1,0) intensity, which decreased upon the first stimulus, further decreased with the second stimulus, indicating that more cross-bridges are formed. The meridional reflections from troponin at 1/38.5 and 1/19.2 nm(-1) were affected only slightly by the second stimulus, showing that attachment of a small number of myosin heads to actin can make a cooperative structural change. In overstretched muscle, the intensity increase of the troponin reflection in response to the second stimulus was smaller than that to the first stimulus. These results show that the summation is not due to an increased Ca binding to troponin and further suggest a highly cooperative nature of the structural changes in the thin filament that are related to the regulation of contraction.
Matsuo
Tatsuhito
T
Research and Utilization Division, Japan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5198, Japan.
Yagi
Naoto
N
D008841:Actin Cytoskeleton / Q000737:chemistry*; D000199:Actins / Q000378:metabolism; D000818:Animals; D004558:Electric Stimulation; D066298:In Vitro Techniques; D009119:Muscle Contraction / Q000502:physiology*; D009129:Muscle Tonus / Q000502:physiology; D009218:Myosins / Q000378:metabolism; D011892:Rana catesbeiana / Q000502:physiology*; D012518:Sarcomeres / Q000378:metabolism; D014336:Troponin / Q000378:metabolism; D014961:X-Ray Diffraction
D000199:Actins; D014336:Troponin; D009218:Myosins