|
|
||||||||
Department of Biophysics, Urals Branch of Academy of Sciences of the USSR, Sverdlovsk.
1. Joule temperature jumps (T-jumps) from 5-9 degrees C up to 40 degrees C were used to study the cross-bridge kinetics and thermodynamics in skinned rabbit muscle fibres. To produce a T-jump, an alternating current pulse was passed through a fibre 5 s after removing the activating solution (pCa congruent to 4.5) from the experimental trough. The pulse frequency was congruent to 30 kHz, amplitude less than or equal to 3 kV, and duration 0.2 ms. The pulse energy liberated in the fibre was calculated using a special analog circuit and then used for estimation of the T-jump amplitude. 2. The T-jump induced a tri-exponential tension transient. Phases 1 and 2 had rate constants k1 = 450-1750 s-1 and k2 = 60-250 s-1 respectively, characterizing the tension rise, whereas phase 3 had a rate constant k3 = 5-10 s-1 representing tension recovery due to the fibre cooling. 3. An increase from 13 to 40 degrees C for the final temperature achieved by the T-jump led to an increase in the amplitudes of phases 1 and 2. After T-jumps to 30-40 degrees C during phase 1, tension increased by 50-80%. During phase 2 an approximately 2-fold tension increase continued. Rate constants k1 and k2 increased with temperature and temperature coefficients (Q10) were 1.6 and 1.7, respectively. 4. To study which processes in the cross-bridges are involved in phases 1 and 2, a series of experiments were made where step length changes of -9 to +3 nm (hs)-1 (nanometres per half-sarcomere length) were applied to the fibre 4 ms before the T-jump. 5. After the step shortening, the rate constant of phase 1 increased, whereas its amplitude decreased compared to those without a length change. This indicates that phase 1 is determined by some force-generating process in the cross-bridges attached to the thin filaments. This process is, most probably, the same as that producing the early tension recovery following the length change. The enthalpy change (delta H) associated with the reaction controlling this process was estimated to be positive (15-30 kJ mol-1). 6. Both the rate constant k2 and the maximal tension achieved at the end of phase 2 were practically independent of the preceding length changes. This means that phase 2 is accompanied by the cross-bridge detachment and reattachment to new sites on the thin filaments.(ABSTRACT TRUNCATED AT 400 WORDS)
This article has been cited by other articles:
![]() |
K. W. Ranatunga, M. E. Coupland, G. J. Pinniger, H. Roots, and G. W. Offer Force generation examined by laser temperature-jumps in shortening and lengthening mammalian (rabbit psoas) muscle fibres J. Physiol., November 15, 2007; 585(1): 263 - 277. [Abstract] [Full Text] [PDF] |
||||
![]() |
K. Franks-Skiba, R. Lardelli, G. Goh, and R. Cooke Myosin light chain phosphorylation inhibits muscle fiber shortening velocity in the presence of vanadate Am J Physiol Regulatory Integrative Comp Physiol, April 1, 2007; 292(4): R1603 - R1612. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. Kawai, T. Kido, M. Vogel, R. H. A. Fink, and S. Ishiwata Temperature change does not affect force between regulated actin filaments and heavy meromyosin in single-molecule experiments J. Physiol., August 1, 2006; 574(3): 877 - 887. [Abstract] [Full Text] [PDF] |
||||
![]() |
K. Burton, R. M. Simmons, J. Sleep, R. M. Simmons, K. Burton, and D. A. Smith Kinetics of force recovery following length changes in active skinned single fibres from rabbit psoas muscle: with an Appendix: Analysis and modelling of the late recovery phase J. Physiol., June 1, 2006; 573(2): 305 - 328. [Abstract] [Full Text] [PDF] |
||||
![]() |
V. Decostre, P. Bianco, V. Lombardi, and G. Piazzesi Effect of temperature on the working stroke of muscle myosin PNAS, September 27, 2005; 102(39): 13927 - 13932. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. E. Coupland, G. J. Pinniger, and K. W. Ranatunga Endothermic force generation, temperature-jump experiments and effects of increased [MgADP] in rabbit psoas muscle fibres J. Physiol., September 1, 2005; 567(2): 471 - 492. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. Sleep, M. Irving, and K. Burton The ATP hydrolysis and phosphate release steps control the time course of force development in rabbit skeletal muscle J. Physiol., March 15, 2005; 563(3): 671 - 687. [Abstract] [Full Text] [PDF] |
||||
![]() |
C. Karatzaferi, M. K. Chinn, and R. Cooke The Force Exerted by a Muscle Cross-Bridge Depends Directly on the Strength of the Actomyosin Bond Biophys. J., October 1, 2004; 87(4): 2532 - 2544. [Abstract] [Full Text] [PDF] |
||||
![]() |
H. Kato, T. Nishizaka, T. Iga, K. Kinosita Jr., and S.'i. Ishiwata Imaging of thermal activation of actomyosin motors PNAS, August 17, 1999; 96(17): 9602 - 9606. [Abstract] [Full Text] [PDF] |
||||
![]() |
S. Y. Bershitsky and A. K. Tsaturyan The elementary force generation process probed by temperature and length perturbations in muscle fibres from the rabbit J. Physiol., May 1, 2002; 540(3): 971 - 988. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |