Comparison of force and shortening velocity of fast and slow rabbit muscle fibers at different temperatures

BIOPHYSICS ◽  
2014 ◽  
Vol 59 (5) ◽  
pp. 786-790 ◽  
Author(s):  
P. V. Kochubey ◽  
S. Y. Bershitsky
Keyword(s):  
Muscle Fibers ◽  
Rabbit Muscle ◽  
Shortening Velocity ◽  
Different Temperatures

scholarly journals Shortening velocity and myosin heavy chains of developing rabbit muscle fibers.

1985 ◽  
Vol 260 (27) ◽  
pp. 14403-14405 ◽  
Author(s):  
P J Reiser ◽  
R L Moss ◽  
G G Giulian ◽  
M L Greaser
Keyword(s):  
Muscle Fibers ◽  
Rabbit Muscle ◽  
Myosin Heavy Chains ◽  
Shortening Velocity ◽  
Heavy Chains

scholarly journals EFFECT OF SPACEFLIGHT ON PEAK FORCE AND MAXIMAL SHORTENING VELOCITY OF HUMAN MUSCLE FIBERS 1084

1997 ◽  
Vol 29 (Supplement) ◽  
pp. 190 ◽  
Author(s):  
J. J. Widrick ◽  
J. G. Romatowski ◽  
K. M. Norenberg ◽  
G. Gettleman ◽  
S. W. Trappe ◽  
...  
Keyword(s):  
Muscle Fibers ◽  
Human Muscle ◽  
Peak Force ◽  
Shortening Velocity

scholarly journals Tension responses to rapid pressure release in glycerinated rabbit muscle fibers.

1991 ◽  
Vol 88 (16) ◽  
pp. 7323-7327 ◽  
Author(s):  
N. S. Fortune ◽  
M. A. Geeves ◽  
K. W. Ranatunga
Keyword(s):  
Muscle Fibers ◽  
Rabbit Muscle ◽  
Pressure Release ◽  
Rapid Pressure

scholarly journals The Fraction of Myosin Motors That Participate in Isometric Contraction of Rabbit Muscle Fibers at Near-Physiological Temperature

2011 ◽  
Vol 101 (2) ◽  
pp. 404-410 ◽  
Author(s):  
Andrey K. Tsaturyan ◽  
Sergey Y. Bershitsky ◽  
Natalia A. Koubassova ◽  
Manuel Fernandez ◽  
Theyencheri Narayanan ◽  
...  
Keyword(s):  
Isometric Contraction ◽  
Muscle Fibers ◽  
Rabbit Muscle ◽  
Physiological Temperature ◽  
Myosin Motors

Regulation of the cross-bridge transition from a weakly to strongly bound state in skinned rabbit muscle fibers

1995 ◽  
Vol 269 (6) ◽  
pp. C1532-C1539 ◽  
Author(s):  
M. Regnier ◽  
C. Morris ◽  
E. Homsher
Keyword(s):  
Muscle Fibers ◽  
Bound State ◽  
Single Step ◽  
Rabbit Muscle ◽  
Weakly Bound ◽  
Cross Bridge ◽  
Skinned Muscle ◽  
Butanedione Monoxime ◽  
Bridge Models ◽  
Parallel Fashion

The regulation of cross-bridge transition from weakly attached to force-bearing states was studied at 10 degrees C in skinned muscle fibers by measuring the rate of force development after a quick release-restretch cycle (ktr), the rate of force decline (kPi) after photogeneration of Pi from caged Pi, and stiffness in the presence and absence of an inhibitor of strong cross-bridge formation, 2,3-butanedione monoxime (BDM). Both BDM and Pi suppressed force more than stiffness. However, reduction of Ca2+ suppressed force and stiffness in a parallel fashion. Both ktr and kPi were reversibly reduced (by 30-35%) in 3 mM BDM, but both were increased by increasing Pi concentration. Reduction of Ca2+ concentration to match the force seen in 3 mM BDM had no effect on kPi but decreased ktr by 85%. These results are inconsistent with cross-bridge models undergoing the transition from a weakly bound to a force-generating state in a single step but are consistent with a model having two steps, one of which is controlled by pCa.

Effect of Pi on unloaded shortening velocity of slow and fast mammalian muscle fibers

2002 ◽  
Vol 282 (4) ◽  
pp. C647-C653 ◽  
Author(s):  
Jeffrey J. Widrick
Keyword(s):  
Fiber Type ◽  
Muscle Fibers ◽  
Medial Gastrocnemius ◽  
Type I ◽  
Shortening Velocity ◽  
Cross Bridge ◽  
Skinned Muscle ◽  
Specific Effects ◽  
Cross Bridges ◽  
Bridge Models

Chemically skinned muscle fibers, prepared from the rat medial gastrocnemius and soleus, were subjected to four sequential slack tests in Ca2+-activating solutions containing 0, 15, 30, and 0 mM added Pi. Pi (15 and 30 mM) had no effect on the unloaded shortening velocity ( V o) of fibers expressing type IIb myosin heavy chain (MHC). For fibers expressing type I MHC, 15 mM Pi did not alter V o, whereas 30 mM Pireduced V o to 81 ± 1% of the original 0 mM Pi value. This effect was readily reversible when Pi was lowered back to 0 mM. These results are not compatible with current cross-bridge models, developed exclusively from data obtained from fast fibers, in which V o is independent of Pi. The response of the type I fibers at 30 mM Pi is most likely the result of increased internal drag opposing fiber shortening resulting from fiber type-specific effects of Pi on cross bridges, the thin filament, or the rate-limiting step of the cross-bridge cycle.

scholarly journals Maximum Shortening Velocity and Myosin Heavy-chain Isoform Expression in Human Masseter Muscle Fibers

2001 ◽  
Vol 80 (9) ◽  
pp. 1845-1848 ◽  
Author(s):  
T.J. Morris ◽  
C.A. Branden ◽  
M.J. Horton ◽  
D.S. Carlson ◽  
J.J. Sciote
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Masseter Muscle ◽  
Muscle Fibers ◽  
Shortening Velocity ◽  
Myosin Heavy Chain Isoform ◽  
Isoform Expression
Sign in / Sign up

Export Citation Format

Share Document