Literature DB >> 8889165

Endothermic force generation in fast and slow mammalian (rabbit) muscle fibers.

K W Ranatunga1.   

Abstract

Isometric tension responses to rapid temperature jumps (T-jumps) of 3-7 degrees C were examined in single skinned fibers isolated from rabbit psoas (fast) and soleus (slow) muscles. T-jumps were induced by an infrared laser pulse (wavelength 1.32 microns, pulse duration 0.2 ms) obtained from a Nd-YAG laser, which heated the fiber and bathing buffer solution in a 50-microliter trough. After a T-jump, the temperature near the fiber remained constant for approximately 0.5 s, and the temperature could be clamped for longer periods by means of Peltier units assembled on the back trough wall. A T-jump produced a step decrease in tension in both fast and slow muscle fibers in rigor, indicating thermal expansion. In maximally Ca-activated (pCa approximately 4) fibers, the increase of steady tension with heating (3-35 degrees C) was approximately sigmoidal, and a T-jump at any temperature induced a more complex tension transient than in rigor fibers. An initial (small amplitude) step decrease in tension followed by a rapid recovery (tau(1); see Davis and Harrington, 1993) was seen in some records from both fiber types, which presumably was an indirect consequence of thermal expansion. The net rise in tension after a T-jump was biexponential, and its time course was characteristically different in the two fibers. At approximately 12 degrees C the reciprocal time constants for the two exponential components (tau(2) and tau(3), respectively, were approximately 70.s(-1) and approximately 15.s(-1) in fast fibers and approximately 20.s(-1) and approximately 3.s(-1) in slow fibers. In both fibers, tau(2) ("endothermic force regeneration") became faster with an increase in temperature. Furthermore, tau(3) was temperature sensitive in slow fibers but not in fast fibers. The results are compared and contrasted with previous findings from T-jump experiments on fast fibers. It is observed that the fast/slow fiber difference in the rate of endothermic force generation (three- to fourfold) is considerably smaller than the reported differences in the "phosphate release steps" (> 30-fold).

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Year:  1996        PMID: 8889165      PMCID: PMC1233657          DOI: 10.1016/S0006-3495(96)79389-X

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  27 in total

1.  Kinetics of force generation and phosphate release in skinned rabbit soleus muscle fibers.

Authors:  N C Millar; E Homsher
Journal:  Am J Physiol       Date:  1992-05

2.  Behaviour of frog and rat muscle at higher temperatures.

Authors:  S HAJDU
Journal:  Enzymologia       Date:  1950-11-15

3.  Myosin head movements are synchronous with the elementary force-generating process in muscle.

Authors:  M Irving; V Lombardi; G Piazzesi; M A Ferenczi
Journal:  Nature       Date:  1992-05-14       Impact factor: 49.962

4.  Effect of joule temperature jump on tension and stiffness of skinned rabbit muscle fibers.

Authors:  A K Tsaturyan
Journal:  Biophys J       Date:  1989-11       Impact factor: 4.033

5.  Pressure sensitivity of active tension in glycerinated rabbit psoas muscle fibres: effects of ADP and phosphate.

Authors:  N S Fortune; M A Geeves; K W Ranatunga
Journal:  J Muscle Res Cell Motil       Date:  1989-04       Impact factor: 2.698

6.  Transient tension changes initiated by laser temperature jumps in rabbit psoas muscle fibres.

Authors:  Y E Goldman; J A McCray; K W Ranatunga
Journal:  J Physiol       Date:  1987-11       Impact factor: 5.182

7.  Force generation by muscle fibers in rigor: a laser temperature-jump study.

Authors:  J S Davis; W F Harrington
Journal:  Proc Natl Acad Sci U S A       Date:  1987-02       Impact factor: 11.205

8.  Laser temperature-jump apparatus for the study of force changes in fibers.

Authors:  J S Davis; W F Harrington
Journal:  Anal Biochem       Date:  1987-03       Impact factor: 3.365

9.  The force-velocity relation of rat fast- and slow-twitch muscles examined at different temperatures.

Authors:  K W Ranatunga
Journal:  J Physiol       Date:  1984-06       Impact factor: 5.182

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

Authors:  N S Fortune; M A Geeves; K W Ranatunga
Journal:  Proc Natl Acad Sci U S A       Date:  1991-08-15       Impact factor: 11.205

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  37 in total

1.  Imaging of thermal activation of actomyosin motors.

Authors:  H Kato; T Nishizaka; T Iga; K Kinosita; S Ishiwata
Journal:  Proc Natl Acad Sci U S A       Date:  1999-08-17       Impact factor: 11.205

2.  Structural changes in the actin-myosin cross-bridges associated with force generation induced by temperature jump in permeabilized frog muscle fibers.

Authors:  A K Tsaturyan; S Y Bershitsky; R Burns; M A Ferenczi
Journal:  Biophys J       Date:  1999-07       Impact factor: 4.033

3.  Temperature change does not affect force between single actin filaments and HMM from rabbit muscles.

Authors:  M Kawai; K Kawaguchi; M Saito; S Ishiwata
Journal:  Biophys J       Date:  2000-06       Impact factor: 4.033

4.  The elementary force generation process probed by temperature and length perturbations in muscle fibres from the rabbit.

Authors:  Sergey Y Bershitsky; Andrey K Tsaturyan
Journal:  J Physiol       Date:  2002-05-01       Impact factor: 5.182

5.  The effects of ramp stretches on active contractions in intact mammalian fast and slow muscle fibres.

Authors:  G Mutungi; K W Ranatunga
Journal:  J Muscle Res Cell Motil       Date:  2001       Impact factor: 2.698

6.  Sarcomeric visco-elasticity of chemically skinned skeletal muscle fibres of the rabbit at rest.

Authors:  K W Ranatunga
Journal:  J Muscle Res Cell Motil       Date:  2001       Impact factor: 2.698

7.  Temperature dependence of the force-generating process in single fibres from frog skeletal muscle.

Authors:  G Piazzesi; M Reconditi; N Koubassova; V Decostre; M Linari; L Lucii; V Lombardi
Journal:  J Physiol       Date:  2003-03-28       Impact factor: 5.182

Review 8.  What do we learn by studying the temperature effect on isometric tension and tension transients in mammalian striated muscle fibres?

Authors:  Masataka Kawai
Journal:  J Muscle Res Cell Motil       Date:  2003       Impact factor: 2.698

9.  Kinetic effects of fiber type on the two subcomponents of the Huxley-Simmons phase 2 in muscle.

Authors:  Julien S Davis; Neal D Epstein
Journal:  Biophys J       Date:  2003-07       Impact factor: 4.033

10.  A simple model with myofilament compliance predicts activation-dependent crossbridge kinetics in skinned skeletal fibers.

Authors:  D A Martyn; P B Chase; M Regnier; A M Gordon
Journal:  Biophys J       Date:  2002-12       Impact factor: 4.033

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