Literature DB >> 11032342

Length-dependent effects of osmotic compression on skinned rabbit psoas muscle fibers.

Y P Wang1, F Fuchs.   

Abstract

The goal of this study was to characterize the interrelationship between sarcomere length and interfilament spacing in the control of Ca2+ sensitivity in skinned rabbit psoas muscle fibers. Measurements were made at sarcomere lengths 2.0, 2.7 and 3.4 microm. At 2.7 microm the fiber width was reduced by 17% relative to that at 2.0 microm and the pCa50 for force development was increased by approximately 0.3 pCa units. In the presence of 5% Dextran T-500 the fiber width at sarcomere length 2.0 microm was also decreased by 17% and the Ca2+ sensitivity was increased to the same value as at 2.7 microm. In contrast, at sarcomere length 2.7 microm the addition of as much as 10% Dextran T-500 had no effect on Ca2+ sensitivity. At sarcomere length 3.4 microm there was an additional 7% compression and the Ca2+ sensitivity was increased slightly (approximately 0.1 pCa units) relative to that at 2.7 microm. However at 3.4 microm the addition of 5% Dextran T-500 caused the Ca2+ sensitivity to decrease to the level seen at 2.0 microm. Given that the skinning process causes a swelling of the filament lattice it is evident that the relationship between sarcomere length and Ca2+ sensitivity observed in skinned fibers may not always be applicable to intact fibers. These data are consistent with measurements of Ca2+ in intact fibers which indicate that there might be a decline in Ca2+ sensitivity at long sarcomere lengths.

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Year:  2000        PMID: 11032342     DOI: 10.1023/a:1005679215704

Source DB:  PubMed          Journal:  J Muscle Res Cell Motil        ISSN: 0142-4319            Impact factor:   2.698


  43 in total

1.  Length dependence of Ca(2+)-tension relationship in aequorin-injected ferret papillary muscles.

Authors:  K Komukai; S Kurihara
Journal:  Am J Physiol       Date:  1997-09

2.  Stretch-induced increase in activation of skinned muscle fibres by calcium.

Authors:  M Endo
Journal:  Nat New Biol       Date:  1972-06-14

3.  X-ray diffraction observations of chemically skinned frog skeletal muscle processed by an improved method.

Authors:  A Magid; M K Reedy
Journal:  Biophys J       Date:  1980-04       Impact factor: 4.033

4.  Parallel measurements of bound calcium and force in glycerinated rabbit psoas muscle fibers.

Authors:  F Fuchs; C Fox
Journal:  Biochim Biophys Acta       Date:  1982-01-20

5.  The variation in isometric tension with sarcomere length in vertebrate muscle fibres.

Authors:  A M Gordon; A F Huxley; F J Julian
Journal:  J Physiol       Date:  1966-05       Impact factor: 5.182

6.  Swelling of skinned muscle fibers of the frog. Experimental observations.

Authors:  R E Godt; D W Maughan
Journal:  Biophys J       Date:  1977-08       Impact factor: 4.033

Review 7.  The role of calcium in the response of cardiac muscle to stretch.

Authors:  S C Calaghan; E White
Journal:  Prog Biophys Mol Biol       Date:  1999       Impact factor: 3.667

8.  Effect of length and cross-bridge attachment on Ca2+ binding to cardiac troponin C.

Authors:  P A Hofmann; F Fuchs
Journal:  Am J Physiol       Date:  1987-07

9.  Osmotic compression of skinned cardiac and skeletal muscle bundles: effects on force generation, Ca2+ sensitivity and Ca2+ binding.

Authors:  Y P Wang; F Fuchs
Journal:  J Mol Cell Cardiol       Date:  1995-06       Impact factor: 5.000

10.  The effect of the lattice spacing change on cross-bridge kinetics in chemically skinned rabbit psoas muscle fibers. II. Elementary steps affected by the spacing change.

Authors:  Y Zhao; M Kawai
Journal:  Biophys J       Date:  1993-01       Impact factor: 4.033

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  1 in total

1.  Titin stiffness modifies the force-generating region of muscle sarcomeres.

Authors:  Yong Li; Patrick Lang; Wolfgang A Linke
Journal:  Sci Rep       Date:  2016-04-15       Impact factor: 4.379

  1 in total

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