Literature DB >> 7858135

Unloaded shortening of skinned muscle fibers from rabbit activated with and without Ca2+.

D A Martyn1, P B Chase, J D Hannon, L L Huntsman, M J Kushmerick, A M Gordon.   

Abstract

Unloaded shortening velocity (VUS) was determined by the slack method and measured at both maximal and submaximal levels of activation in glycerinated fibers from rabbit psoas muscle. Graded activation was achieved by two methods. First, [Ca2+] was varied in fibers with endogenous skeletal troponin C (sTnC) and after replacement of endogenous TnC with either purified cardiac troponin C (cTnC) or sTnC. Alternatively, fibers were either partially or fully reconstituted with a modified form of cTnC (aTnC) that enables force generation and shortening in the absence of Ca2+. Uniformity of the distribution of reconstituted TnC across the fiber radius was evaluated using fluorescently labeled sTnC and laser scanning fluorescence confocal microscopy. Fiber shortening was nonlinear under all conditions tested and was characterized by an early rapid phase (VE) followed by a slower late phase (VL). In fibers with endogenous sTnC, both VE and VL varied with [Ca2+], but VE was less affected than VL. Similar results were obtained after extraction of TnC and reconstitution with either sTnC or cTnC, except for a small increase in the apparent activation dependence of VE. Partial activation with aTnC was obtained by fully extracting endogenous sTnC followed by reconstitution with a mixture of aTnC and cTnC (aTnC:cTnC molar ratio 1:8.5). At pCa 9.2, VE and VL were similar to those obtained in fibers reconstituted with sTnC or cTnC at equivalent force levels. In these fibers, which contained aTnC and cTnC, VE and VL increased with isometric force when [Ca2+] was increased from pCa 9.2 to 4.0. Fibers that contained a mixture of a TnC and cTnC were then extracted a second time to selectively remove cTnC. In fibers containing aTnC only, VE and VL were proportional to the resulting submaximal isometric force compared with maximum Ca(2+)-activated control. With aTnC alone, force, VE, and VL were not affected by changes in [Ca2+]. The similarity of activation dependence of VUS whether fibers were activated in a Ca(2+)-sensitive or -insensitive manners implies that VUS is determined by the average level of thin filament activation and that, with sTnC or cTnC, VUS is affected by Ca2+ binding to TnC only.

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Year:  1994        PMID: 7858135      PMCID: PMC1225573          DOI: 10.1016/S0006-3495(94)80681-2

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


  49 in total

1.  Thin filament regulation of shortening velocity in rat skinned skeletal muscle: effects of osmotic compression.

Authors:  J M Metzger; R L Moss
Journal:  J Physiol       Date:  1988-04       Impact factor: 5.182

2.  The necessity of using two parameters to describe isotonic shortening velocity of muscle tissues: the effect of various interventions upon initial shortening velocity (vi) and curvature (b).

Authors:  B Brenner
Journal:  Basic Res Cardiol       Date:  1986 Jan-Feb       Impact factor: 17.165

3.  Effects on shortening velocity of rabbit skeletal muscle due to variations in the level of thin-filament activation.

Authors:  R L Moss
Journal:  J Physiol       Date:  1986-08       Impact factor: 5.182

4.  Altered Ca2+ dependence of tension development in skinned skeletal muscle fibers following modification of troponin by partial substitution with cardiac troponin C.

Authors:  R L Moss; M R Lauer; G G Giulian; M L Greaser
Journal:  J Biol Chem       Date:  1986-05-05       Impact factor: 5.157

5.  Effect of Ca2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: implications for regulation of muscle contraction.

Authors:  B Brenner
Journal:  Proc Natl Acad Sci U S A       Date:  1988-05       Impact factor: 11.205

6.  Effects of pH on contraction of rabbit fast and slow skeletal muscle fibers.

Authors:  P B Chase; M J Kushmerick
Journal:  Biophys J       Date:  1988-06       Impact factor: 4.033

7.  Equatorial x-ray diffraction from single skinned rabbit psoas fibers at various degrees of activation. Changes in intensities and lattice spacing.

Authors:  B Brenner; L C Yu
Journal:  Biophys J       Date:  1985-11       Impact factor: 4.033

8.  Contraction kinetics of intact and skinned frog muscle fibers and degree of activation. Effects of intracellular Ca2+ on unloaded shortening.

Authors:  J Gulati; A Babu
Journal:  J Gen Physiol       Date:  1985-10       Impact factor: 4.086

9.  Influence of partial activation on force-velocity properties of frog skinned muscle fibers in millimolar magnesium ion.

Authors:  R A Podolin; L E Ford
Journal:  J Gen Physiol       Date:  1986-04       Impact factor: 4.086

10.  Extra calcium on shortening in barnacle muscle. Is the decrease in calcium binding related to decreased cross-bridge attachment, force, or length?

Authors:  A M Gordon; E B Ridgway
Journal:  J Gen Physiol       Date:  1987-09       Impact factor: 4.086

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  33 in total

1.  Regulation of skeletal muscle tension redevelopment by troponin C constructs with different Ca2+ affinities.

Authors:  M Regnier; A J Rivera; P B Chase; L B Smillie; M M Sorenson
Journal:  Biophys J       Date:  1999-05       Impact factor: 4.033

2.  Strong binding of myosin increases shortening velocity of rabbit skinned skeletal muscle fibres at low levels of Ca(2+).

Authors:  D R Swartz; R L Moss
Journal:  J Physiol       Date:  2001-06-01       Impact factor: 5.182

3.  A myopathy-linked tropomyosin mutation severely alters thin filament conformational changes during activation.

Authors:  Julien Ochala; Hiroyuki Iwamoto; Lars Larsson; Naoto Yagi
Journal:  Proc Natl Acad Sci U S A       Date:  2010-05-10       Impact factor: 11.205

4.  Isotonic force modulates force redevelopment rate of intact frog muscle fibres: evidence for cross-bridge induced thin filament activation.

Authors:  Rene Vandenboom; James D Hannon; Gary C Sieck
Journal:  J Physiol       Date:  2002-09-01       Impact factor: 5.182

5.  Effect of viscosity on mechanics of single, skinned fibers from rabbit psoas muscle.

Authors:  P B Chase; T M Denkinger; M J Kushmerick
Journal:  Biophys J       Date:  1998-03       Impact factor: 4.033

6.  Thin filament cooperativity as a major determinant of shortening velocity in skeletal muscle fibers.

Authors:  H Iwamoto
Journal:  Biophys J       Date:  1998-03       Impact factor: 4.033

7.  Calcium regulation of skeletal muscle thin filament motility in vitro.

Authors:  A M Gordon; M A LaMadrid; Y Chen; Z Luo; P B Chase
Journal:  Biophys J       Date:  1997-03       Impact factor: 4.033

8.  Thin filament activation and unloaded shortening velocity of rabbit skinned muscle fibres.

Authors:  Carl A Morris; Larry S Tobacman; Earl Homsher
Journal:  J Physiol       Date:  2003-05-02       Impact factor: 5.182

9.  Functional differences between the N-terminal domains of mouse and human myosin binding protein-C.

Authors:  Justin F Shaffer; Peony Wong; Kristina L Bezold; Samantha P Harris
Journal:  J Biomed Biotechnol       Date:  2010-04-07

10.  Unloaded shortening velocity of voluntarily and electrically activated human dorsiflexor muscles in vivo.

Authors:  Kazushige Sasaki; Naokata Ishii
Journal:  PLoS One       Date:  2010-09-27       Impact factor: 3.240

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