Literature DB >> 4074840

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

B Brenner, L C Yu.   

Abstract

Equatorial x-ray diffraction patterns were obtained from single skinned rabbit psoas fibers during various degrees of activation under isometric conditions at ionic strength 170 mM and 6-9 degrees C. By direct calcium activation, contraction was homogeneous throughout the preparation, and by using a cycling technique (Brenner, 1983) integrity of the fiber was maintained even during prolonged steady activation. The intensity ratio of the two innermost reflections I11/I10, and the normalized intensities I*10 and I*11 varied linearly with increasing force. Thus the result agreed qualitatively with an earlier finding, obtained from the whole sartorius muscle, that intensity changes in 10 and 11 are directly correlated with isometric force level (Yu et al., 1979). Spacing of the myofilament lattice (d10) was found to decrease with increasing isometric tension. With the filaments in full overlap, maximum shrinkage was 14%. The lattice spacing started to level off when the degree of calcium activation was greater than or equal to 50%, approaching a limit approximately at 380-360 A. This decrease of the lattice spacing indicates that there is a radial force produced by force generating cross-bridges, but the net radial force appears to become insignificant as lattice spacing approaches 380-360 A.

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Year:  1985        PMID: 4074840      PMCID: PMC1329408          DOI: 10.1016/S0006-3495(85)83841-8

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


  16 in total

1.  Structure and force generation in muscle.

Authors:  J M Squire
Journal:  Nature       Date:  1979-09-13       Impact factor: 49.962

2.  X-ray diffraction of actively shortening muscle.

Authors:  R J Podolsky; H St Onge; L Yu; R W Lymn
Journal:  Proc Natl Acad Sci U S A       Date:  1976-03       Impact factor: 11.205

3.  X-ray evidence for radial cross-bridge movement and for the sliding filament model in actively contracting skeletal muscle.

Authors:  J C Haselgrove; H E Huxley
Journal:  J Mol Biol       Date:  1973-07-15       Impact factor: 5.469

4.  Structural difference between resting and rigor muscle; evidence from intensity changes in the lowangle equatorial x-ray diagram.

Authors:  H E Huxley
Journal:  J Mol Biol       Date:  1968-11-14       Impact factor: 5.469

5.  The relation between calcium and contraction kinetics in skinned muscle fibres.

Authors:  R J Podolsky; L E Teichholz
Journal:  J Physiol       Date:  1970-11       Impact factor: 5.182

6.  Equatorial x-ray intensities and isometric force levels in frog sartorius muscle.

Authors:  L P Yu; J E Hartt; R J Podolsky
Journal:  J Mol Biol       Date:  1979-07-25       Impact factor: 5.469

7.  Geometrical factors influencing muscle force development. II. Radial forces.

Authors:  M Schoenberg
Journal:  Biophys J       Date:  1980-04       Impact factor: 4.033

8.  Lateral filamentary spacing in chemically skinned murine muscles during contraction.

Authors:  I Matsubara; Y Umazume; N Yagi
Journal:  J Physiol       Date:  1985-03       Impact factor: 5.182

9.  Myosin subfragment-1 attachment to actin. Expected effect on equatorial reflections.

Authors:  R W Lymn
Journal:  Biophys J       Date:  1978-01       Impact factor: 4.033

10.  Radial forces within muscle fibers in rigor.

Authors:  D W Maughan; R E Godt
Journal:  J Gen Physiol       Date:  1981-01       Impact factor: 4.086

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  48 in total

1.  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

2.  Time-resolved X-ray diffraction by skinned skeletal muscle fibers during activation and shortening.

Authors:  B K Hoskins; C C Ashley; G Rapp; P J Griffiths
Journal:  Biophys J       Date:  2001-01       Impact factor: 4.033

3.  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

4.  Structural characterization of weakly attached cross-bridges in the A*M*ATP state in permeabilized rabbit psoas muscle.

Authors:  S Xu; J Gu; G Melvin; L C Yu
Journal:  Biophys J       Date:  2002-04       Impact factor: 4.033

5.  Influence of length on force and activation-dependent changes in troponin c structure in skinned cardiac and fast skeletal muscle.

Authors:  D A Martyn; A M Gordon
Journal:  Biophys J       Date:  2001-06       Impact factor: 4.033

6.  Troponin I in the murine myocardium: influence on length-dependent activation and interfilament spacing.

Authors:  John P Konhilas; Thomas C Irving; Beata M Wolska; Eias E Jweied; Anne F Martin; R John Solaro; Pieter P de Tombe
Journal:  J Physiol       Date:  2003-01-24       Impact factor: 5.182

7.  Length-dependent activation in three striated muscle types of the rat.

Authors:  John P Konhilas; Thomas C Irving; Pieter P de Tombe
Journal:  J Physiol       Date:  2002-10-01       Impact factor: 5.182

8.  Tetragonal deformation of the hexagonal myofilament matrix in single skinned skeletal muscle fibres owing to change in sarcomere length.

Authors:  P Schiereck; E L de Beer; R L Grundeman; T Manussen; N Kylstra; W Bras
Journal:  J Muscle Res Cell Motil       Date:  1992-10       Impact factor: 2.698

Review 9.  Length-dependent Ca(2+) activation in cardiac muscle: some remaining questions.

Authors:  Franklin Fuchs; Donald A Martyn
Journal:  J Muscle Res Cell Motil       Date:  2005-10-05       Impact factor: 2.698

10.  Effects of inorganic phosphate analogues on stiffness and unloaded shortening of skinned muscle fibres from rabbit.

Authors:  P B Chase; D A Martyn; M J Kushmerick; A M Gordon
Journal:  J Physiol       Date:  1993-01       Impact factor: 5.182

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