Literature DB >> 2621610

Cross-bridge movement in rat cardiac muscle as a function of calcium concentration.

I Matsubara1, D W Maughan, Y Saeki, N Yagi.   

Abstract

1. By applying the X-ray diffraction method to chemically skinned papillary muscles of the rat, the transfer of myosin heads from the thick to the thin filaments was studied as a function of Ca2+ concentration. 2. No significant transfer of the heads occurred when the Ca2+ concentration was below the threshold of contraction (pCa 6.2). 3. During the maximum isometric contraction at pCa 4.4, 80% of the myosin heads were transferred to the thin filament. 4. When the muscle was activated isometrically at low Ca2+ concentrations (pCa 6.2-5.8), where the average tension was less than 20% of the maximum, a disproportionately large number of myosin heads were transferred to the thin filament. 5. It was concluded that a significant fraction of the heads transferred at the low Ca2+ concentrations does not produce tension.

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Year:  1989        PMID: 2621610      PMCID: PMC1189283          DOI: 10.1113/jphysiol.1989.sp017818

Source DB:  PubMed          Journal:  J Physiol        ISSN: 0022-3751            Impact factor:   5.182


  23 in total

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Authors:  J W Krueger; G H Pollack
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Authors:  G F ELLIOTT; C R WORTHINGTON
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3.  Use of an X-ray television for diffraction of the frog striated muscle.

Authors:  I Matsubara; N Yagi; H Hashizume
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4.  Kinetics of reaction in calcium-activated skinned muscle fibres.

Authors:  D G Moisescu
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5.  An X-ray diffraction study of the cross-circulated canine heart.

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

Review 7.  Contractile proteins of the heart.

Authors:  A M Katz
Journal:  Physiol Rev       Date:  1970-01       Impact factor: 37.312

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Authors:  I Matsubara; B M Millman
Journal:  J Mol Biol       Date:  1974-02-05       Impact factor: 5.469

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

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10.  Thermodynamic quantities associated with the interaction of adenosine triphosphate with metal ions.

Authors:  M M Khan; A E Martell
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  15 in total

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5.  Radial displacement of myosin cross-bridges in mouse myocardium due to ablation of myosin binding protein-C.

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6.  Cross-bridge movement in rat slow skeletal muscle as a function of calcium concentration.

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7.  Theoretical treatment of striated muscle: Dynamic extension of four-state model.

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9.  Changes in cardiac contractility related to calcium-mediated changes in phosphorylation of myosin-binding protein C.

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10.  Multiple structures of thick filaments in resting cardiac muscle and their influence on cross-bridge interactions.

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