Literature DB >> 16453159

Connecting filament mechanics in the relaxed sarcomere.

Ekaterina Nagornyak1, Gerald H Pollack.   

Abstract

By examining the mechanical properties of single unactivated myofibrils it has been shown that shortening and stretching of sarcomeres occurs in stepwise fashion, and that steps are seen also in the relaxed state (Yang et al. (1998) Biophys J 74: 1473-1483; Blyakhman et al. (2001) Biophys J 81: 1093-1100; Nagornyak et al. (2004) J. Muscle. Res. Cell Motil. 25: 37-43). The latter are inevitably associated with connecting filaments. Here, we carried out measurements on single myofibrils from rabbit psoas muscle to investigate steps in unactivated specimens in more detail. Myofibrils were stretched and released in ramp-like fashion. For the single sarcomere the time course of length change was consistently stepwise. We found that in the unactivated myofibrils, step size depended on initial sarcomere length, diminishing progressively with increase of initial sarcomere length, whereas in the case of activated sarcomeres, step size was consistently 2.7 nm.

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Year:  2005        PMID: 16453159     DOI: 10.1007/s10974-005-9036-3

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


  20 in total

1.  'Minimum average risk' as a new peak-detection algorithm applied to myofibrillar dynamics.

Authors:  S Yu Sokolov; A A Grinko; A V Tourovskaia; F B Reitz; O Yakovenko; G H Pollack; F A Blyakhman
Journal:  Comput Methods Programs Biomed       Date:  2003-09       Impact factor: 5.428

2.  Effect of sarcomere length on step size in relaxed rabbit psoas muscle.

Authors:  Ekaterina Nagornyak; Felix Blyakhman; Gerald H Pollack
Journal:  J Muscle Res Cell Motil       Date:  2004       Impact factor: 2.698

3.  Stepwise dynamics of connecting filaments measured in single myofibrillar sarcomeres.

Authors:  P Yang; T Tameyasu; G H Pollack
Journal:  Biophys J       Date:  1998-03       Impact factor: 4.033

4.  Immunoglobulin-like modules from titin I-band: extensible components of muscle elasticity.

Authors:  S Improta; A S Politou; A Pastore
Journal:  Structure       Date:  1996-03-15       Impact factor: 5.006

5.  Basis of passive tension and stiffness in isolated rabbit myofibrils.

Authors:  M L Bartoo; W A Linke; G H Pollack
Journal:  Am J Physiol       Date:  1997-07

6.  Reversible unfolding of individual titin immunoglobulin domains by AFM.

Authors:  M Rief; M Gautel; F Oesterhelt; J M Fernandez; H E Gaub
Journal:  Science       Date:  1997-05-16       Impact factor: 47.728

7.  Passive and active tension in single cardiac myofibrils.

Authors:  W A Linke; V I Popov; G H Pollack
Journal:  Biophys J       Date:  1994-08       Impact factor: 4.033

8.  Elasticity and unfolding of single molecules of the giant muscle protein titin.

Authors:  L Tskhovrebova; J Trinick; J A Sleep; R M Simmons
Journal:  Nature       Date:  1997-05-15       Impact factor: 49.962

9.  The assembly of immunoglobulin-like modules in titin: implications for muscle elasticity.

Authors:  S Improta; J K Krueger; M Gautel; R A Atkinson; J F Lefèvre; S Moulton; J Trewhella; A Pastore
Journal:  J Mol Biol       Date:  1998-12-04       Impact factor: 5.469

10.  Molecular size and shape of beta-connectin, an elastic protein of striated muscle.

Authors:  K Maruyama; S Kimura; H Yoshidomi; H Sawada; M Kikuchi
Journal:  J Biochem       Date:  1984-05       Impact factor: 3.387

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