Literature DB >> 3209858

Fine structure of the A-band in cryo-sections. Diversity of M-band structure in chicken breast muscle.

A C Edman1, J M Squire, M Sjöström.   

Abstract

Electron micrographs of longitudinal ultrathin cryo-sections and plastic sections of chicken pectoralis muscle together with their average images have been used to study in detail the axial structure of the M-band. It was found that M-band structure could vary markedly in different fibres, even within the white part of the muscle. Strong M-band density ("M-bridges") could be seen at M4 and M4' in all fibres. On the other hand the density at M1 or M6 could vary systematically. Some fibres (probably fast) had M1 strong, M6 weak (a "3-line" M-band), and the Z-band was narrow. Other fibres, especially (but not exclusively) in the red part of the muscle and probably slow, had M6 strong, M1 weak (a "4-line" M-band), and the Z-band was broad. However, the majority of fibres ranged in structure between those two extremes and had a more or less "5-line" M-band with M1 and M6 both strong and a Z-band of intermediate width. Since they were such a constant feature, the M4 lines may be the sites of the primarily structural component of the M-band, whereas the different proteins at M1 and M6 may vary in quantity according to the physiological needs of the fibre. Finally, detailed analysis sometimes revealed substructure within the strong M-bridge lines. This substructure may represent additional unknown M-band proteins or may be an indication of the shape of single proteins at these positions.

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Year:  1988        PMID: 3209858     DOI: 10.1016/0889-1605(88)90054-7

Source DB:  PubMed          Journal:  J Ultrastruct Mol Struct Res        ISSN: 0889-1605


  8 in total

Review 1.  M-band: a safeguard for sarcomere stability?

Authors:  Irina Agarkova; Elisabeth Ehler; Stephan Lange; Roman Schoenauer; Jean-Claude Perriard
Journal:  J Muscle Res Cell Motil       Date:  2003       Impact factor: 2.698

2.  Interpretation of the X-ray diffraction pattern from relaxed skeletal muscle and modelling of the thick filament structure.

Authors:  S B Malinchik; V V Lednev
Journal:  J Muscle Res Cell Motil       Date:  1992-08       Impact factor: 2.698

3.  Comparative histochemistry of a flatfish fin muscle and of other vertebrate muscles used for ultrastructural studies.

Authors:  N Chayen; A Freundlich; J M Squire
Journal:  J Muscle Res Cell Motil       Date:  1987-08       Impact factor: 2.698

4.  M-band structure, M-bridge interactions and contraction speed in vertebrate cardiac muscles.

Authors:  H T Pask; K L Jones; P K Luther; J M Squire
Journal:  J Muscle Res Cell Motil       Date:  1994-12       Impact factor: 2.698

5.  Making muscle elastic: the structural basis of myomesin stretching.

Authors:  Larissa Tskhovrebova; John Trinick
Journal:  PLoS Biol       Date:  2012-02-14       Impact factor: 8.029

6.  Three-dimensional structure of the M-region (bare zone) of vertebrate striated muscle myosin filaments by single-particle analysis.

Authors:  Hind A Al-Khayat; Robert W Kensler; Edward P Morris; John M Squire
Journal:  J Mol Biol       Date:  2010-09-17       Impact factor: 5.469

7.  Mutant myocilin impacts sarcomere ultrastructure in mouse gastrocnemius muscle.

Authors:  Jeffrey M Lynch; Andrew J Dolman; Chenying Guo; Katie Dolan; Chuanxi Xiang; Samir Reda; Bing Li; Ganesh Prasanna
Journal:  PLoS One       Date:  2018-11-05       Impact factor: 3.240

Review 8.  The role of the M-band myomesin proteins in muscle integrity and cardiac disease.

Authors:  Ekaterina P Lamber; Pascale Guicheney; Nikos Pinotsis
Journal:  J Biomed Sci       Date:  2022-03-07       Impact factor: 8.410

  8 in total

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