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

Edman, Anne-Christine; Squire, John M.; Sjöstróm, Michael

doi:10.1016/0889-1605(88)90054-7

Cited by 22 publications

(12 citation statements)

References 27 publications

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“…In contrast to both of these structures, the fish heart M-band was lacking a strong MI, giving rise to a four-line M-band. Such a four-line structure appears to be characteristic of slow fibres; it is similar to that observed in some human Type I fibres such as masseter muscle (Thornell & Carlsson, 1984;Walliman & Eppenberger, 1985), in rat soleus Type I fibres (Sjostrom & Squire, 1977b) and in chicken pectoralis red (Type I) fibres (Edman et al, 1988a). M4 and M4' were strongly present in all the M-bands studied, supporting the view that the protein in this position is an important component of the M-band.…”

Section: Cardiac M-band Appearancesmentioning

confidence: 69%

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

Pask

Jones

Luther

et al. 1994

J Muscle Res Cell Motil

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Cardiac muscle M-band structures in several mammals (guinea pig, rabbit, rat and cow) and also from three teleosts (plaice, carp and roach), have been studied using electron microscopy and image processing. Axial structure seen in negatively stained isolated myofibrils or negatively stained cryo-sections shows the presence of five strong M-bridge lines (M6, M4, M1, M4' and M6') except in the case of the teleost M-bands in which the central M-line (M1) is absent, giving a four-line M-band. The M4 (M4') lines are consistently strong in all muscles, supporting the suggestion that bridges at this position are important for the structural integrity of the A-band myosin filament lattice. Across the vertebrate kingdom, cardiac M-band ultrastructure appears to correlate roughly with heartbeat frequency, just as in skeletal muscles it correlates with contraction speed, reinforcing the suggestion that some M-band components may have a significant physiological role. Apart from rat heart, which is relatively fast and has a conventional five-line M-band with M1 and M4 approximately equal, the rabbit, guinea pig and beef heart M-bands from a new 1 + 4 class; M1 is relatively very much stronger than M4. Transverse sections of the teleost (roach) cardiac A-band show a simple lattice arrangement of myosin filaments, just as teleost skeletal muscles. Almost all other vertebrate striated muscles, including mammalian heart muscles, have a statistical superlattice structure. The high degree of filament lattice order in teleost cardiac muscles indicates their potential usefulness for ultrastructural studies. It is shown that, in four-line M-bands in which the central (M1) M-bridges are missing, interactions at M4 (M4') are sufficient to define the different myosin filament orientations in simple lattice and superlattice A-bands. However the presence of M1 bridges may improve the axial order of the A-band.

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Section: Cardiac M-band Appearancesmentioning

confidence: 69%

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

Pask

Jones

Luther

et al. 1994

J Muscle Res Cell Motil

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“…Generally 9,15,23,24 The expression of myomesin and that of M-protein were correlated to the appearance of the prominent M4/M4′ lines and the variable M1 line, respectively. 9,16,25 Our results suggest that the presence of myomesin 3 might be responsible for the M6/M6′ lines in the M-band.…”

Section: Discussionmentioning

confidence: 95%

“…Indeed, the expression of myomesin 3 in type IIA fibers and its localisation to the M-band of the sarcomere fit well into this picture and correlate with the appearance of the M6/M6′ lines in fibers of intermediate speed. 24,26 According to a recent study, myomesin forms antiparallel dimers via its last C-terminal domain. 11 Sequence comparison of the C-terminal Ig domains of myomesin, M-protein and myomesin 3 displayed a high level of identity within the protein family and throughout evolution.…”

Section: Discussionmentioning

confidence: 98%

Myomesin 3, a Novel Structural Component of the M-band in Striated Muscle

Schoenauer

Lange

Hirschy

et al. 2008

Journal of Molecular Biology

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“…1C). The number and composition of lines vary by fiber type (640). Myosin-based thick filaments are cross-linked in the M-band via “M-bridges” composed of myomesin.…”

Section: M-band: Cross-links Myosin Filaments and Acts As A Hub For Mmentioning

confidence: 99%

Overview of the Muscle Cytoskeleton

Henderson

Gomez

Novak

et al. 2017

Comprehensive Physiology

220

193

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Cardiac and skeletal striated muscles are intricately designed machines responsible for muscle contraction. Coordination of the basic contractile unit, the sarcomere, and the complex cytoskeletal networks are critical for contractile activity. The sarcomere is comprised of precisely organized individual filament systems that include thin (actin), thick (myosin), titin, and nebulin. Connecting the sarcomere to other organelles (e.g., mitochondria and nucleus) and serving as the scaffold to maintain cellular integrity are the intermediate filaments. The costamere, on the other hand, tethers the sarcomere to the cell membrane. Unique structures like the intercalated disc in cardiac muscle and the myotendinous junction in skeletal muscle help synchronize and transmit force. Intense investigation has been done on many of the proteins that make up these cytoskeletal assemblies. Yet the details of their function and how they interconnect have just started to be elucidated. A vast number of human myopathies are contributed to mutations in muscle proteins; thus understanding their basic function provides a mechanistic understanding of muscle disorders. In this review, we highlight the components of striated muscle with respect to their interactions, signaling pathways, functions, and connections to disease.

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

Cited by 22 publications

References 27 publications

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

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

Myomesin 3, a Novel Structural Component of the M-band in Striated Muscle

Overview of the Muscle Cytoskeleton

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