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Cited by 40Muscle Physiology and DisordersCardiomyopathy and Myosin StudiesMeat and Animal Product Quality

Myosin: Formation and maintenance of thick filaments

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Ojima, Koichi·2019·Animal Science Journal
DOI 10.1111/asj.13226PMC PMC6618170
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Abstract

Skeletal muscle consists of bundles of myofibers containing millions of myofibrils, each of which is formed of longitudinally aligned sarcomere structures. Sarcomeres are the minimum contractile unit, which mainly consists of four components: Z‐bands, thin filaments, thick filaments, and connectin/titin. The size and shape of the sarcomere component is strictly controlled. Surprisingly, skeletal muscle cells not only synthesize a series of myofibrillar proteins but also regulate the assembly of those proteins into the sarcomere structures. However, authentic sarcomere structures cannot be reconstituted by combining purified myofibrillar proteins in vitro, therefore there must be an elaborate mechanism ensuring the correct formation of myofibril structure in skeletal muscle cells. This review discusses the role of myosin, a main component of the thick filament, in thick filament formation and the dynamics of myosin in skeletal muscle cells. Changes in the number of myofibrils in myofibers can cause muscle hypertrophy or atrophy. Therefore, it is important to understand the fundamental mechanisms by which myofibers control myofibril formation at the molecular level to develop approaches that effectively enhance muscle growth in animals.

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  • In the transverse direction, the myosin myofilaments are assembled in ordered hexagonal lattices.

    “In the transverse direction, the myosin myofilaments are assembled in ordered hexagonal lattices (SI Appendix, Fig. S25) (32).”

    From Light diffraction by sarcomeres produces iridescence in transmission in the transparent ghost catfish (2023) · cites this paper as [32]

    The Introduction sections on myofibril structure and myosin assembly describe a highly ordered sarcomere and organized myosin thick filaments. They do not describe the filaments’ transverse arrangement as a hexagonal lattice (searched: “hexagonal lattice transverse thick filaments” and “hexagonal”). The reference to a myosin molecule as a hexamer concerns its components, not its lattice arrangement. Page numbers were unavailable in our copy. (LLM, conf=0.82)

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Cited by

Sorted by citations

Authors
Ojima, K.
Affiliations
National Agriculture and Food Research Organization (JP)
Corresponding author
Ojima, Koichi
ORCID
Ojima, Koichi
Venue
Animal Science Journal
Publisher
Wiley
Published
2019-05-27
Volume
90
Issue
7
Pages
801-807
ISSN
  • 1344-3941 (ISSN-L)
  • 1740-0929
DOI
10.1111/asj.13226
PMC
PMC6618170
OpenAlex
W2947168641
Cited by
40
References
0
Citations by year
2026: 4 · 2025: 7 · 2024: 6 · 2023: 8 · 2022: 3 · 2021: 5 · 2020: 5 · 2019: 2
FWCI
0.34
Type
journal article
Language
en
Open access
Licence
Locations
  • Animal Science Journal (publishedVersion, cc-by-nc)
  • PubMed Central (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
  • Institutional Repositories DataBase (IRDB) (submittedVersion, cc-by-nc-nd)
Funders
  • Japan Society for the Promotion of Science (16K08079, 22580301)
  • Uehara Memorial Foundation
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
  • Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiomyopathy and Myosin Studies
  • Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Meat and Animal Product Quality
Keywords
myosin, thick filaments, myofibril assembly, sarcomere, skeletal muscle, myofibrillar proteins, muscle fibers, muscle hypertrophy, muscle atrophy, muscle growth
MeSH terms
Animals, Atrophy, Cytoskeleton, Hypertrophy, Myofibrils, Myosins, Sarcomeres, Muscle, Skeletal

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