Evidence map›Paper›PMID 14609030›Full record

ReviewJournal of muscle research and cell motility2003

M-band: a safeguard for sarcomere stability?

Irina Agarkova, Elisabeth Ehler, Stephan Lange, Roman Schoenauer, Jean-Claude Perriard

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of muscle research and cell motility, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

34 citing papers in PubMed.

  1. Article
  2. Article
  3. Sarcomere maturation: function acquisition, molecular mechanism, and interplay with other organelles.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2022
    Review
  4. Nanosurgical Manipulation of Titin and Its M-Complex.Nanomaterials (Basel, Switzerland) · 2022
    Article
  5. Article
  6. Identification ofDisease models & mechanisms · 2020
    Article
  7. Article
  8. Overview of the Muscle Cytoskeleton.Comprehensive Physiology · 2017
    Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Force is a signal that cells cannot ignore.Molecular biology of the cell · 2014
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Fast-folding alpha-helices as reversible strain absorbers in the muscle protein myomesin.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  19. Cytoskeletal protein kinases: titin and its relations in mechanosensing.Pflugers Archiv : European journal of physiology · 2011
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Irina AgarkovaInstitute of Cell Biology, ETH-Zurich Hoenggerberg, CH-8093 Zurich, Switzerland.
Elisabeth Ehler
Stephan Lange
Roman Schoenauer
Jean-Claude Perriard

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The sarcomere of striated muscle is a very efficient machine transforming chemical energy into movement. However, a wrong distribution of the generated forces may lead to self-destruction of the engine itself. A well-known example for this is eccentric contraction (elongation of the sarcomere in the activated state), which damages sarcomeric structure and leads to a reduced muscle performance. The goal of this review is to discuss the involvement of different cytoskeletal systems, in particular the M-band filaments, in the mechanisms that provide stability during sarcomeric contraction. The M-band is the transverse structure in the center of the sarcomeric A-band, which is responsible both for the regular packing of thick filaments and for the uniform distribution of the tension over the myosin filament lattice in the activated sarcomere. Although some proteins from the Ig-superfamily, like myomesin and M-protein, are the major candidates for the role of M-band bridges, the exact molecular organisation of the M-band is not clear. However, the protein composition of the M-band seems to modulate the mechanical characteristics of the thick filament lattice, in particular its stiffness, adjusting it to the specific demands in different muscle types. The special M-band design in slow fibers might be part of structural adaptations, favouring sarcomere stability for a continuous contractile activity over a broad working range. In conclusion, we discuss why the interference with M-band structure might have fatal consequences for the integrity of the working sarcomere.

Indexed as

AnimalsConnectinCytoskeletonElasticityHumansModels, BiologicalMuscle ContractionMuscle Fibers, Fast-TwitchMuscle Fibers, Slow-TwitchMuscle ProteinsMuscle, SkeletalMyofibrilsProtein IsoformsProtein KinasesSarcomeresSignal TransductionConnectinMuscle ProteinsProtein IsoformsProtein KinasesTTN protein, human

Identifiers

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.