Evidence map›Paper›PMID 12562996›Full record

ArticleThe Journal of physiology2003

Orthologous myosin isoforms and scaling of shortening velocity with body size in mouse, rat, rabbit and human muscles.

M A Pellegrino, M Canepari, R Rossi, G D'Antona, C Reggiani, R Bottinelli

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed
4.6field-weighted citation impact, top 4% of its field
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

101 citing papers in PubMed, 216 citations in OpenAlex.

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  6. Research into the physiology of myosins - a personal odyssey.European journal of translational myology · 2025
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  10. Sexual dimorphisms in skeletal muscle: current concepts and research horizons.Journal of applied physiology (Bethesda, Md. : 1985) · 2024
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  14. Exercise metabolism and adaptation in skeletal muscle.Nature reviews. Molecular cell biology · 2023
    Review
  15. Developmental, physiologic and phylogenetic perspectives on the expression and regulation of myosin heavy chains in mammalian skeletal muscles.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2023
    Review
  16. Stochastic survival of the densest and mitochondrial DNA clonal expansion in aging.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  17. Article
  18. From fibre to function: are we accurately representing muscle architecture and performance?Biological reviews of the Cambridge Philosophical Society · 2022
    Review
  19. Article
  20. Effect of Myosin Isoforms on Cardiac Muscle Twitch of Mice, Rats and Humans.International journal of molecular sciences · 2022
    Article

41 more citing papers are in PubMed but not listed here.

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

6 authors at 2 institutions in 1 country.

M A PellegrinoDepartment of Experimental Medicine, Human Physiology Unit, University of Pavia, Pavia, Italy.
M Canepari
R Rossi
G D'Antona
C Reggiani
R Bottinelli
University of Pavia · ITUniversity of Padua · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Maximum shortening velocity (V(0)) was determined in single fibres dissected from hind limb skeletal muscles of rabbit and mouse and classified according to their myosin heavy chain (MHC) isoform composition. The values for rabbit and mouse V(0) were compared with the values previously obtained in man and rat under identical experimental conditions. Significant differences in V(0) were found between fibres containing corresponding myosin isoforms in different species: as a general rule for each isoform V(0) decreased with body mass. Myosin isoform distributions of soleus and tibialis anterior were analysed in mouse, rat, rabbit and man: the proportion of slow myosin generally increased with increasing body size. The diversity between V(0) of corresponding myosin isoforms and the different myosin isoform composition of corresponding muscles determine the scaling of shortening velocity of whole muscles with body size, which is essential for optimisation of locomotion. The speed of actin translocation (V(f)) in in vitro motility assay was determined with myosins extracted from single muscle fibres of all four species: significant differences were found between myosin isoforms in each species and between corresponding myosin isoforms in different species. The values of V(0) and V(f) determined for each myosin isoform were significantly correlated, strongly supporting the view that the myosin isoform expressed is the major determinant of maximum shortening velocity in muscle fibres.

Indexed as

AnimalsBody ConstitutionHumansIsoenzymesMiceMuscle ContractionMuscle Fibers, SkeletalMyosin Heavy ChainsRabbitsRatsSpecies SpecificityTime FactorsIsoenzymesMyosin Heavy Chains

Identifiers

PMID12562996
PMCPMC2342590
OpenAlexW2098438164

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.