Evidence map›Paper›PMID 10412092›Full record

ArticleJournal of muscle research and cell motility1999

Analysis of myosin heavy chains at the protein level in horse skeletal muscle.

J L Rivero, A L Serrano, E Barrey, J P Valette, M Jouglin

Abstract read
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In one paragraph

Article in Journal of muscle research and cell motility, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

20 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
  2. 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
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  5. Immune Response in Young Thoroughbred Racehorses under Training.Animals : an open access journal from MDPI · 2020
    Article
  6. The New Frontier in Oxytocin Physiology: The Oxytonic Contraction.International journal of molecular sciences · 2020
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Contractile properties of muscle fibers from the deep and superficial digital flexors of horses.American journal of physiology. Regulatory, integrative and comparative physiology · 2010
    Article
  16. Immunohistochemical analysis of laryngeal muscles in normal horses and horses with subclinical recurrent laryngeal neuropathy.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2009
    Article
  17. Article
  18. Immunohistochemical analysis of myosin heavy chain expression in laryngeal muscles of the rabbit, cat, and baboon.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2008
    Article
  19. Myosin isoforms and fibre types in limb muscles of Australian marsupials: adaptations to hopping and non-hopping locomotion.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2008
    Article
  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 at 4 institutions in 3 countries.

J L RiveroDepartment of Anatomy, Faculty of Veterinary Science, University of Cordoba, Spain. anllorij@lucano.uco.es
A L Serrano
E Barrey
J P Valette
M Jouglin
École Nationale Vétérinaire d'Alfort · FRDépartement Génétique Animale · FRNational Research Council · ITUniversity of Córdoba · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Combined methodologies of enzyme-linked immunosorbent assay (ELISA), sodium dodecyl sulphate polyacrilamide gel electrophoresis (SDS-PAGE), immunoblotting, traditional myofibrillar ATPase (mATPase) histochemistry and immunocytochemistry of whole biopsied samples were used to study myosin heavy chain (MHC) isoforms in the equine gluteus medius muscle. The ELISA technique allowed the quantification of the three MHC isoforms known to be present in different horse muscles: slow (MHC-I) and two fast (termed MHC-IIA and MCH-IIX). The SDS-PAGE method resolved MHCs in three bands: MHC-I, MHC-IIX and MHC-IIA from the fastest to the slowest migrating band and a quantification by densitometry for each MHC isoform was also possible. The identity of these three MHCs was confirmed by immunoblots with specific monoclonal antibodies. Five fibre types were defined immunohistochemically according to their MHC content: I, I + IIA, IIA, the hybrid IIAX and IIX. When quantitative data obtained with the four different methodologies were combined and compared, they were consistent and, when considered together, showed significant correlation. Nevertheless, the percentage of MHC-IIA histochemically derived was underestimated, while that of MHC-IIX was overestimated in comparison with the immunocytochemical determination of these MHC isoforms. The percentage of MHC-I obtained by ELISA technique was underestimated. In short, these integrated methods for the analysis of MHCs at the protein level demonstrate that equine skeletal muscle does not express the MHC-IIB, so type II fibres have been misclassified in numerous previous studies based upon the vary traditional mATPase histochemistry. They also offer new prospects for muscle fibre typing in equine experimental studies and veterinary medicine.

Indexed as

AnimalsElectrophoresis, Polyacrylamide GelEnzyme-Linked Immunosorbent AssayHorsesImmunohistochemistryMaleMuscle, SkeletalMyosin Heavy ChainsMyosin Heavy Chains

Identifiers

PMID10412092
OpenAlexW80438934

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.