Evidence map›Paper›PMID 11227794›Full record

ArticleJournal of muscle research and cell motility2000

Jaw-closing muscles of kangaroos express alpha-cardiac myosin heavy chain.

J F Hoh, Y Kim, L G Sieber, W W Zhong, C A Lucas

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of muscle research and cell motility, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.4field-weighted citation impact, top 33% 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

16 citing papers in PubMed, 30 citations in OpenAlex.

  1. Research into the physiology of myosins - a personal odyssey.European journal of translational myology · 2025
    Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Developmental changes in ventricular myosin isoenzymes of the tammar wallaby.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2007
    Article
  12. Marsupial cardiac myosins are similar to those of eutherians in subunit composition and in the correlation of their expression with body size.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2007
    Article
  13. Article
  14. Myosin isoforms and fibre types in jaw-closing muscles of Australian marsupials.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2006
    Article
  15. Article
  16. 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 1 institution in 1 country.

J F HohDepartment of Physiology and Institute for Biomedical Research, The University of Sydney, NSW, Australia. joeh@physiol.usyd.edu.au
Y Kim
L G Sieber
W W Zhong
C A Lucas
University of Sydney · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The masseter muscle of eutherian grazing mammals typically express beta or slow myosin heavy chain (MyHC). Myosins in the masseter of 4 species of kangaroos and a slow limb muscle of one of them were compared with their cardiac myosin by pyrophosphate and sodium dodecyl sulphate (SDS) gel electrophoresis, immunoblotting and immunohistochemistry. It was found that ventricular muscle contains three isoforms homologous to V1 (alpha-MyHC homodimer), V2 (heterodimer) and V3 (beta-MyHC homodimer) of eutherian cardiac muscle, and that the masseter contained V1, with traces of V2 and V3, in great contrast to eutherian ruminants, which express only V3. A polyclonal antibody (anti-KJM) was raised in rabbits against red kangaroo masseter myosin. After cross-absorption against limb muscle myofibrils, anti-KJM specifically reacted in Westerns with MyHCs from masseter but not limb muscles, and immunohistochemically with masseter, but not limb muscle fibers. In pyrophosphate Western blots, anti-KJM reacted with V1 but not with V3. However, a monoclonal antibody specific for eutherian slow myosin stained all kangaroo slow muscle fibers but only weakly stained scattered fibers in the masseter. The SDS-PAGE revealed that light chain composition of masseter and ventricular myosins is identical, but isoforms of both light chains of kangaroo limb slow myosin were observed. These results confirm that kangaroo jaw muscle express alpha-MyHC rather than beta-MyHC. The difference in MyHC gene expression between marsupial and eutherian grazers may be related to the fact that kangaroos are not ruminants, and have only a single chance to comminute food into fine particles, hence the need for the greater speed and power of muscle contraction associated with V1 containing muscle fibers.

Indexed as

MacropodidaeAnimalsJawMuscle, SkeletalMyosin Heavy ChainsMyosin Heavy Chains

Identifiers

PMID11227794
OpenAlexW68510221

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.