Evidence map›Paper›PMID 16192301›Full record

ArticleAmerican journal of physiology. Cell physiology2006

Coupled expression of troponin T and troponin I isoforms in single skeletal muscle fibers correlates with contractility.

Marco A Brotto, Brandon J Biesiadecki, Leticia S Brotto, Thomas M Nosek, Jian-Ping Jin

Open access · greenAbstract read
In one paragraph

Article in American journal of physiology. Cell physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

35 citing papers in PubMed, 69 citations in OpenAlex.

  1. Review
  2. Article
  3. Targeting mitochondrial CaThe Journal of physiology · 2024
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  5. A Novel Variant inInternational journal of molecular sciences · 2023
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  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. The CaThe Journal of physiology · 2017
    Article
  15. Article
  16. Article
  17. Influence of ageing and essential amino acids on quantitative patterns of troponin T alternative splicing in human skeletal muscle.Applied physiology, nutrition, and metabolism = Physiologie appliquee, nutrition et metabolisme · 2015
    Article
  18. Article
  19. Article
  20. Mechanical properties of respiratory muscles.Comprehensive Physiology · 2013
    Review
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 2 institutions in 1 country.

Marco A BrottoDepartment of Physiology and Biophysics, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA.
Brandon J Biesiadecki
Leticia S Brotto
Thomas M Nosek
Jian-Ping Jin
Case Western Reserve University · USUniversity School · US

Funding

Role of Troponin T Isoforms in Nemaline MyopathyR01AR048816 · NIAMS · WAYNE STATE UNIVERSITY · PI JIN, JIAN-PING · 2003 to 2014
$3.2M
Myofilament Protein Isoforms in Neuromuscular ReflexR21HD044824 · NICHD · NORTHSHORE UNIV HEALTHSYSTEM RES INST · PI JIN, JIAN-PING · 2003 to 2005
$457k
NIAMS NIH HHS AR-048816NIAMS NIH HHS R01 AR048816NICHD NIH HHS HD-044824NICHD NIH HHS R21 HD044824
6 · The paper itself

Abstract

Striated muscle contraction is powered by actin-activated myosin ATPase. This process is regulated by Ca(2+) via the troponin complex. Slow- and fast-twitch fibers of vertebrate skeletal muscle express type I and type II myosin, respectively, and these myosin isoenzymes confer different ATPase activities, contractile velocities, and force. Skeletal muscle troponin has also diverged into fast and slow isoforms, but their functional significance is not fully understood. To investigate the expression of troponin isoforms in mammalian skeletal muscle and their functional relationship to that of the myosin isoforms, we concomitantly studied myosin, troponin T (TnT), and troponin I (TnI) isoform contents and isometric contractile properties in single fibers of rat skeletal muscle. We characterized a large number of Triton X-100-skinned single fibers from soleus, diaphragm, gastrocnemius, and extensor digitorum longus muscles and selected fibers with combinations of a single myosin isoform and a single class (slow or fast) of the TnT and TnI isoforms to investigate their role in determining contractility. Types IIa, IIx, and IIb myosin fibers produced higher isometric force than that of type I fibers. Despite the polyploidy of adult skeletal muscle fibers, the expression of fast or slow isoforms of TnT and TnI is tightly coupled. Fibers containing slow troponin had higher Ca(2+) sensitivity than that of the fast troponin fibers, whereas fibers containing fast troponin showed a higher cooperativity of Ca(2+) activation than that of the slow troponin fibers. These results demonstrate distinct but coordinated regulation of troponin and myosin isoform expression in skeletal muscle and their contribution to the contractile properties of muscle.

Indexed as

Muscle Fibers, SkeletalMuscle, SkeletalActin CytoskeletonAnimalsCalciumMaleMuscle ContractionMyosin Heavy ChainsProtein IsoformsRatsRats, Sprague-DawleyTroponin ITroponin TCalciumMyosin Heavy ChainsProtein IsoformsTroponin ITroponin T

Identifiers

PMID16192301
PMCPMC1409758
OpenAlexW1969306642

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.