Evidence map›Paper›PMID 20559861›Full record

ArticleJournal of muscle research and cell motility2010

The role of tropomyosin isoforms and phosphorylation in force generation in thin-filament reconstituted bovine cardiac muscle fibres.

Xiaoying Lu, David H Heeley, Lawrence B Smillie, Masataka Kawai

Open access · greenAbstract read
In one paragraph

Article in Journal of muscle research and cell motility, 2010. 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
1.9field-weighted citation impact, top 14% 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, 31 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Phosphorylation of tropomyosin in striated muscle.Journal of muscle research and cell motility · 2013
    Review
  14. Review
  15. Tropomyosin Ser-283 pseudo-phosphorylation slows myofibril relaxation.Archives of biochemistry and biophysics · 2013
    Article
  16. Article
  17. Article
  18. Article
  19. Structural and functional aspects of the myosin essential light chain in cardiac muscle contraction.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011
    Article
  20. 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

4 authors at 3 institutions in 2 countries.

Xiaoying LuDepartment of Anatomy and Cell Biology, University of Iowa, Iowa City, IA 52242, USA. xiaoying-lu@uiowa.edu
David H Heeley
Lawrence B Smillie
Masataka Kawai
University of Iowa · USMemorial University of Newfoundland · CAUniversity of Alberta · CA

Funding

Role of actin domains in force generation in myocardiumR01HL070041 · NHLBI · UNIVERSITY OF IOWA · PI KAWAI, MASATAKA · 2002 to 2011
$2.5M
CIHRNHLBI NIH HHS HL70041NHLBI NIH HHS R01 HL070041
6 · The paper itself

Abstract

The thin filament extraction and reconstitution protocol was used to investigate the functional roles of tropomyosin (Tm) isoforms and phosphorylation in bovine myocardium. The thin filament was extracted by gelsolin, reconstituted with G-actin, and further reconstituted with cardiac troponin together with one of three Tm varieties: phosphorylated alphaTm (alphaTm.P), dephosphorylated alphaTm (alphaTm.deP), and dephosphorylated betaTm (betaTm.deP). The effects of Ca, phosphate, MgATP and MgADP concentrations were examined in the reconstituted fibres at pH 7.0 and 25 degrees C. Our data show that Ca(2+) sensitivity (pCa(50): half saturation point) was increased by 0.19 +/- 0.07 units when betaTm.deP was used instead of alphaTm.deP (P < 0.05), and by 0.27 +/- 0.06 units when phosphorylated alphaTm was used (P < 0.005). The cooperativity (Hill factor) decreased (but insignificantly) from 3.2 +/- 0.3 (5) to 2.8 +/- 0.2 (7) with phosphorylation. The cooperativity decreased significantly from 3.2 +/- 0.3 (5) to 2.1 +/- 0.2 (9) with isoform change from alphaTm.deP to betaTm.deP. There was no significant difference in isometric tension or stiffness between alphaTm.P, alphaTm.deP, and betaTm.deP muscle fibres at saturating [Ca(2+)] or after rigor induction. Based on the six-state cross-bridge model, sinusoidal analysis indicated that the equilibrium constants of elementary steps differed up to 1.7x between alphaTm.deP and betaTm.deP, and up to 2.0x between alphaTm.deP and alphaTm.P. The rate constants differed up to 1.5x between alphaTm.deP and betaTm.deP, and up to 2.4x between alphaTm.deP and alphaTm.P. We conclude that tension and stiffness per cross-bridge are not significantly different among the three muscle models.

Indexed as

ActinsAdenosine DiphosphateAdenosine TriphosphateAnimalsCalciumCattleHeartMyofibrilsPhosphatesPhosphorylationProtein IsoformsTropomyosinTroponinActinsAdenosine DiphosphateAdenosine TriphosphateCalciumPhosphatesProtein IsoformsTropomyosinTroponin

Identifiers

PMID20559861
PMCPMC3089900
OpenAlexW1971253387

What OpenQuestion holds

Textmetadata
LicenceTDM
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.