Evidence map›Paper›PMID 16443664›Full record

ArticleBiophysical journal2006

Troponin T modulates sarcomere length-dependent recruitment of cross-bridges in cardiac muscle.

Murali Chandra, Matthew L Tschirgi, Indika Rajapakse, Kenneth B Campbell

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
1.8field-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

38 citing papers in PubMed, 48 citations in OpenAlex.

  1. Sarcomere length-dependent effects on CaThe Journal of general physiology · 2019
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  15. Cardiovascular engineering and technology · 2013
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  18. Interplay between the overlapping ends of tropomyosin and the N terminus of cardiac troponin T affects tropomyosin states on actin.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013
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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 1 institution in 1 country.

Murali ChandraDepartment of Veterinary and Comparative Anatomy, Pharmacology and Physiology, Washington State University, Pullman, 99164-6520, USA. murali@vetmed.wsu.edu
Matthew L Tschirgi
Indika Rajapakse
Kenneth B Campbell
Washington State University · US

Funding

Mechanistic Understanding of Troponin T Role in Cardiac Thin Filament ActivationR01HL075643 · NHLBI · WASHINGTON STATE UNIVERSITY · PI CHANDRA, MURALI · 2004 to 2012
$2.7M
NHLBI NIH HHS HL-075643NHLBI NIH HHS R01 HL075643
6 · The paper itself

Abstract

The heterogenic nature of troponin T (TnT) isoforms in fast skeletal and cardiac muscle suggests important functional differences. Dynamic features of rat cardiac TnT (cTnT) and rat fast skeletal TnT (fsTnT) reconstituted cardiac muscle preparations were captured by fitting the force response of small amplitude (0.5%) muscle length changes to the recruitment-distortion model. The recruitment of force-bearing cross-bridges (XBs) by increases in muscle length was favored by cTnT. The recruitment magnitude was approximately 1.5 times greater for cTnT- than for fsTnT-reconstituted muscle fibers. The speed of length-mediated XB recruitment (b) in cTnT-reconstituted muscle fiber was 0.50-0.57 times as fast as fsTnT-reconstituted muscle fibers (3.05 vs. 5.32 s(-1) at sarcomere length, SL, of 1.9 microm and 4.16 vs. 8.36 s(-1) at SL of 2.2 microm). Due to slowing of b in cTnT-reconstituted muscle fibers, the frequency of minimum stiffness (f(min)) was shifted to lower frequencies of muscle length changes (at SL of 1.9 microm, 0.64 Hz, and 1.16 Hz for cTnT- and fsTnT-reconstituted muscle fibers, respectively; at SL of 2.2 microm, 0.79 Hz, and 1.11 Hz for cTnT- and fsTnT-reconstituted muscle fibers, respectively). Our model simulation of the data implicates TnT as a participant in the process by which SL- and XB-regulatory unit cooperative interactions activate thin filaments. Our data suggest that the amino-acid sequence differences in cTnT may confer a heart-specific regulatory role. cTnT may participate in tuning the heart muscle by decreasing the speed of XB recruitment so that the heart beats at a rate commensurate with f(min).

Indexed as

Models, BiologicalAdenosine TriphosphatasesAnimalsHeartMuscle Fibers, SkeletalMyocardial ContractionMyocardiumProtein IsoformsRatsSarcomeresTroponin ITroponin TAdenosine TriphosphatasesProtein IsoformsTroponin ITroponin T

Identifiers

PMID16443664
PMCPMC1414571
OpenAlexW2079284465

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.