Maximal ATPase activity and calcium sensitivity of reconstituted myofilaments are unaltered by the fetal troponin T re-expressed during human heart failure

Jose R. Torrealba, Emilio Lozano, Michael Griffin, Scott Stoker, Kerry McDonald, Marion Greaser, Matthew R. Wolff

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Re-expression of a fetal isoform of troponin T (TnT4) has been demonstrated in failing human ventricular myocardium and associated with a decrease in myofibrillar ATPase activity. In order to elucidate the regulatory role of the re-expressed TnT4 in the failing human heart, we measured ATPase activity in reconstituted cardiac myofilaments prepared with recombinant human TnT4 or the adult human isoform of troponin T (TnT3). Neither the maximal calcium-activated ATPase activity nor the calcium sensitivity of this biochemical assay was significantly different between reconstituted myofilaments containing adult TnT3 or fetal TnT4. Our results suggest that the re-expressed fetal TnT4 is not responsible for the depressed ATPase activity of failing ventricular myofibrils. The increased expression of the fetal isoform of this thin filament regulatory protein in the failing ventricle may be a consequence of a programmed change in gene expression occurring in response to hemodynamic stress, but probably does not contribute to depressed ventricular function characteristic of dilated cardiomyopathies.

Original languageEnglish (US)
Pages (from-to)797-805
Number of pages9
JournalJournal of Molecular and Cellular Cardiology
Volume34
Issue number7
DOIs
StatePublished - Jul 1 2002

Fingerprint

Troponin T
Myofibrils
Adenosine Triphosphatases
Heart Failure
Calcium
Protein Isoforms
Ventricular Function
Calcium-Transporting ATPases
Dilated Cardiomyopathy
Myocardium
Hemodynamics
Gene Expression
Proteins

Keywords

  • Calcium sensitivity
  • Contractile proteins
  • Heart failure
  • Human cardiac troponin T
  • Myofilaments
  • Myosin ATPase
  • Troponin T isoforms

ASJC Scopus subject areas

  • Molecular Biology
  • Cardiology and Cardiovascular Medicine

Cite this

Maximal ATPase activity and calcium sensitivity of reconstituted myofilaments are unaltered by the fetal troponin T re-expressed during human heart failure. / Torrealba, Jose R.; Lozano, Emilio; Griffin, Michael; Stoker, Scott; McDonald, Kerry; Greaser, Marion; Wolff, Matthew R.

In: Journal of Molecular and Cellular Cardiology, Vol. 34, No. 7, 01.07.2002, p. 797-805.

Research output: Contribution to journalArticle

Torrealba, Jose R. ; Lozano, Emilio ; Griffin, Michael ; Stoker, Scott ; McDonald, Kerry ; Greaser, Marion ; Wolff, Matthew R. / Maximal ATPase activity and calcium sensitivity of reconstituted myofilaments are unaltered by the fetal troponin T re-expressed during human heart failure. In: Journal of Molecular and Cellular Cardiology. 2002 ; Vol. 34, No. 7. pp. 797-805.
@article{26155782b8914748a63f661bc90afbe1,
title = "Maximal ATPase activity and calcium sensitivity of reconstituted myofilaments are unaltered by the fetal troponin T re-expressed during human heart failure",
abstract = "Re-expression of a fetal isoform of troponin T (TnT4) has been demonstrated in failing human ventricular myocardium and associated with a decrease in myofibrillar ATPase activity. In order to elucidate the regulatory role of the re-expressed TnT4 in the failing human heart, we measured ATPase activity in reconstituted cardiac myofilaments prepared with recombinant human TnT4 or the adult human isoform of troponin T (TnT3). Neither the maximal calcium-activated ATPase activity nor the calcium sensitivity of this biochemical assay was significantly different between reconstituted myofilaments containing adult TnT3 or fetal TnT4. Our results suggest that the re-expressed fetal TnT4 is not responsible for the depressed ATPase activity of failing ventricular myofibrils. The increased expression of the fetal isoform of this thin filament regulatory protein in the failing ventricle may be a consequence of a programmed change in gene expression occurring in response to hemodynamic stress, but probably does not contribute to depressed ventricular function characteristic of dilated cardiomyopathies.",
keywords = "Calcium sensitivity, Contractile proteins, Heart failure, Human cardiac troponin T, Myofilaments, Myosin ATPase, Troponin T isoforms",
author = "Torrealba, {Jose R.} and Emilio Lozano and Michael Griffin and Scott Stoker and Kerry McDonald and Marion Greaser and Wolff, {Matthew R.}",
year = "2002",
month = "7",
day = "1",
doi = "10.1006/jmcc.2002.2016",
language = "English (US)",
volume = "34",
pages = "797--805",
journal = "Journal of Molecular and Cellular Cardiology",
issn = "0022-2828",
publisher = "Academic Press Inc.",
number = "7",

}

TY - JOUR

T1 - Maximal ATPase activity and calcium sensitivity of reconstituted myofilaments are unaltered by the fetal troponin T re-expressed during human heart failure

AU - Torrealba, Jose R.

AU - Lozano, Emilio

AU - Griffin, Michael

AU - Stoker, Scott

AU - McDonald, Kerry

AU - Greaser, Marion

AU - Wolff, Matthew R.

PY - 2002/7/1

Y1 - 2002/7/1

N2 - Re-expression of a fetal isoform of troponin T (TnT4) has been demonstrated in failing human ventricular myocardium and associated with a decrease in myofibrillar ATPase activity. In order to elucidate the regulatory role of the re-expressed TnT4 in the failing human heart, we measured ATPase activity in reconstituted cardiac myofilaments prepared with recombinant human TnT4 or the adult human isoform of troponin T (TnT3). Neither the maximal calcium-activated ATPase activity nor the calcium sensitivity of this biochemical assay was significantly different between reconstituted myofilaments containing adult TnT3 or fetal TnT4. Our results suggest that the re-expressed fetal TnT4 is not responsible for the depressed ATPase activity of failing ventricular myofibrils. The increased expression of the fetal isoform of this thin filament regulatory protein in the failing ventricle may be a consequence of a programmed change in gene expression occurring in response to hemodynamic stress, but probably does not contribute to depressed ventricular function characteristic of dilated cardiomyopathies.

AB - Re-expression of a fetal isoform of troponin T (TnT4) has been demonstrated in failing human ventricular myocardium and associated with a decrease in myofibrillar ATPase activity. In order to elucidate the regulatory role of the re-expressed TnT4 in the failing human heart, we measured ATPase activity in reconstituted cardiac myofilaments prepared with recombinant human TnT4 or the adult human isoform of troponin T (TnT3). Neither the maximal calcium-activated ATPase activity nor the calcium sensitivity of this biochemical assay was significantly different between reconstituted myofilaments containing adult TnT3 or fetal TnT4. Our results suggest that the re-expressed fetal TnT4 is not responsible for the depressed ATPase activity of failing ventricular myofibrils. The increased expression of the fetal isoform of this thin filament regulatory protein in the failing ventricle may be a consequence of a programmed change in gene expression occurring in response to hemodynamic stress, but probably does not contribute to depressed ventricular function characteristic of dilated cardiomyopathies.

KW - Calcium sensitivity

KW - Contractile proteins

KW - Heart failure

KW - Human cardiac troponin T

KW - Myofilaments

KW - Myosin ATPase

KW - Troponin T isoforms

UR - http://www.scopus.com/inward/record.url?scp=0036660874&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036660874&partnerID=8YFLogxK

U2 - 10.1006/jmcc.2002.2016

DO - 10.1006/jmcc.2002.2016

M3 - Article

C2 - 12099719

AN - SCOPUS:0036660874

VL - 34

SP - 797

EP - 805

JO - Journal of Molecular and Cellular Cardiology

JF - Journal of Molecular and Cellular Cardiology

SN - 0022-2828

IS - 7

ER -