Cardiac titin isoforms are coexpressed in the half-sarcomere and extend independently

K. Trombitás, Y. Wu, D. Labeit, S. Labeit, Hendrikus "Henk" Granzier

Research output: Contribution to journalArticle

66 Citations (Scopus)

Abstract

Titin, the third myofilament type of cardiac muscle, contains a molecular spring segment that gives rise to passive forces in stretched myocardium and to restoring forces in shortened myocardium. We studied cardiac titin isoforms (N2B and N2BA) that contain length variants of the molecular spring segment. We investigated how coexpression of isoforms takes place at the level of the half-sarcomere, and whether coexpression affects the extensibility of the isoforms. Immunoelectron microscopy was used to study local coexpression of isoforms in a range of species. It was found that the cardiac sarcomere of large mammals coexpresses N2B and N2BA titin isoforms at the level of the half-sarcomere, and that when coexpressed, the isoforms act independently of one another. Coexpressing isoforms at varying ratios results in modulation of the passive mechanical behavior of the sarcomere without impacting other functions of titin and allows for adjustment of the diastolic properties of the myocardium.

Original languageEnglish (US)
JournalAmerican Journal of Physiology - Heart and Circulatory Physiology
Volume281
Issue number4 50-4
StatePublished - 2001
Externally publishedYes

Fingerprint

Connectin
Sarcomeres
Protein Isoforms
Myocardium
Immunoelectron Microscopy
Myofibrils
Mammals

Keywords

  • Diastole
  • Elasticity
  • Mechanics
  • Physiology
  • Structure

ASJC Scopus subject areas

  • Physiology
  • Physiology (medical)

Cite this

Cardiac titin isoforms are coexpressed in the half-sarcomere and extend independently. / Trombitás, K.; Wu, Y.; Labeit, D.; Labeit, S.; Granzier, Hendrikus "Henk".

In: American Journal of Physiology - Heart and Circulatory Physiology, Vol. 281, No. 4 50-4, 2001.

Research output: Contribution to journalArticle

@article{cabce080c9474d6c923ee59f1ee841dc,
title = "Cardiac titin isoforms are coexpressed in the half-sarcomere and extend independently",
abstract = "Titin, the third myofilament type of cardiac muscle, contains a molecular spring segment that gives rise to passive forces in stretched myocardium and to restoring forces in shortened myocardium. We studied cardiac titin isoforms (N2B and N2BA) that contain length variants of the molecular spring segment. We investigated how coexpression of isoforms takes place at the level of the half-sarcomere, and whether coexpression affects the extensibility of the isoforms. Immunoelectron microscopy was used to study local coexpression of isoforms in a range of species. It was found that the cardiac sarcomere of large mammals coexpresses N2B and N2BA titin isoforms at the level of the half-sarcomere, and that when coexpressed, the isoforms act independently of one another. Coexpressing isoforms at varying ratios results in modulation of the passive mechanical behavior of the sarcomere without impacting other functions of titin and allows for adjustment of the diastolic properties of the myocardium.",
keywords = "Diastole, Elasticity, Mechanics, Physiology, Structure",
author = "K. Trombit{\'a}s and Y. Wu and D. Labeit and S. Labeit and Granzier, {Hendrikus {"}Henk{"}}",
year = "2001",
language = "English (US)",
volume = "281",
journal = "American Journal of Physiology",
issn = "0363-6143",
publisher = "American Physiological Society",
number = "4 50-4",

}

TY - JOUR

T1 - Cardiac titin isoforms are coexpressed in the half-sarcomere and extend independently

AU - Trombitás, K.

AU - Wu, Y.

AU - Labeit, D.

AU - Labeit, S.

AU - Granzier, Hendrikus "Henk"

PY - 2001

Y1 - 2001

N2 - Titin, the third myofilament type of cardiac muscle, contains a molecular spring segment that gives rise to passive forces in stretched myocardium and to restoring forces in shortened myocardium. We studied cardiac titin isoforms (N2B and N2BA) that contain length variants of the molecular spring segment. We investigated how coexpression of isoforms takes place at the level of the half-sarcomere, and whether coexpression affects the extensibility of the isoforms. Immunoelectron microscopy was used to study local coexpression of isoforms in a range of species. It was found that the cardiac sarcomere of large mammals coexpresses N2B and N2BA titin isoforms at the level of the half-sarcomere, and that when coexpressed, the isoforms act independently of one another. Coexpressing isoforms at varying ratios results in modulation of the passive mechanical behavior of the sarcomere without impacting other functions of titin and allows for adjustment of the diastolic properties of the myocardium.

AB - Titin, the third myofilament type of cardiac muscle, contains a molecular spring segment that gives rise to passive forces in stretched myocardium and to restoring forces in shortened myocardium. We studied cardiac titin isoforms (N2B and N2BA) that contain length variants of the molecular spring segment. We investigated how coexpression of isoforms takes place at the level of the half-sarcomere, and whether coexpression affects the extensibility of the isoforms. Immunoelectron microscopy was used to study local coexpression of isoforms in a range of species. It was found that the cardiac sarcomere of large mammals coexpresses N2B and N2BA titin isoforms at the level of the half-sarcomere, and that when coexpressed, the isoforms act independently of one another. Coexpressing isoforms at varying ratios results in modulation of the passive mechanical behavior of the sarcomere without impacting other functions of titin and allows for adjustment of the diastolic properties of the myocardium.

KW - Diastole

KW - Elasticity

KW - Mechanics

KW - Physiology

KW - Structure

UR - http://www.scopus.com/inward/record.url?scp=0034786066&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034786066&partnerID=8YFLogxK

M3 - Article

C2 - 11557573

AN - SCOPUS:0034786066

VL - 281

JO - American Journal of Physiology

JF - American Journal of Physiology

SN - 0363-6143

IS - 4 50-4

ER -