Titin-based tension in the cardiac sarcomere: Molecular origin and physiological adaptations

Brian R. Anderson, Henk L. Granzier

Research output: Contribution to journalReview article

48 Scopus citations

Abstract

The passive stiffness of cardiac muscle plays a critical role in ventricular filling during diastole and is determined by the extracellular matrix and the sarcomeric protein titin. Titin spans from the Z-disk to the M-band of the sarcomere and also contains a large extensible region that acts as a molecular spring and develops passive force during sarcomere stretch. This extensible segment is titin's I-band region, and its force-generating mechanical properties determine titin-based passive tension. The properties of titin's I-band region can be modulated by isoform splicing and post-translational modification and are intimately linked to diastolic function. This review discusses the physical origin of titin-based passive tension, the mechanisms that alter titin stiffness, and titin's role in stress-sensing signaling pathways.

Original languageEnglish (US)
Pages (from-to)204-217
Number of pages14
JournalProgress in Biophysics and Molecular Biology
Volume110
Issue number2-3
DOIs
StatePublished - Oct 1 2012

Keywords

  • Connectin
  • Entropic force
  • Mechanical signaling
  • Passive tension

ASJC Scopus subject areas

  • Biophysics
  • Molecular Biology

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