The mechanically active domain of titin in cardiac muscle

Károly Trombitás, Jian Ping Jin, Henk Granzier

Research output: Contribution to journalArticlepeer-review

117 Scopus citations


One of the main contributors to passive tension of the myocardium is titin. However, it is not exactly known what portions of this ≃1 μm-long molecule are anchored in the sarcomere (hence, are rendered inelastic) and what portions are elastic (hence, are mechanically active in developing passive tension). We assessed the length of the elastic domain of cardiac titin by ultrastructural and mechanical methods. Single cardiac myocytes were stretched by various amounts, and while in the stretched state, they were processed for immunoelectron microscopy. Several monoclonal anti-titin antibodies were used, and the locations of the titin epitopes in the sarcomere were studied as a function of sarcomere length. Only a small fraction (5% to 10%) of the ≃1000-nm-long molecule behaved elastically under physiological conditions. This mechanically active domain is located close to the A/I junction, and its contour length when unstretched is estimated at ≃50 to 100 nm. In sarcomeres that are slack (length ≃1.85 μm), the mechanically active domain is folded on top of itself, and the length of the domain reaches an elastic limit of ≃550 nm in sarcomeres that are ≃2.9 μm long.

Original languageEnglish (US)
Pages (from-to)856-861
Number of pages6
JournalCirculation research
Issue number4
StatePublished - Oct 1995


  • cardiac myocytes
  • elasticity
  • immunoelectron microscopy
  • passive tension
  • titin

ASJC Scopus subject areas

  • Physiology
  • Cardiology and Cardiovascular Medicine


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