Troponin and titin coordinately regulate length-dependent activation in skinned porcine ventricular muscle

Takako Terui, Munguntsetseg Sodnomtseren, Douchi Matsuba, Jun Udaka, Shin'Ichi Ishiwata, Iwao Ohtsuki, Satoshi Kurihara, Norio Fukuda

    Research output: Contribution to journalArticle

    38 Citations (Scopus)

    Abstract

    We investigated the molecular mechanism by which troponin (Tn) regulates the Frank-Starling mechanism of the heart. Quasi-complete reconstitution of thin filaments with rabbit fast skeletal Tn (sTn) attenuated length-dependent activation in skinned porcine left ventricular muscle, to a magnitude similar to that observed in rabbit fast skeletal muscle. The rate of force redevelopment increased upon sTn reconstitution at submaximal levels, coupled with an increase in Ca2+ sensitivity of force, suggesting the acceleration of cross-bridge formation and, accordingly, a reduction in the fraction of resting cross-bridges that can potentially produce additional active force. An increase in titin-based passive force, induced by manipulating the prehistory of stretch, enhanced length-dependent activation, in both control and sTn-reconstituted muscles. Furthermore, reconstitution of rabbit fast skeletal muscle with porcine left ventricular Tn enhanced length-dependent activation, accompanied by a decrease in Ca2+ sensitivity of force. These findings demonstrate that Tn plays an important role in the Frank-Starling mechanism of the heart via on-off switching of the thin filament state, in concert with titin-based regulation.

    Original languageEnglish
    Pages (from-to)275-283
    Number of pages9
    JournalJournal of General Physiology
    Volume131
    Issue number3
    DOIs
    Publication statusPublished - 2008 Mar

    Fingerprint

    Connectin
    Troponin
    Swine
    Starlings
    Muscles
    Rabbits
    Skeletal Muscle

    ASJC Scopus subject areas

    • Physiology

    Cite this

    Terui, T., Sodnomtseren, M., Matsuba, D., Udaka, J., Ishiwata, SI., Ohtsuki, I., ... Fukuda, N. (2008). Troponin and titin coordinately regulate length-dependent activation in skinned porcine ventricular muscle. Journal of General Physiology, 131(3), 275-283. https://doi.org/10.1085/jgp.200709895

    Troponin and titin coordinately regulate length-dependent activation in skinned porcine ventricular muscle. / Terui, Takako; Sodnomtseren, Munguntsetseg; Matsuba, Douchi; Udaka, Jun; Ishiwata, Shin'Ichi; Ohtsuki, Iwao; Kurihara, Satoshi; Fukuda, Norio.

    In: Journal of General Physiology, Vol. 131, No. 3, 03.2008, p. 275-283.

    Research output: Contribution to journalArticle

    Terui, T, Sodnomtseren, M, Matsuba, D, Udaka, J, Ishiwata, SI, Ohtsuki, I, Kurihara, S & Fukuda, N 2008, 'Troponin and titin coordinately regulate length-dependent activation in skinned porcine ventricular muscle', Journal of General Physiology, vol. 131, no. 3, pp. 275-283. https://doi.org/10.1085/jgp.200709895
    Terui, Takako ; Sodnomtseren, Munguntsetseg ; Matsuba, Douchi ; Udaka, Jun ; Ishiwata, Shin'Ichi ; Ohtsuki, Iwao ; Kurihara, Satoshi ; Fukuda, Norio. / Troponin and titin coordinately regulate length-dependent activation in skinned porcine ventricular muscle. In: Journal of General Physiology. 2008 ; Vol. 131, No. 3. pp. 275-283.
    @article{4c3754547dbb4c5c9232b02f8f111353,
    title = "Troponin and titin coordinately regulate length-dependent activation in skinned porcine ventricular muscle",
    abstract = "We investigated the molecular mechanism by which troponin (Tn) regulates the Frank-Starling mechanism of the heart. Quasi-complete reconstitution of thin filaments with rabbit fast skeletal Tn (sTn) attenuated length-dependent activation in skinned porcine left ventricular muscle, to a magnitude similar to that observed in rabbit fast skeletal muscle. The rate of force redevelopment increased upon sTn reconstitution at submaximal levels, coupled with an increase in Ca2+ sensitivity of force, suggesting the acceleration of cross-bridge formation and, accordingly, a reduction in the fraction of resting cross-bridges that can potentially produce additional active force. An increase in titin-based passive force, induced by manipulating the prehistory of stretch, enhanced length-dependent activation, in both control and sTn-reconstituted muscles. Furthermore, reconstitution of rabbit fast skeletal muscle with porcine left ventricular Tn enhanced length-dependent activation, accompanied by a decrease in Ca2+ sensitivity of force. These findings demonstrate that Tn plays an important role in the Frank-Starling mechanism of the heart via on-off switching of the thin filament state, in concert with titin-based regulation.",
    author = "Takako Terui and Munguntsetseg Sodnomtseren and Douchi Matsuba and Jun Udaka and Shin'Ichi Ishiwata and Iwao Ohtsuki and Satoshi Kurihara and Norio Fukuda",
    year = "2008",
    month = "3",
    doi = "10.1085/jgp.200709895",
    language = "English",
    volume = "131",
    pages = "275--283",
    journal = "Journal of General Physiology",
    issn = "0022-1295",
    publisher = "Rockefeller University Press",
    number = "3",

    }

    TY - JOUR

    T1 - Troponin and titin coordinately regulate length-dependent activation in skinned porcine ventricular muscle

    AU - Terui, Takako

    AU - Sodnomtseren, Munguntsetseg

    AU - Matsuba, Douchi

    AU - Udaka, Jun

    AU - Ishiwata, Shin'Ichi

    AU - Ohtsuki, Iwao

    AU - Kurihara, Satoshi

    AU - Fukuda, Norio

    PY - 2008/3

    Y1 - 2008/3

    N2 - We investigated the molecular mechanism by which troponin (Tn) regulates the Frank-Starling mechanism of the heart. Quasi-complete reconstitution of thin filaments with rabbit fast skeletal Tn (sTn) attenuated length-dependent activation in skinned porcine left ventricular muscle, to a magnitude similar to that observed in rabbit fast skeletal muscle. The rate of force redevelopment increased upon sTn reconstitution at submaximal levels, coupled with an increase in Ca2+ sensitivity of force, suggesting the acceleration of cross-bridge formation and, accordingly, a reduction in the fraction of resting cross-bridges that can potentially produce additional active force. An increase in titin-based passive force, induced by manipulating the prehistory of stretch, enhanced length-dependent activation, in both control and sTn-reconstituted muscles. Furthermore, reconstitution of rabbit fast skeletal muscle with porcine left ventricular Tn enhanced length-dependent activation, accompanied by a decrease in Ca2+ sensitivity of force. These findings demonstrate that Tn plays an important role in the Frank-Starling mechanism of the heart via on-off switching of the thin filament state, in concert with titin-based regulation.

    AB - We investigated the molecular mechanism by which troponin (Tn) regulates the Frank-Starling mechanism of the heart. Quasi-complete reconstitution of thin filaments with rabbit fast skeletal Tn (sTn) attenuated length-dependent activation in skinned porcine left ventricular muscle, to a magnitude similar to that observed in rabbit fast skeletal muscle. The rate of force redevelopment increased upon sTn reconstitution at submaximal levels, coupled with an increase in Ca2+ sensitivity of force, suggesting the acceleration of cross-bridge formation and, accordingly, a reduction in the fraction of resting cross-bridges that can potentially produce additional active force. An increase in titin-based passive force, induced by manipulating the prehistory of stretch, enhanced length-dependent activation, in both control and sTn-reconstituted muscles. Furthermore, reconstitution of rabbit fast skeletal muscle with porcine left ventricular Tn enhanced length-dependent activation, accompanied by a decrease in Ca2+ sensitivity of force. These findings demonstrate that Tn plays an important role in the Frank-Starling mechanism of the heart via on-off switching of the thin filament state, in concert with titin-based regulation.

    UR - http://www.scopus.com/inward/record.url?scp=40849097709&partnerID=8YFLogxK

    UR - http://www.scopus.com/inward/citedby.url?scp=40849097709&partnerID=8YFLogxK

    U2 - 10.1085/jgp.200709895

    DO - 10.1085/jgp.200709895

    M3 - Article

    C2 - 18299397

    AN - SCOPUS:40849097709

    VL - 131

    SP - 275

    EP - 283

    JO - Journal of General Physiology

    JF - Journal of General Physiology

    SN - 0022-1295

    IS - 3

    ER -