Literature DB >> 8601441

Calcium-dependent inhibition of in vitro thin-filament motility by native titin.

M S Kellermayer1, H L Granzier.   

Abstract

Titin ( also known as connectin) is a giant filamentous protein that spans the distance between the Z- and M-lines of the vertebrate muscle sarcomere and plays a fundamental role in the generation of passive tension. Titin has been shown to bind strongly to myosin, making it tightly associated to the thick filament in the sarcomere. Recent observations have suggested the possibility that titin also interacts with actin, implying further functions of titin in muscle contraction. We show -- using in vitro motility and binding assays -- that native titin interacts with both filamentous actin and reconstituted thin filaments. The interaction results in the inhibition of the filaments' in vitro motility. Furthermore, the titin-thin filament interaction occurs in a calcium-dependent manner: increased calcium results in enhanced binding of thin filaments to titin and greater suppression of in vitro motility.

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Year:  1996        PMID: 8601441     DOI: 10.1016/0014-5793(96)00055-5

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  41 in total

1.  Global configuration of single titin molecules observed through chain-associated rhodamine dimers.

Authors:  L Grama; B Somogyi; M S Kellermayer
Journal:  Proc Natl Acad Sci U S A       Date:  2001-11-20       Impact factor: 11.205

2.  Crossbridge and non-crossbridge contributions to tension in lengthening rat muscle: force-induced reversal of the power stroke.

Authors:  G J Pinniger; K W Ranatunga; G W Offer
Journal:  J Physiol       Date:  2006-04-20       Impact factor: 5.182

Review 3.  Stretching and visualizing titin molecules: combining structure, dynamics and mechanics.

Authors:  Miklós S Z Kellermayer; László Grama
Journal:  J Muscle Res Cell Motil       Date:  2002       Impact factor: 2.698

4.  Non-crossbridge calcium-dependent stiffness in slow and fast skeletal fibres from mouse muscle.

Authors:  Marta Nocella; Barbara Colombini; Maria Angela Bagni; Joseph Bruton; Giovanni Cecchi
Journal:  J Muscle Res Cell Motil       Date:  2011-11-10       Impact factor: 2.698

Review 5.  The mechanisms of the residual force enhancement after stretch of skeletal muscle: non-uniformity in half-sarcomeres and stiffness of titin.

Authors:  Dilson E Rassier
Journal:  Proc Biol Sci       Date:  2012-04-25       Impact factor: 5.349

6.  Activation and stretch-induced passive force enhancement--are you pulling my chain? Focus on "Regulation of muscle force in the absence of actin-myosin-based cross-bridge interaction".

Authors:  Henk L Granzier
Journal:  Am J Physiol Cell Physiol       Date:  2010-05-05       Impact factor: 4.249

7.  The increase in non-cross-bridge forces after stretch of activated striated muscle is related to titin isoforms.

Authors:  Anabelle S Cornachione; Felipe Leite; Maria Angela Bagni; Dilson E Rassier
Journal:  Am J Physiol Cell Physiol       Date:  2015-09-24       Impact factor: 4.249

8.  Spatially and temporally synchronized atomic force and total internal reflection fluorescence microscopy for imaging and manipulating cells and biomolecules.

Authors:  Miklós S Z Kellermayer; Arpád Karsai; András Kengyel; Attila Nagy; Pasquale Bianco; Tamás Huber; Agnes Kulcsár; Csaba Niedetzky; Roger Proksch; László Grama
Journal:  Biophys J       Date:  2006-07-21       Impact factor: 4.033

Review 9.  Cardiac titin: a multifunctional giant.

Authors:  Martin M LeWinter; Henk Granzier
Journal:  Circulation       Date:  2010-05-18       Impact factor: 29.690

10.  Titin is a target of matrix metalloproteinase-2: implications in myocardial ischemia/reperfusion injury.

Authors:  Mohammad A M Ali; Woo Jung Cho; Bryan Hudson; Zamaneh Kassiri; Henk Granzier; Richard Schulz
Journal:  Circulation       Date:  2010-11-01       Impact factor: 29.690

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