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Keywords: Titin
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Journal Articles
J Exp Biol (2022) 225 (21): jeb244962.
Published: 4 November 2022
...) when cross-bridge cycling is inhibited, possibly because of the contribution of the elastic force produced by titin. * Author for correspondence ( afr15171@fc.ritsumei.ac.jp ) Competing interests The authors declare no competing or financial interests. 2 9 2022 11 10 2022...
Journal Articles
J Exp Biol (2022) 225 (10): jeb244011.
Published: 30 May 2022
... strong cross-bridge binding. Cross-bridge cycling Slow stretch Fast stretch Muscle slipping Titin Three filament sarcomere model Canada Research Chairs http://dx.doi.org/10.13039/501100001804 Killam Trusts http://dx.doi.org/10.13039/501100004073 Natural...
Journal Articles
J Exp Biol (2022) 225 (10): jeb243732.
Published: 26 May 2022
... deletion in N2A titin, has been proposed to prevent N2A titin–actin interactions so that active mdm muscles are more compliant than wild type (WT). This decrease in active muscle stiffness is associated with reduced RFE. We investigated RFE in permeabilized soleus (SOL) and extensor digitorum longus (EDL...
Journal Articles
J Exp Biol (2021) 224 (19): jeb225086.
Published: 4 October 2021
...: Here, we consider insights into muscle mechanics based on new ideas about the giant protein titin as a tunable viscoelastic element in active muscles, and discuss implications for design and control of robotic prostheses. Muscle mechanics Muscle models Preflex Titin W. M. Keck...
Journal Articles
J Exp Biol (2019) 222 (13): jeb206557.
Published: 28 June 2019
... energy Attached cross-bridges Soleus Sarcomere Titin Residual force enhancement The mechanical work during a concentric contraction (shortening) phase is increased when shortening is preceded by muscle stretching. This increase in work during a stretch–shortening cycle (SSC) has been called...
Journal Articles
J Exp Biol (2018) 221 (22): jeb182089.
Published: 16 November 2018
...Gretchen Meyer; Richard L. Lieber ABSTRACT Differences in passive muscle mechanical properties between amphibians and mammals have led to differing hypotheses on the functional role of titin in skeletal muscle. Early studies of frog muscle clearly demonstrated intracellular load bearing by titin...
Journal Articles
Journal Articles
J Exp Biol (2016) 219 (2): 183–188.
Published: 1 January 2016
.... Titin, the missing filament in the sliding filament model, is a muscle spring, which functions very differently in cardiac versus skeletal muscle; its possible role in these two muscle types is discussed relative to their contrasting function. The good news for those of us who choose to work on skeletal...
Journal Articles
J Exp Biol (2016) 219 (2): 153–160.
Published: 1 January 2016
... to a calcium-dependent stiffening of a non-crossbridge sarcomere structure, such as the titin filament. According to this hypothesis, titin, in addition to its well-recognized role in determining the muscle passive tension, could have a role during muscle activity. Titin is the largest protein (3–4 MDa...
Journal Articles
J Exp Biol (2016) 219 (2): 135–145.
Published: 1 January 2016
... cytoskeleton proteins and their roles in dissipating mechanical forces in order to maintain sarcomere integrity during passive extension and active contraction. α-Actinin crosslinks in the Z-disk show a pivot-and-rod structure that anchors both titin and actin filaments. In contrast, the myosin crosslinks...
Journal Articles
J Exp Biol (2014) 217 (20): 3629–3636.
Published: 15 October 2014
... produced during muscle activation is proportional to the amount of filament overlap. Previous studies from our laboratory demonstrated enhanced titin-based force in myofibrils that were actively stretched to lengths which exceeded filament overlap. This observation cannot be explained by the sliding...
Journal Articles
J Exp Biol (2014) 217 (16): 2825–2833.
Published: 15 August 2014
... the properties of isometrically and concentrically contracting muscle, it has failed miserably in explaining experimental observations in eccentric contractions. Here, I suggest, and provide evidence, that a third filament, titin, is involved in force regulation of sarcomeres by adjusting its stiffness...
Journal Articles
J Exp Biol (2014) 217 (14): 2445–2448.
Published: 15 July 2014
... was disrupted. Following passive recovery, SLs returned to 82% SL 0 , creating a region of double-overlapping actin filaments. Recovery required recoil of intracellular titin filaments, elastic cytoskeletal components for realigning myofibrils, and muscle activation. Stretch of whole muscles exceeded...
Includes: Supplementary data
Journal Articles
J Exp Biol (2012) 215 (15): 2551–2559.
Published: 1 August 2012
...Timothy F. Tirrell; Mark S. Cook; J. Austin Carr; Evie Lin; Samuel R. Ward; Richard L. Lieber SUMMARY The molecular components largely responsible for muscle attributes such as passive tension development (titin and collagen), active tension development (myosin heavy chain, MHC...
Includes: Supplementary data
Journal Articles
J Exp Biol (2003) 206 (20): 3635–3643.
Published: 15 October 2003
... that is governed by the length of the contractile components, possibly the sarcomeres. Based on these results, the molecular spring titin emerges as a possible candidate for the passive component of the steady-state force enhancement observed in this and previous studies. References Abbott, B. C. and Aubert...
Journal Articles
J Exp Biol (2002) 205 (15): 2211–2216.
Published: 1 August 2002
... to result in enhanced force, work or power outputs. We present data that support the concept that this ability of muscle to store and recover elastic strain energy is an adaptable property of skeletal muscle. Further, we speculate that a crucial element in that muscle spring may be the protein titin. It too...
Journal Articles
J Exp Biol (1999) 202 (4): 393–406.
Published: 15 February 1999
... studies have shown these fibres to have the lowest passive stiffness and the largest titin isoform, allowing them to attain large strain amplitudes with relatively low passive tensions. * e-mail: Igor.Spierts@morf.edc.wau.nl 23 11 1998 21 01 1999 © 1999 by Company...