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      Residual force enhancement following shortening is speed-dependent

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          Abstract

          The steady-state isometric force following active muscle shortening or lengthening is smaller (force depression; FD) or greater (residual force enhancement; RFE) than a purely isometric contraction at the corresponding length. The mechanisms underlying these phenomena are not explained within the context of the cross-bridge theory and are rarely studied in concert. Previous studies have shown RFE to be speed-independent. In the present study, we investigated if RFE preceded by active shortening is time-dependent by electrically evoking RFE in the human adductor pollicis muscle. The results shown that a slow stretch following FD fully re-established RFE compared to higher speeds of stretch. The mechanism(s) responsible for the recovery of RFE following a preceding shortening contraction (FD) might be associated with the recovery of cross-bridge based force and/or the re-engagement of a passive structural element (titin). Voluntary interaction with one’s environment involves highly coordinated shortening and lengthening muscle contractions. Therefore comprehending these history-dependent muscle properties in the context of movement control is paramount in understanding the behavior of in vivo motor control.

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          Most cited references26

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          Muscle structure and theories of contraction.

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            Calcium-dependent molecular spring elements in the giant protein titin.

            Titin (also known as connectin) is a giant protein with a wide range of cellular functions, including providing muscle cells with elasticity. Its physiological extension is largely derived from the PEVK segment, rich in proline (P), glutamate (E), valine (V), and lysine (K) residues. We studied recombinant PEVK molecules containing the two conserved elements: approximately 28-residue PEVK repeats and E-rich motifs. Single molecule experiments revealed that calcium-induced conformational changes reduce the bending rigidity of the PEVK fragments, and site-directed mutagenesis identified four glutamate residues in the E-rich motif that was studied (exon 129), as critical for this process. Experiments with muscle fibers showed that titin-based tension is calcium responsive. We propose that the PEVK segment contains E-rich motifs that render titin a calcium-dependent molecular spring that adapts to the physiological state of the cell.
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              Proposed mechanism of force generation in striated muscle.

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                Author and article information

                Journal
                Sci Rep
                Sci Rep
                Scientific Reports
                Nature Publishing Group
                2045-2322
                12 February 2016
                2016
                : 5
                : 21513
                Affiliations
                [1 ]Human Performance Laboratory, Faculty of Kinesiology, University of Calgary , Calgary, Canada
                [2 ]Department of Human Health and Nutritional Sciences, College of Biological Sciences, University of Guelph , Guelph, Ontario, Canada
                [3 ]Department of Biomechanics in Sports, Faculty of Sport and Health Sciences, Technische Universität München , Munich, Germany
                Author notes
                Article
                srep21513
                10.1038/srep21513
                4751464
                26869508
                3b07cb26-a9db-4113-bccf-1daed9f49daf
                Copyright © 2016, Macmillan Publishers Limited

                This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

                History
                : 14 September 2015
                : 20 January 2016
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