Literature DB >> 28251466

Shortening speed dependent force potentiation is attenuated but not eliminated in skeletal muscles without myosin phosphorylation.

William Gittings1, Jordan Bunda1, Rene Vandenboom2.   

Abstract

We investigated the influence of shortening speed on concentric force potentiation at different frequencies in muscles devoid of skeletal myosin light chain kinase (skMLCK-/-) and unable to phosphorylate myosin. EDL muscles from skMLCK-/- mice were activated in vitro (25 °C) across a range of stimulation frequencies (10-100 Hz) during shortening ramps at 0.10, 0.30, or 0.50 of maximum shortening velocity (Vmax) before and after a potentiating stimulus (PS). When collapsed across all frequencies, the PS increased relative (post/pre) concentric force to 1.27 ± 0.02 and 1.17 ± 0.02 of pre-PS values at 0.50 and 0.30 Vmax, respectively (n = 4, P < 0.05 for all speeds). In addition, potentiation was significantly greater at low and intermediate-than at high stimulus frequencies at both speeds. In contrast, during shortening at 0.10 Vmax, a posttetanic depression was observed as mean concentric forces were reduced to 0.85 ± 0.02 of pre-PS values. Thus, although reduced compared to published values for wildtype muscles (Gittings et al., J Muscle Res Cell Motil 33:359-368, 2012), skMLCK-/- muscles displayed a speed dependent potentiation of concentric force during moderate and fast shortening speed at all frequencies tested. Our data support the presence of a myosin phosphorylation-independent mechanism(s) for concentric force potentiation at moderate speeds of shortening, and also suggests that myosin phosphorylation may be necessary to prevent the concentric force depression that may be present at slow speeds of shortening. Although additive in nature, further work is needed to parse out the relative influence of myosin phosphorylation-independent and dependent potentiation mechanisms on wildtype contractile function during dynamic conditions.

Entities:  

Keywords:  Concentric; Force; Myosin; Myosin light chain kinase; Phosphorylation; Potentiation; RLC; Regulatory light chain; SkMLCK; Skeletal muscle

Mesh:

Year:  2017        PMID: 28251466     DOI: 10.1007/s10974-017-9465-9

Source DB:  PubMed          Journal:  J Muscle Res Cell Motil        ISSN: 0142-4319            Impact factor:   2.698


  27 in total

Review 1.  Myosin light chain kinase and the role of myosin light chain phosphorylation in skeletal muscle.

Authors:  James T Stull; Kristine E Kamm; Rene Vandenboom
Journal:  Arch Biochem Biophys       Date:  2011-02-01       Impact factor: 4.013

Review 2.  Fiber types in mammalian skeletal muscles.

Authors:  Stefano Schiaffino; Carlo Reggiani
Journal:  Physiol Rev       Date:  2011-10       Impact factor: 37.312

3.  Tetanic force potentiation of mouse fast muscle is shortening speed dependent.

Authors:  William Gittings; Jian Huang; Rene Vandenboom
Journal:  J Muscle Res Cell Motil       Date:  2012-10-01       Impact factor: 2.698

4.  Staircase in mammalian muscle without light chain phosphorylation.

Authors:  D E Rassier; L A Tubman; B R MacIntosh
Journal:  Braz J Med Biol Res       Date:  1999-01       Impact factor: 2.590

5.  Myosin light chain phosphorylation and tension potentiation in mouse skeletal muscle.

Authors:  B M Palmer; R L Moore
Journal:  Am J Physiol       Date:  1989-11

6.  The force dependence of isometric and concentric potentiation in mouse muscle with and without skeletal myosin light chain kinase.

Authors:  William Gittings; Harish Aggarwal; James T Stull; Rene Vandenboom
Journal:  Can J Physiol Pharmacol       Date:  2015-01       Impact factor: 2.273

Review 7.  Myosin phosphorylation and force potentiation in skeletal muscle: evidence from animal models.

Authors:  Rene Vandenboom; William Gittings; Ian C Smith; Robert W Grange; James T Stull
Journal:  J Muscle Res Cell Motil       Date:  2013-10-27       Impact factor: 2.698

8.  Enhanced skeletal muscle contraction with myosin light chain phosphorylation by a calmodulin-sensing kinase.

Authors:  Jeffrey W Ryder; Kim S Lau; Kristine E Kamm; James T Stull
Journal:  J Biol Chem       Date:  2007-05-15       Impact factor: 5.157

9.  Myosin phosphorylation enhances rate of force development in fast-twitch skeletal muscle.

Authors:  R Vandenboom; R W Grange; M E Houston
Journal:  Am J Physiol       Date:  1995-03

10.  Potentiation in mouse lumbrical muscle without myosin light chain phosphorylation: is resting calcium responsible?

Authors:  Ian C Smith; William Gittings; Jian Huang; Elliott M McMillan; Joe Quadrilatero; A Russell Tupling; Rene Vandenboom
Journal:  J Gen Physiol       Date:  2013-02-11       Impact factor: 4.086

View more
  2 in total

Review 1.  Post-activation Potentiation Versus Post-activation Performance Enhancement in Humans: Historical Perspective, Underlying Mechanisms, and Current Issues.

Authors:  Anthony J Blazevich; Nicolas Babault
Journal:  Front Physiol       Date:  2019-11-01       Impact factor: 4.566

2.  Do Thirty-Second Post-activation Potentiation Exercises Improve the 50-m Freestyle Sprint Performance in Adolescent Swimmers?

Authors:  Zied Abbes; Karim Chamari; Iñigo Mujika; Montassar Tabben; Khalid W Bibi; Ali Mostafa Hussein; Cyril Martin; Monoem Haddad
Journal:  Front Physiol       Date:  2018-10-22       Impact factor: 4.566

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.