scholarly journals Skeletal myosin light chain kinase regulates skeletal myogenesis by phosphorylation of MEF2C

2011 ◽  
Vol 30 (12) ◽  
pp. 2477-2489 ◽  
Author(s):  
Ashraf Said Al Madhoun ◽  
Virja Mehta ◽  
Grace Li ◽  
Daniel Figeys ◽  
Nadine Wiper-Bergeron ◽  
...  
Keyword(s):  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Skeletal Myogenesis ◽  
Skeletal Myosin

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

2015 ◽  
Vol 93 (1) ◽  
pp. 23-32 ◽  
Author(s):  
William Gittings ◽  
Harish Aggarwal ◽  
James T. Stull ◽  
Rene Vandenboom
Keyword(s):  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Isometric Force ◽  
Conditioning Stimulus ◽  
Mouse Muscle ◽  
Tetanic Force ◽  
Concentric Force ◽  
Skeletal Myosin ◽  
Contraction Type

The isometric potentiation associated with myosin phosphorylation is force dependent. The purpose of this study was to assess the influence of a pre-existing period of isometric force on the concentric force potentiation displayed by mouse muscles with and without the ability to phosphorylate myosin. We tested isometric (ISO) and concentric (CON) potentiation, as well as concentric potentiation after isometric force (ISO-CON), in muscles from wild-type (WT) and skeletal myosin light chain kinase-deficient (skMLCK−/−) mice. A conditioning stimulus increased (i.e., potentiated) mean concentric force in the ISO-CON and CON conditions to 1.31 ± 0.02 and 1.35 ± 0.02 (WT) and to 1.19 ± 0.02 and 1.21 ± 0.01 (skMLCK−/−) of prestimulus levels, respectively (data n = 6–8, p < 0.05). No potentiation of mean isometric force was observed in either genotype. The potentiation of mean concentric force was inversely related to relative tetanic force level (P/Po) in both genotypes. Moreover, concentric potentiation varied greatly within each contraction type and was negatively correlated with unpotentiated force in both genotypes. Thus, although no effect of pre-existing force was observed, strong and inverse relationships between concentric force potentiation and unpotentiated concentric force may suggest an influence of attached and force-generating crossbridges on potentiation magnitude in both WT and skMLCK−/− muscles.

The effect of skeletal myosin light chain kinase gene ablation on the fatigability of mouse fast muscle

2011 ◽  
Vol 31 (5-6) ◽  
pp. 337-348 ◽  
Author(s):  
William Gittings ◽  
Jiang Huang ◽  
Ian C. Smith ◽  
Joe Quadrilatero ◽  
Rene Vandenboom
Keyword(s):  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Fast Muscle ◽  
Kinase Gene ◽  
Gene Ablation ◽  
Skeletal Myosin

scholarly journals Halothane binds to druggable sites in the [Ca2+]4-calmodulin (CaM) complex, but does not inhibit [Ca2+]4-CaM activation of kinase

2013 ◽  
Vol 78 (11) ◽  
pp. 1655-1670 ◽  
Author(s):  
Nenad Juranic ◽  
Keith Jones ◽  
Alan Penheiter ◽  
Thomas Hock ◽  
John Streiff
Keyword(s):  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Volatile Anesthetics ◽  
Recognition Sequence ◽  
Peptide Recognition ◽  
High Resolution Nmr ◽  
Dependent Activity ◽  
Skeletal Myosin ◽  
Muscle Myosin

The mechanism(s) of volatile anesthetics (VA) are poorly understood. We used high resolution NMR spectroscopy to determine the structure of the halothane/calmodulin([Ca2+]4-CaM) complex, and found that halothane molecules bind in the druggable sites. We then examined whether VA binding to druggable sites in calmodulin would effect [Ca2+]4-CaM dependent activity of myosin light chain kinase. We used fluorescence assays to determine that VA effect [Ca2+]4-CaM activation of smooth-muscle-myosin-light-chain-kinase (smMLCK), but not the Kd of [Ca2+]4-CaM binding to skeletal-myosin-light-chain-kinase-peptide recognition sequence (skMLCKp). These results suggest that VA do not alter [Ca2+]4-CaM dependent MLCK activity via direct interactions with [Ca2+]4-CaM.

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