Correlation between myofibrillar ATPase activity and myosin heavy chain composition in single human muscle fibers

1991 ◽  
Vol 96 (1) ◽  
pp. 21-24 ◽  
Author(s):  
R. S. Staron
Keyword(s):  
Atpase Activity ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Muscle Fibers ◽  
Human Muscle ◽  
Myofibrillar Atpase ◽  
Myofibrillar Atpase Activity ◽  
Chain Composition ◽  
Myosin Heavy Chain Composition

Myosin heavy chain composition of muscle fibers in spinal muscular atrophy

1989 ◽  
Vol 12 (1) ◽  
pp. 43-51 ◽  
Author(s):  
Donatella Biral ◽  
Elio Scarpini ◽  
Corrado Angelini ◽  
Giovanni Salviati ◽  
Alfredo Margreth
Keyword(s):  
Spinal Muscular Atrophy ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Muscular Atrophy ◽  
Muscle Fibers ◽  
Chain Composition ◽  
Myosin Heavy Chain Composition

Relationship between calpastatin activity and the slow and fast myosin heavy chain content of ovine skeletal muscles

2002 ◽  
Vol 2002 ◽  
pp. 173-173
Author(s):  
A.Q. Sazili ◽  
P.L. Sensky ◽  
T. Parr ◽  
R.G. Bardsley ◽  
P.J. Buttery
Keyword(s):  
Atpase Activity ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Skeletal Muscles ◽  
Myofibrillar Atpase ◽  
Heavy Chains ◽  
Fast Myosin ◽  
Myofibrillar Atpase Activity ◽  
Fast Myosin Heavy Chain ◽  
The Relationship

Calpastatin, the specific endogenous inhibitor of the calpain system, is considered to be a principle contributor to variations in meat tenderisation (Parr et al., 1999). Previous studies have suggested that the differences in calpastatin activity in different ovine skeletal muscles could be influenced by muscle metabolic and contractile characteristics according to myofibrillar ATPase activity (Ouali and Talmant, 1990). The type of myofibrillar ATPase activity is largely determined by the content of slow or fast myosin heavy chains (Rivero et al., 1999). The present study was designed to investigate the relationship between calpastatin inhibitory activity and slow myosin heavy chain (MHC-s) and fast myosin heavy chain (MHC-f) expression.

Increased myosin phosphorylation in sensitized canine tracheal smooth muscle

1990 ◽  
Vol 259 (2) ◽  
pp. L53-L56 ◽  
Author(s):  
S. K. Kong ◽  
A. J. Halayko ◽  
N. L. Stephens
Keyword(s):  
Smooth Muscle ◽  
Atpase Activity ◽  
Myosin Heavy Chain ◽  
Airway Smooth Muscle ◽  
Heavy Chain ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Tracheal Smooth Muscle ◽  
Myofibrillar Atpase ◽  
Myofibrillar Atpase Activity

We have reported that the maximal velocity of shortening and myofibrillar adenosine triphosphatase (ATPase) activity of antigen-sensitized airway smooth muscle are higher than that of nonsensitized airway smooth muscle (Kong, S. K., R. P. C. Shiu, and N. L. Stephens. J. Appl. Physiol. 60: 92–94, 1986). To extend these studies, we attempted to determine whether the increased myofibrillar ATPase activity from sensitized airway smooth muscle was associated with either a change in distribution of two myosin heavy chain isozymes or an increase in myosin light chain phosphorylation. Myosin heavy chain isozymes from both control and sensitized airway smooth muscle were separated by 4% sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Gels were analyzed by densitometry, which indicated that isozyme band pattern of sensitized airway smooth muscle was not different from that of the control. The maximal levels of phosphorylated myosin light chain from whole cell homogenates of sensitized and control tracheal smooth muscles were 0.65 +/- 0.029 (n = 6) and 0.40 +/- 0.025 mol Pi/mol light chain (n = 6), respectively. The degree of phosphorylation of myosin light chain of sensitized airway smooth muscle was significantly higher than that of the control (P less than 0.05). This study also indicated that increased myofibrillar ATPase activity in sensitized tracheal smooth muscle was correlated with phosphorylation of myosin light chain.

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