A rapid electrophoretic method for separating rabbit skeletal muscle myosin heavy chains at high resolution

1997 ◽  
Vol 18 (1) ◽  
pp. 64-66 ◽  
Author(s):  
Hans-Peter Kubis ◽  
Gerolf Gros
Keyword(s):  
Skeletal Muscle ◽  
High Resolution ◽  
Rabbit Skeletal Muscle ◽  
Myosin Heavy Chains ◽  
Electrophoretic Method ◽  
Skeletal Muscle Myosin ◽  
Heavy Chains ◽  
Muscle Myosin

Skeletal muscle myosin heavy chains in heart failureCorrelation between magnitude of the isozyme shift, exercise capacity, and gas exchange measurements

1998 ◽  
Vol 135 (1) ◽  
pp. 130-137 ◽  
Author(s):  
Giorgio Vescovo ◽  
Francesco Serafini ◽  
Luciano Dalla Libera ◽  
Cristiana Leprotti ◽  
Luigi Facchin ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Gas Exchange ◽  
Exercise Capacity ◽  
Myosin Heavy Chains ◽  
Skeletal Muscle Myosin ◽  
Heavy Chains ◽  
Muscle Myosin

scholarly journals Properties of the non-specific calcium-binding sites of rabbit skeletal-muscle myosin

1980 ◽  
Vol 185 (1) ◽  
pp. 265-268 ◽  
Author(s):  
J Wikman-Coffelt
Keyword(s):  
Skeletal Muscle ◽  
Light Chain ◽  
Binding Sites ◽  
Calcium Binding ◽  
Light Chains ◽  
Binding Properties ◽  
Skeletal Muscle Myosin ◽  
Heavy Chains ◽  
Calcium Binding Sites ◽  
Muscle Myosin

The non-specific Ca2+-binding sites of skeletal-muscle myosin are located on the light chains; with the dissociation of light chains there is a corresponding decrease in the number of Ca2+-binding sites on light-chain-deficient myosin. The released light chains have a decreased binding affinity. Myosin heavy chains indirectly influence the Ca2+-binding properties of light chains by increasing the affinity of light chains for bivalent cations; this influence varies with pH. Because of light-chain dissociation at low Ca2+ and/or Mg2+ concentrations, anomalies may exist when analyses of non-specific Ca2+-binding properties of myosin are assessed by dialysis equilibrium.

scholarly journals The P-light chain of rabbit skeletal muscle myosin: A 31 P NMR study

FEBS Letters ◽  
1980 ◽  
Vol 117 (1-2) ◽  
pp. 199-202 ◽  
Author(s):  
B. Koppitz ◽  
K. Feldmann ◽  
L.M.G. Heilmeyer
Keyword(s):  
Skeletal Muscle ◽  
Light Chain ◽  
Rabbit Skeletal Muscle ◽  
Skeletal Muscle Myosin ◽  
Nmr Study ◽  
Muscle Myosin

scholarly journals Skeletal myosin heavy chain function in cultured lung myofibroblasts

2003 ◽  
Vol 163 (1) ◽  
pp. 119-129 ◽  
Author(s):  
Nancy A. Rice ◽  
Leslie A. Leinwand
Keyword(s):  
Skeletal Muscle ◽  
Promoter Activity ◽  
Molecular Mechanisms ◽  
Smooth Muscle Actin ◽  
Myogenic Regulatory Factor ◽  
Skeletal Muscle Myosin ◽  
Heavy Chains ◽  
Skeletal Myosin ◽  
Muscle Genes ◽  
Muscle Myosin

Myofibroblasts are unique contractile cells with both muscle and nonmuscle properties. Typically myofibroblasts are identified by the expression of α smooth muscle actin (ASMA); however some myofibroblasts also express sarcomeric proteins. In this study, we show that pulmonary myofibroblasts express three of the eight known sarcomeric myosin heavy chains (MyHCs) (IIa, IId, and embryonic) and that skeletal muscle myosin enzymatic activity is required for pulmonary myofibroblast contractility. Furthermore, inhibition of skeletal myosin activity and myofibroblast contraction results in a decrease in both ASMA and skeletal MyHC promoter activity and ASMA protein expression, suggesting a potential coupling of skeletal myosin activity and ASMA expression in myofibroblast differentiation. To understand the molecular mechanisms whereby skeletal muscle genes are regulated in myofibroblasts, we have found that members of the myogenic regulatory factor family of transcription factors and Ca2+-regulated pathways are involved in skeletal MyHC promoter activity. Interestingly, the regulation of skeletal myosin expression in myofibroblasts is distinct from that observed in muscle cells and suggests that cell context is important in its control.

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