Protein Synthesis in Isolated Human Skeletal Muscle Tissue: Evaluation of an Experimental Model

1979 ◽  
Vol 57 (2) ◽  
pp. 221-223 ◽  
Author(s):  
K. Lundholm ◽  
T. Scherstén
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Protein Synthesis ◽  
Experimental Model ◽  
Muscle Tissue ◽  
Time Course ◽  
Human Skeletal Muscle ◽  
Skeletal Muscle Tissue ◽  
Muscle Fibres ◽  
Skeletal Muscle Fibres

Amino acids were incorporated into soluble proteins, myosin and myoglobin at constant rates for at least 4 h on incubation of isolated human skeletal muscle fibres. The time course of incorporation of leucine into proteins not attached to ribosomes was approximately constant, suggesting a continuous termination of proteins. A comparison between estimated pool size of ribosomes and incorporation rate of leucine into proteins indicated that initiation of peptides occurred even in the absence of insulin.

Oestrogen receptor β is present in both muscle fibres and endothelial cells within human skeletal muscle tissue

2005 ◽  
Vol 124 (2) ◽  
pp. 161-165 ◽  
Author(s):  
Anna Wiik ◽  
Marianne Ekman ◽  
Gareth Morgan ◽  
Olle Johansson ◽  
Eva Jansson ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Endothelial Cells ◽  
Muscle Tissue ◽  
Oestrogen Receptor ◽  
Human Skeletal Muscle ◽  
Skeletal Muscle Tissue ◽  
Muscle Fibres

Protein Degradation in Human Skeletal Muscle Tissue: The Effect of Insulin, Leucine, Amino Acids and Ions

1981 ◽  
Vol 60 (3) ◽  
pp. 319-326 ◽  
Author(s):  
K. Lundholm ◽  
S. Edström ◽  
L. Ekman ◽  
I. Karlberg ◽  
P. Walker ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Protein Synthesis ◽  
Protein Degradation ◽  
Muscle Tissue ◽  
Human Skeletal Muscle ◽  
Degradation Rate ◽  
Rectus Abdominus ◽  
Protein Degradation Rate

1. The protein degradation rate of human skeletal muscle was evaluated in vitro in isolated fibre bundles from the rectus abdominus muscle by measuring the tyrosine released from muscle tissue proteins. Protein metabolism in this semi-intact preparation was compared with that of the intact extensor digitorum longus muscles from rats under the same experimental conditions. 2. Protein balance was negative in both preparations, but protein synthesis and degradation were two to three times higher in the rat muscles. Tyrosine was released at a constant rate for at least 3 h of incubation independent of whether protein synthesis was inhibited or not. Disintegration of the muscle fibres more than doubled the tyrosine release rate. Human red gastrocnemius muscle showed 37% higher degradation rate compared with the predominantly white rectus abdominus muscle. The half-life of human skeletal muscle protein in vitro was estimated to be 20 days when calculated from the rate of tyrosine release. 3. The addition of leucine to the incubation medium decreased the rate of protein degradation, which was further decreased by the addition of other amino acids. Insulin did not influence the protein degradation rate during 2 h of incubation. This did not reflect a lack of sensitivity to insulin of the preparation, since protein synthesis responded to insulin. Calcium (5 mmol/l) stimulated and zinc (0.1 mmol/l) inhibited the protein degradation. 4. This experimental system may be suitable as an additional tool for evaluating protein degradation in human skeletal muscles.

The role of agrin during the maturation of human skeletal muscle fibres

2006 ◽  
Vol 99 (2-3) ◽  
pp. 1
Author(s):  
Fabio Ruzzier ◽  
Elena Bandi ◽  
Mihaela Jurdana ◽  
Paola Lorenzon ◽  
Marina Sciancalepore
Keyword(s):  
Skeletal Muscle ◽  
Human Skeletal Muscle ◽  
Muscle Fibres ◽  
Skeletal Muscle Fibres
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