Protein catabolism and impairment of skeletal muscle insulin signalling in heart failure

2010 ◽  
Vol 119 (11) ◽  
pp. 465-466 ◽  
Author(s):  
P. Christian Schulze

Derangements in systemic and local metabolism develop in patients with CHF [chronic HF (heart failure)] and contribute to the progression of the disease. Impaired skeletal muscle metabolism, morphology and function leading to exercise intolerance are hallmarks of the syndrome of CHF. These changes result in abnormal glucose and lipid metabolism, and the associated insulin resistance, which contribute to progression of skeletal muscle catabolism and development of muscle atrophy in patients with advanced HF. In the present issue of Clinical Science, Toth and co-workers demonstrate the impairment of skeletal muscle protein metabolism in patients with HF, and specifically show an impaired anabolic response in the skeletal muscle of these patients following a period of nutritional deficiency.

1999 ◽  
Vol 39 (1) ◽  
pp. 61-74 ◽  
Author(s):  
Jean Grizard ◽  
Dominique Dardevet ◽  
Michèle Balage ◽  
Daniel Larbaud ◽  
Sandrine Sinaud ◽  
...  

2019 ◽  
Vol 49 (11) ◽  
pp. 1637-1650 ◽  
Author(s):  
Olivia E. Knowles ◽  
Brad Aisbett ◽  
Luana C. Main ◽  
Eric J. Drinkwater ◽  
Liliana Orellana ◽  
...  

2004 ◽  
Vol 36 (Supplement) ◽  
pp. S323
Author(s):  
Masao Mizuno ◽  
Tokuko Mizuno ◽  
Keitaro Matsumoto ◽  
Bo Dilling-Hansen ◽  
Axel Lahoz ◽  
...  

1973 ◽  
Vol 136 (3) ◽  
pp. 773-780
Author(s):  
S. Daniel Alexis ◽  
Vernon R. Young

1. Crude polyribosomes from skeletal muscle of the hind leg of rats fed on a low-protein diet for 10 days are less active in cell-free protein synthesis than are polyribosomes obtained from well-nourished control rats. 2. The polyribosomes were salt-washed (0.5m-NH4Cl) and the wash extract was examined for its amino acid incorporating activity and for EF (elongation factor) 1 and EF 2 activities. 3. Compared with preparations from control rats, the salt-wash fraction from protein-depleted rats was less active and showed lower EF 1 and EF 2 activity. 4. The ribosomes were rendered equal in activity by salt-washing, but no inhibitor was detected in the salt wash. 5. Differences in the incorporating activity of crude polyribosomes from the diet groups persisted in the presence of saturating amounts of partially purified EF 1 and EF 2. 6. It is concluded that the lowered protein-synthetic activity of crude polyribosomes caused by restricted protein intake is not causally related to the lower activities of EF 1 and EF 2 in the polyribosome preparations. 7. The possible nature of the change in crude polyribosome activity due to low-protein feeding is discussed.


1995 ◽  
Vol 8 (1) ◽  
pp. 67-91 ◽  
Author(s):  
Jean Grizard ◽  
Dominique Dardevet ◽  
Isabelle Papet ◽  
Laurent Mosoni ◽  
Philippe Patureau Mirand ◽  
...  

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