Purification and Some Properties of a Myofibrillar Protein-Degrading Protease, Cathepsin L, from Rabbit Skeletal Muscle1

1987 ◽  
Vol 86 (4) ◽  
pp. 379-383 ◽  
Author(s):  
M. A. J. Taylor ◽  
R. E. almond ◽  
D. J. Etherington

2005 ◽  
Vol 41 ◽  
pp. 173-186 ◽  
Author(s):  
Didier Attaix ◽  
Sophie Ventadour ◽  
Audrey Codran ◽  
Daniel Béchet ◽  
Daniel Taillandier ◽  
...  

The ubiquitin–proteasome system (UPS) is believed to degrade the major contractile skeletal muscle proteins and plays a major role in muscle wasting. Different and multiple events in the ubiquitination, deubiquitination and proteolytic machineries are responsible for the activation of the system and subsequent muscle wasting. However, other proteolytic enzymes act upstream (possibly m-calpain, cathepsin L, and/or caspase 3) and downstream (tripeptidyl-peptidase II and aminopeptidases) of the UPS, for the complete breakdown of the myofibrillar proteins into free amino acids. Recent studies have identified a few critical proteins that seem necessary for muscle wasting {i.e. the MAFbx (muscle atrophy F-box protein, also called atrogin-1) and MuRF-1 [muscle-specific RING (really interesting new gene) finger 1] ubiquitin–protein ligases}. The characterization of their signalling pathways is leading to new pharmacological approaches that can be useful to block or partially prevent muscle wasting in human patients.


1960 ◽  
Vol 235 (10) ◽  
pp. 2797-2800
Author(s):  
Patricia Z. Thomas ◽  
Enrico Forchielli ◽  
Ralph I. Dorfman

1993 ◽  
Vol 268 (20) ◽  
pp. 14687-14693 ◽  
Author(s):  
Y. Cao ◽  
A.M. Mahrenholz ◽  
A.A. DePaoli-Roach ◽  
P.J. Roach

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