Chronic hypobaric hypoxia mediated skeletal muscle atrophy: role of ubiquitin–proteasome pathway and calpains

2012 ◽  
Vol 364 (1-2) ◽  
pp. 101-113 ◽  
Author(s):  
Pooja Chaudhary ◽  
Geetha Suryakumar ◽  
Rajendra Prasad ◽  
Som Nath Singh ◽  
Shakir Ali ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Atrophy ◽  
Hypobaric Hypoxia ◽  
Skeletal Muscle Atrophy ◽  
Ubiquitin Proteasome Pathway ◽  
Ubiquitin Proteasome ◽  
Proteasome Pathway

Mergla K + channel induces skeletal muscle atrophy by activating the ubiquitin proteasome pathway

2006 ◽  
Vol 20 (9) ◽  
pp. 1531-1533 ◽  
Author(s):  
Xun Wang ◽  
Gregory H. Hockerman ◽  
Henry W. Green ◽  
Charles F. Babbs ◽  
Sulma I. Mohammad ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Atrophy ◽  
Skeletal Muscle Atrophy ◽  
K Channel ◽  
Ubiquitin Proteasome Pathway ◽  
Ubiquitin Proteasome ◽  
Proteasome Pathway

Role of the ubiquitin-proteasome pathway in muscle atrophy in cachexia

2008 ◽  
Vol 2 (4) ◽  
pp. 262-266 ◽  
Author(s):  
Didier Attaix ◽  
Lydie Combaret ◽  
Daniel Béchet ◽  
Daniel Taillandier
Keyword(s):  
Muscle Atrophy ◽  
Ubiquitin Proteasome Pathway ◽  
Ubiquitin Proteasome ◽  
Proteasome Pathway

scholarly journals The Molecular Mechanisms of Calpains Action on Skeletal Muscle Atrophy

2016 ◽  
pp. 547-560 ◽  
Author(s):  
J. HUANG ◽  
X. ZHU
Keyword(s):  
Skeletal Muscle ◽  
Muscle Atrophy ◽  
Molecular Mechanisms ◽  
Muscle Protein ◽  
Therapeutic Interventions ◽  
Skeletal Muscle Atrophy ◽  
Akt Phosphorylation ◽  
Downstream Effects ◽  
Ubiquitin Proteasome ◽  
Proteasome Pathway

Skeletal muscle atrophy is associated with a loss of muscle protein which may result from both increased proteolysis and decreased protein synthesis. Investigations on cell signaling pathways that regulate muscle atrophy have promoted our understanding of this complicated process. Emerging evidence implicates that calpains play key roles in dysregulation of proteolysis seen in muscle atrophy. Moreover, studies have also shown that abnormally activated calpain results muscle atrophy via its downstream effects on ubiquitin-proteasome pathway (UPP) and Akt phosphorylation. This review will discuss the role of calpains in regulation of skeletal muscle atrophy mainly focusing on its collaboration with either UPP or Akt in atrophy conditions in hope to stimulate the interest in development of novel therapeutic interventions for skeletal muscle atrophy.

scholarly journals Role of altered proteostasis network in chronic hypobaric hypoxia induced skeletal muscle atrophy

PLoS ONE ◽  
2018 ◽  
Vol 13 (9) ◽  
pp. e0204283 ◽  
Author(s):  
Akanksha Agrawal ◽  
Richa Rathor ◽  
Ravi Kumar ◽  
Geetha Suryakumar ◽  
Lilly Ganju
Keyword(s):  
Skeletal Muscle ◽  
Muscle Atrophy ◽  
Hypobaric Hypoxia ◽  
Skeletal Muscle Atrophy

scholarly journals High Fat Diet-Induced Skeletal Muscle Wasting Is Decreased by Mesenchymal Stem Cells Administration: Implications on Oxidative Stress, Ubiquitin Proteasome Pathway Activation, and Myonuclear Apoptosis

2016 ◽  
Vol 2016 ◽  
pp. 1-13 ◽  
Author(s):  
Johanna Abrigo ◽  
Juan Carlos Rivera ◽  
Javier Aravena ◽  
Daniel Cabrera ◽  
Felipe Simon ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Skeletal Muscle ◽  
Stem Cells ◽  
Muscle Atrophy ◽  
High Fat Diet ◽  
Muscle Wasting ◽  
High Fat ◽  
Ubiquitin Proteasome Pathway ◽  
Ubiquitin Proteasome ◽  
Proteasome Pathway

Obesity can lead to skeletal muscle atrophy, a pathological condition characterized by the loss of strength and muscle mass. A feature of muscle atrophy is a decrease of myofibrillar proteins as a result of ubiquitin proteasome pathway overactivation, as evidenced by increased expression of the muscle-specific ubiquitin ligases atrogin-1 and MuRF-1. Additionally, other mechanisms are related to muscle wasting, including oxidative stress, myonuclear apoptosis, and autophagy. Stem cells are an emerging therapy in the treatment of chronic diseases such as high fat diet-induced obesity. Mesenchymal stem cells (MSCs) are a population of self-renewable and undifferentiated cells present in the bone marrow and other mesenchymal tissues of adult individuals. The present study is the first to analyze the effects of systemic MSC administration on high fat diet-induced skeletal muscle atrophy in the tibialis anterior of mice. Treatment with MSCs reduced losses of muscle strength and mass, decreases of fiber diameter and myosin heavy chain protein levels, and fiber type transitions. Underlying these antiatrophic effects, MSC administration also decreased ubiquitin proteasome pathway activation, oxidative stress, and myonuclear apoptosis. These results are the first to indicate that systemically administered MSCs could prevent muscle wasting associated with high fat diet-induced obesity and diabetes.

scholarly journals Chronic contractile activity upregulates the proteasome system in rabbit skeletal muscle

2000 ◽  
Vol 88 (3) ◽  
pp. 1134-1141 ◽  
Author(s):  
George A. Ordway ◽  
P. Darrell Neufer ◽  
Eva R. Chin ◽  
George N. DeMartino
Keyword(s):  
Skeletal Muscle ◽  
Protein Degradation ◽  
Contractile Activity ◽  
Motor Nerve ◽  
Ubiquitin Proteasome System ◽  
Ubiquitin Proteasome Pathway ◽  
Ubiquitin Proteasome ◽  
Proteasome Pathway ◽  
Hydrolysis Of

Remodeling of skeletal muscle in response to altered patterns of contractile activity is achieved, in part, by the regulated degradation of cellular proteins. The ubiquitin-proteasome system is a dominant pathway for protein degradation in eukaryotic cells. To test the role of this pathway in contraction-induced remodeling of skeletal muscle, we used a well-established model of continuous motor nerve stimulation to activate tibialis anterior (TA) muscles of New Zealand White rabbits for periods up to 28 days. Western blot analysis revealed marked and coordinated increases in protein levels of the 20S proteasome and two of its regulatory proteins, PA700 and PA28. mRNA of a representative proteasome subunit also increased coordinately in contracting muscles. Chronic contractile activity of TA also increased total proteasome activity in extracts, as measured by the hydrolysis of a proteasome-specific peptide substrate, and the total capacity of the ubiquitin-proteasome pathway, as measured by the ATP-dependent hydrolysis of an exogenous protein substrate. These results support the potential role of the ubiquitin-proteasome pathway of protein degradation in the contraction-induced remodeling of skeletal muscle.

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