scholarly journals Physical training attenuates gene expression of ubiquitin‐proteasome pathway in diabetic mouse skeletal muscle

2007 ◽  
Vol 21 (6) ◽  
Author(s):  
Maarit Lehti ◽  
Mika Silvennoinen ◽  
Riikka Kivelä ◽  
Heikki Kainulainen ◽  
Jyrki Komulainen
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Physical Training ◽  
Diabetic Mouse ◽  
Ubiquitin Proteasome Pathway ◽  
Mouse Skeletal Muscle ◽  
Ubiquitin Proteasome ◽  
Proteasome Pathway

scholarly journals Changes in Ubiquitin Proteasome Pathway Gene Expression in Skeletal Muscle With Exercise and Statins

2005 ◽  
Vol 25 (12) ◽  
pp. 2560-2566 ◽  
Author(s):  
Maria L. Urso ◽  
Priscilla M. Clarkson ◽  
Dustin Hittel ◽  
Eric P. Hoffman ◽  
Paul D. Thompson
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Ubiquitin Proteasome Pathway ◽  
Pathway Gene ◽  
Ubiquitin Proteasome ◽  
Proteasome Pathway

Skeletal muscle mRNA levels for cathepsin B, but not components of the ubiquitin–proteasome pathway, are increased in patients with lung cancer referred for thoracotomy

2002 ◽  
Vol 102 (3) ◽  
pp. 353-361 ◽  
Author(s):  
R. Thomas JAGOE ◽  
Christopher P.F. REDFERN ◽  
Russell G. ROBERTS ◽  
G. John GIBSON ◽  
Timothy H.J. GOODSHIP
Keyword(s):  
Gene Expression ◽  
Lung Cancer ◽  
Skeletal Muscle ◽  
Cathepsin B ◽  
Muscle Wasting ◽  
Fat Free Mass ◽  
Mrna Levels ◽  
Ubiquitin Proteasome Pathway ◽  
Ubiquitin Proteasome ◽  
Proteasome Pathway

Muscle wasting is a common and prominent feature of advanced cancer, including lung cancer. Evidence from animal experiments suggests that accelerated proteolysis via the ubiquitin-proteasome pathway is the primary cause of cancer-related cachexia. However, there are few data on the role of this pathway in determining muscle wasting in human cancer. The present study was designed to measure whether skeletal muscle gene expression of components of the ubiquitin-proteasome pathway and/or the lysosomal proteolytic pathway was increased in patients with early lung cancer. A total of 36 patients with lung cancer referred for curative resection and 10 control subjects had biopsies of latissimus dorsi muscle taken at operation. mRNA levels of four components of the ubiquitin-proteasome pathway, i.e. polyubiquitin, C2α proteasome subunit, 14kDa ubiquitin-carrier protein and ubiquitin-activating protein, and of two lysosomal proteolytic enzymes, i.e. cathepsin B and cathepsin D, were measured using quantitative Northern blotting. mRNA levels for cathepsin B, but not for components of the ubiquitin-proteasome pathway, were higher in patients with cancer compared with controls (P = 0.01). Among lung cancer patients, cathepsin B mRNA levels correlated with fat-free mass index (r =-0.57, P = 0.003) and tumour stage (rs = 0.45, P = 0.03), and were higher in smokers (P = 0.04). Thus gene expression of the lysosomal protease cathepsin B is increased in the skeletal muscle of patients with early lung cancer, and the strong inverse relationship with fat-free mass suggests that cathepsin B may have a role in inducing muscle wasting in the early stages of lung cancer.

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

Mechanisms of Cancer Cachexia

2009 ◽  
Vol 89 (2) ◽  
pp. 381-410 ◽  
Author(s):  
Michael J. Tisdale
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Adipose Tissue ◽  
Protein Degradation ◽  
Initiation Factor ◽  
Tissue Loss ◽  
Α Subunit ◽  
Ubiquitin Proteasome Pathway ◽  
Ubiquitin Proteasome ◽  
Proteasome Pathway

Up to 50% of cancer patients suffer from a progressive atrophy of adipose tissue and skeletal muscle, called cachexia, resulting in weight loss, a reduced quality of life, and a shortened survival time. Anorexia often accompanies cachexia, but appears not to be responsible for the tissue loss, particularly lean body mass. An increased resting energy expenditure is seen, possibly arising from an increased thermogenesis in skeletal muscle due to an increased expression of uncoupling protein, and increased operation of the Cori cycle. Loss of adipose tissue is due to an increased lipolysis by tumor or host products. Loss of skeletal muscle in cachexia results from a depression in protein synthesis combined with an increase in protein degradation. The increase in protein degradation may include both increased activity of the ubiquitin-proteasome pathway and lysosomes. The decrease in protein synthesis is due to a reduced level of the initiation factor 4F, decreased elongation, and decreased binding of methionyl-tRNA to the 40S ribosomal subunit through increased phosphorylation of eIF2 on the α-subunit by activation of the dsRNA-dependent protein kinase, which also increases expression of the ubiquitin-proteasome pathway through activation of NFκB. Tumor factors such as proteolysis-inducing factor and host factors such as tumor necrosis factor-α, angiotensin II, and glucocorticoids can all induce muscle atrophy. Knowledge of the mechanisms of tissue destruction in cachexia should improve methods of treatment.

Ubiquitin proteasome pathway gene expression varies in rhesus monkey oocytes and embryos of different developmental potential

2007 ◽  
Vol 31 (1) ◽  
pp. 1-14 ◽  
Author(s):  
Namdori R. Mtango ◽  
Keith E. Latham
Keyword(s):  
Gene Expression ◽  
Rhesus Monkey ◽  
Early Embryo ◽  
Developmental Competence ◽  
Cell Physiology ◽  
Developmental Potential ◽  
Ubiquitin Proteasome Pathway ◽  
Pathway Gene ◽  
Ubiquitin Proteasome ◽  
Proteasome Pathway

Protein degradation via the ubiquitin-proteasome pathway (UPP) plays a key role in diverse aspects of cell physiology and development. In the early embryo, the UPP may play an important role in the transition from maternal to embryonic control of development. Disruptions in the UPP could thus compromise embryo developmental potential. Additionally, species-specific requirements may dictate diverse patterns of regulation of the UPP components. To investigate the expression of UPP components in a nonhuman primate embryo model, to compare expression between a primate and nonprimate species, and to determine whether disruption of this pathway may contribute to reduced developmental potential, we examined the expression of >50 mRNAs encoding UPP components in rhesus monkey oocytes and embryos. We compared this expression between the rhesus monkey and mouse embryo and between rhesus monkey oocytes and embryos of high, intermediate, and low developmental potential. We report here the temporal patterns of UPP gene expression in oocytes and during preimplantation development, including striking differences between the rhesus monkey and mouse. We also report significant differences in UPP gene expression correlating with oocyte and embryo developmental competence and associated with altered regulation of maternally inherited mRNAs encoding these proteins.

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