Ubiquitin ligase gene expression in healthy volunteers with 20‐day bedrest

Ogawa, Takayuki; Furochi, Harumi; Mameoka, Mai; Hirasaka, Katsuya; Onishi, Yuko; Suzue, Naoto; Oarada, Motoko; Akamatsu, Motoki; Akima, Hiroshi; Fukunaga, Tetsuo; Kishi, Kazushi; Yasui, Natsuo; Ishidoh, Kazumi; Fukuoka, Hiroshi; Nikawa, Takeshi

doi:10.1002/mus.20611

Cited by 79 publications

(63 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The Cbl-b gene is highly sensitive to mechanical stress (unloading) (30,31). Therefore, we hypothesized that some of the components of the signal transduction pathways that regulate the expression of Cbl-b are important sensors of mechanical stress.…”

Section: Discussionmentioning

confidence: 99%

“…To measure the mRNA amount in small samples, realtime reverse transcription-PCR (RT-PCR) was performed with SYBR green dye using an ABI 7300 real-time PCR system (Applied Biosystems, Foster City, CA) as described previously (31). The oligonucleotide primers used for amplification are listed in Table S3 in the supplemental material.…”

Section: Cbl-b-deficient Mice Mice Deficient In the Cbl-b Gene (Cbl-mentioning

confidence: 99%

See 1 more Smart Citation

Ubiquitin Ligase Cbl-b Is a Negative Regulator for Insulin-Like Growth Factor 1 Signaling during Muscle Atrophy Caused by Unloading

Nakao¹,

Hirasaka²,

Goto³

et al. 2009

Molecular and Cellular Biology

Self Cite

165

164

View full text Add to dashboard Cite

Skeletal muscle atrophy caused by unloading is characterized by both decreased responsiveness to myogenicThe impairment of growth factor signaling is a near-universal feature of skeletal myopathies induced by unloading (6, 13). Clinical trials have established that during unloading, muscle tissue fails to respond to IGF-1, a dominant myotrophic hormone (7,19,34). Under normal conditions and in response to hypertrophic stimuli, IGF-1 promotes muscle growth and suppresses muscle loss largely through the Akt-dependent phosphorylation and cytosolic sequestration of FOXO transcription factors in skeletal myocytes, which leads to the inhibition of FOXO-dependent gene expression (38, 41). In contrast, IGF-1-dependent Akt signaling is impaired during muscle atrophy, which decreases the phosphorylation and increases the transactivation of FOXO target genes. In particular, FOXO regulates the expression of atrophy-related genes (atrogenes) that encode atrogin-1/MAFbx and MuRF-1, which are RING-type ubiquitin ligases that are critical mediators of atrophic myopathies in vivo (3,14). Atrogin-1 and MuRF-1 regulate the degradation of key proteins involved in striated muscle growth and differentiation, including MyoD, calcineurin, and troponin-I (24, 27, 47). Although diminished growth factor responsiveness and enhanced proteolysis both are major atrophyrelated processes, the mechanisms by which skeletal muscle becomes refractory to the trophic actions of muscle growth factors during unloading are not well defined.In a previous study designed to evaluate changes in skeletal muscle gene expression in rats exposed to a 16-day spaceflight (30), we identified novel potential atrogenes (37) using microarray analysis. The response of skeletal muscle to mechanical stress is accompanied by marked alterations in atrogene expression, and we showed that microgravity induces Siah-1A, MuRF-1 (30), and atrogin-1 (see Table S1 in the supplemental material). Microgravity also resulted in the increased expression of Cbl-b (greater than eightfold). Cbl-b is another RING-type ubiquitin ligase previously established as a negative regulator of receptor tyrosine kinase signaling in a variety of cells (23,45). These results complement our recent finding that Cbl-b downregulates bone formation

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Cbl-b-deficient Mice Mice Deficient In the Cbl-b Gene (Cbl-mentioning

confidence: 99%

Ubiquitin Ligase Cbl-b Is a Negative Regulator for Insulin-Like Growth Factor 1 Signaling during Muscle Atrophy Caused by Unloading

Nakao¹,

Hirasaka²,

Goto³

et al. 2009

Molecular and Cellular Biology

Self Cite

165

164

View full text Add to dashboard Cite

show abstract

“…In response to decreased mechanical stress, skeletal muscle tissue undergoes rapid atrophy characterized by the loss of mass and size. 204,205 On the other hand, mechanical stimulation of the tissue leads to increased mitochondrial content, 206 improved insulin sensitivity, 207 enhanced muscle strength, and increased size. 208 During catabolic conditions, muscle proteins are catabolized to maintain gluconeogenesis in the liver, 209 but excessive degradation of the muscle tissue may be extremely damaging for the organism, leading to muscle wasting and even death.…”

Section: Exercise As a Modelmentioning

confidence: 99%

Heat shock response and autophagy—cooperation and control

2015

View full text Add to dashboard Cite

Abbreviations: AKT, v-akt murine thymoma viral oncogene homolog 1; AMPK, adenosine monophosphate-activated protein kinase; ATG, autophagy-related; BECN1, Beclin 1, autophagy related; EIF4EBP1, eukaryotic translation initiation factor 4E binding protein 1; ER, endoplasmic reticulum; FOXO, forkhead box O; HSF1, heat shock transcription factor 1; HSP, heat shock protein; HSPA8/ HSC70, heat shock 70kDa protein 8; IL, interleukin; LC3, MAP1LC3, microtubule-associated protein 1 light chain 3; MTMR14/ hJumpy, myotubularin related protein 14; MTOR, mechanistic target of rapamycin; NR1D1/Rev-Erb-a, nuclear receptor subfamily 1, group D, member 1; PBMC, peripheral blood mononuclear cell; PPARGC1A/PGC-1a, peroxisome proliferator-activated receptor, gamma, coactivator 1 a; RHEB, Ras homolog enriched in brain; SOD, superoxide dismutase; SQSTM1/p62, sequestosome 1; TPR, translocated promoter region, nuclear basket protein; TSC, tuberous sclerosis complex; ULK1, unc-51 like autophagy activating kinase 1.Protein quality control (proteostasis) depends on constant protein degradation and resynthesis, and is essential for proper homeostasis in systems from single cells to whole organisms. Cells possess several mechanisms and processes to maintain proteostasis. At one end of the spectrum, the heat shock proteins modulate protein folding and repair. At the other end, the proteasome and autophagy as well as other lysosome-dependent systems, function in the degradation of dysfunctional proteins. In this review, we examine how these systems interact to maintain proteostasis. Both the direct cellular data on heat shock control over autophagy and the time course of exercise-associated changes in humans support the model that heat shock response and autophagy are tightly linked. Studying the links between exercise stress and molecular control of proteostasis provides evidence that the heat shock response and autophagy coordinate and undergo sequential activation and downregulation, and that this is essential for proper proteostasis in eukaryotic systems.

show abstract

“…The muscle RING finger 1 (MurF1) and muscle atrophy F-box (MAFbx) are the main ubiquitin ligases responsible for protein degradation in skeletal muscle. It is well established that immobilization causes an accumulation of polyubiquitinated proteins in rodent and human skeletal muscle [96][97][98] due to increase in both MuRF-1 and MAFbx expression [53,57,62,99]. The nuclear factor-κB (NF-κB) directly regulates the transcription of MuRF1, and consequently plays an important role in immobilization-induced protein degradation [100,101].…”

Section: Cellular Mechanisms Involved In Immobilization-induced Skelementioning

confidence: 99%

From physical inactivity to immobilization: Dissecting the role of oxidative stress in skeletal muscle insulin resistance and atrophy

Pierre

Appriou

Gratas-Delamarche

et al. 2016

Free Radical Biology and Medicine

View full text Add to dashboard Cite

In the literature, the terms physical inactivity and immobilization are largely used as synonyms. The present review emphasizes the need to establish a clear distinction between these two situations. Physical inactivity is a behavior characterized by a lack of physical activity, whereas immobilization is a deprivation of movement for medical purpose. In agreement with these definitions, appropriate models exist to study either physical inactivity or immobilization, leading thereby to distinct conclusions. In this review, we examine the involvement of oxidative stress in skeletal muscle insulin resistance and atrophy induced by, respectively, physical inactivity and immobilization. A large body of evidence demonstrates that immobilization-induced atrophy depends on the chronic overproduction of reactive oxygen and nitrogen species (RONS). On the other hand, the involvement of RONS in physical inactivity-induced insulin resistance has not been investigated. This observation outlines the need to elucidate the mechanism by which physical inactivity promotes insulin resistance.

show abstract

Ubiquitin ligase gene expression in healthy volunteers with 20‐day bedrest

Cited by 79 publications

References 21 publications

Ubiquitin Ligase Cbl-b Is a Negative Regulator for Insulin-Like Growth Factor 1 Signaling during Muscle Atrophy Caused by Unloading

Ubiquitin Ligase Cbl-b Is a Negative Regulator for Insulin-Like Growth Factor 1 Signaling during Muscle Atrophy Caused by Unloading

Heat shock response and autophagy—cooperation and control

From physical inactivity to immobilization: Dissecting the role of oxidative stress in skeletal muscle insulin resistance and atrophy

Contact Info

Product

Resources

About