scholarly journals Meeting Synopsis: Advances in Skeletal Muscle Biology in Health and Disease (Gainesville, Florida, February 22nd to 24th 2012) – Day 1: “Cell Signaling Mechanisms Mediating Muscle Atrophy and Hypertrophy” and “muscle Force, Calcium Handling, and Stress Response”

2012 ◽  
Vol 3 ◽  
Author(s):  
Andrew R. Judge ◽  
Scott K. Powers ◽  
Leonardo F. Ferreira ◽  
Marcas M. Bamman
Keyword(s):  
Skeletal Muscle ◽  
Stress Response ◽  
Cell Signaling ◽  
Muscle Atrophy ◽  
Muscle Force ◽  
Calcium Handling ◽  
Signaling Mechanisms ◽  
Muscle Biology ◽  
Health And Disease ◽  
Atrophy And Hypertrophy

Myostatin and the skeletal muscle atrophy and hypertrophy signaling pathways

2014 ◽  
Vol 71 (22) ◽  
pp. 4361-4371 ◽  
Author(s):  
J. Rodriguez ◽  
B. Vernus ◽  
I. Chelh ◽  
I. Cassar-Malek ◽  
J. C. Gabillard ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Signaling Pathways ◽  
Muscle Atrophy ◽  
Skeletal Muscle Atrophy ◽  
Atrophy And Hypertrophy

scholarly journals Denervation does not induce muscle atrophy through oxidative stress

2017 ◽  
Vol 27 (1) ◽  
Author(s):  
Eva Pigna ◽  
Emanuela Greco ◽  
Giulio Morozzi ◽  
Silvia Grottelli ◽  
Alessio Rotini ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Skeletal Muscle ◽  
Stress Response ◽  
Muscle Atrophy ◽  
Oxidative Stress Response ◽  
Skeletal Muscle Atrophy ◽  
Molecular Pathways ◽  
Ubiquitin Proteasome ◽  
Anti Oxidant ◽  
Kinetics Of

Denervation leads to the activation of the catabolic pathways, such as the ubiquitin-proteasome and autophagy, resulting in skeletal muscle atrophy and weakness. Furthermore, denervation induces oxidative stress in skeletal muscle, which is thought to contribute to the induction of skeletal muscle atrophy. Several muscle diseases are characterized by denervation, but the molecular pathways contributing to muscle atrophy have been only partially described. Our study delineates the kinetics of activation of oxidative stress response in skeletal muscle following denervation. Despite the denervation-dependent induction of oxidative stress in skeletal muscle, treatments with anti-oxidant drugs do not prevent the reduction of muscle mass. Our results indicate that, although oxidative stress may contribute to the activation of the response to denervation, it is not responsible by itself of oxidative damage or neurogenic muscle atrophy.

scholarly journals A transient antioxidant stress response accompanies the onset of disuse atrophy in human skeletal muscle

2009 ◽  
Vol 107 (2) ◽  
pp. 549-557 ◽  
Author(s):  
Luciano Dalla Libera ◽  
Barbara Ravara ◽  
Valerio Gobbo ◽  
Elena Tarricone ◽  
Maurizio Vitadello ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Skeletal Muscle ◽  
Stress Response ◽  
Muscle Atrophy ◽  
Cross Sectional Area ◽  
Heme Oxygenase 1 ◽  
Sectional Area ◽  
Cross Sectional ◽  
Protein Levels ◽  
Antioxidant Stress

It is presently unknown whether oxidative stress increases in disused skeletal muscle in humans. Markers of oxidative stress were investigated in biopsies from the vastus lateralis muscle, collected from healthy subjects before [ time 0 (T0)], after 1 wk (T8), and after 5 wk (T35) of bed rest. An 18% decrease in fiber cross-sectional area was detected in T35 biopsies ( P < 0.05). Carbonylation of muscle proteins significantly increased about twofold at T35 ( P < 0.02) and correlated positively with the decrease in fiber cross-sectional area ( P = 0.04). Conversely, T8 biopsies showed a significant increase in protein levels of heme oxygenase-1 and glucose-regulated protein-75 (Grp75)/mitochondrial heat shock protein-70, two stress proteins involved in the antioxidant defense ( P < 0.05). Heme oxygenase-1 increase, which involved a larger proportion of slow fibers compared with T0, appeared blunted in T35 biopsies. Grp75 protein level increased threefold in T8 biopsies and localized especially in slow fibers ( P < 0.025), to decrease significantly in T35 biopsies ( P < 0.05). Percent change in Grp75 levels positively correlated with fiber cross-sectional area ( P = 0.01). Parallel investigations on rat soleus muscles, performed after 1–15 days of hindlimb suspension, showed that Grp75 protein levels significantly increased after 24 h of unloading ( P = 0.02), i.e., before statistically significant evidence of muscle atrophy, to decrease thereafter in relation to the degree of muscle atrophy ( P = 0.03). Therefore, in humans as in rodents, disuse muscle atrophy is characterized by increased protein carbonylation and by the blunting of the antioxidant stress response evoked by disuse.

scholarly journals Nox2 Inhibition Regulates Stress Response and Mitigates Skeletal Muscle Fiber Atrophy during Simulated Microgravity

2021 ◽  
Vol 22 (6) ◽  
pp. 3252
Author(s):  
John M. Lawler ◽  
Jeffrey M. Hord ◽  
Pat Ryan ◽  
Dylan Holly ◽  
Mariana Janini Gomes ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Stress Response ◽  
Muscle Atrophy ◽  
Muscle Fiber ◽  
Skeletal Muscle Atrophy ◽  
Positive Staining ◽  
Angiotensin Ii Receptor ◽  
Mechanical Unloading ◽  
Muscle Fiber Atrophy ◽  
Fiber Atrophy

Insufficient stress response and elevated oxidative stress can contribute to skeletal muscle atrophy during mechanical unloading (e.g., spaceflight and bedrest). Perturbations in heat shock proteins (e.g., HSP70), antioxidant enzymes, and sarcolemmal neuronal nitric oxidase synthase (nNOS) have been linked to unloading-induced atrophy. We recently discovered that the sarcolemmal NADPH oxidase-2 complex (Nox2) is elevated during unloading, downstream of angiotensin II receptor 1, and concomitant with atrophy. Here, we hypothesized that peptidyl inhibition of Nox2 would attenuate disruption of HSP70, MnSOD, and sarcolemmal nNOS during unloading, and thus muscle fiber atrophy. F344 rats were divided into control (CON), hindlimb unloaded (HU), and hindlimb unloaded +7.5 mg/kg/day gp91ds-tat (HUG) groups. Unloading-induced elevation of the Nox2 subunit p67phox-positive staining was mitigated by gp91ds-tat. HSP70 protein abundance was significantly lower in HU muscles, but not HUG. MnSOD decreased with unloading; however, MnSOD was not rescued by gp91ds-tat. In contrast, Nox2 inhibition protected against unloading suppression of the antioxidant transcription factor Nrf2. nNOS bioactivity was reduced by HU, an effect abrogated by Nox2 inhibition. Unloading-induced soleus fiber atrophy was significantly attenuated by gp91ds-tat. These data establish a causal role for Nox2 in unloading-induced muscle atrophy, linked to preservation of HSP70, Nrf2, and sarcolemmal nNOS.

Sign in / Sign up

Export Citation Format

Share Document