Desmin and α-actinin-2 content in rat soleus muscle in the dynamics of gravitational unloading and subsequent reloading

Mirzoev, Timur M.; Шенкман, Борис; Ушаков, И. Б.

doi:10.1134/s1607672912030052

Cited by 11 publications

(9 citation statements)

References 15 publications

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“…On the basis of ultrastructural data, Riley and colleagues have hypothesized a similarity of the principal mechanisms of muscle structural changes during early recovery from mechanical unloading or space flight and following eccentric exercise. Recently, we have confirmed this hypothesis by observing a significant decrease in cytoskeletal protein (desmin and alpha‐actinin‐2) content in rat soleus muscle early in recovery from simulated microgravity . During the early reloading period and following eccentric exercise, increased activity of calpains and impaired permeability of the sarcolemma to macromolecules was detected .…”

mentioning

confidence: 61%

“…Recently, we have confirmed this hypothesis by observing a significant decrease in cytoskeletal protein (desmin and alpha-actinin-2) content in rat soleus muscle early in recovery from simulated microgravity. 7 During the early reloading period and following eccentric exercise, increased activity of calpains 8 and impaired permeability of the sarcolemma to macromolecules was detected. 9,10 If the processes during reloading and recovery (at least in the early stage) are similar to those that occur after eccentric exercise, it can be hypothesized that the parameters of the key signaling cascade regulating protein synthesis (PS), mammalian (or mechanistic) target of rapamycin complex 1 (mTORC1), and 70 kDa ribosomal protein S6 kinase (p70S6K), should be activated, leading to an increase in muscle mass.…”

mentioning

confidence: 99%

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Akt-dependent and Akt-independent pathways are involved in protein synthesis activation during reloading of disused soleus muscle

2016

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confidence: 61%

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confidence: 99%

Akt-dependent and Akt-independent pathways are involved in protein synthesis activation during reloading of disused soleus muscle

2016

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“…In addition, an important role can be provided by the cytoskeleton in the transmission of a mechanical signal from the surface of the muscle fiber to anabolic regulatory proteins [19]. For example, HU-induced decrease in desmin content in rat soleus muscle [20,21], could interfere with a propagation of a mechanical signal to muscle PS. There is evidence that mechano-dependent activation of mTORC1 is directly mediated by phosphatidic acid, which is synthesized with the help of ζ-isoform of diacylglycerol kinase (DGK-ζ) [22].…”

Section: Discussionmentioning

confidence: 99%

An Anabolic Signaling Response of Rat Soleus Muscle to Eccentric Contractions Following Hindlimb Unloading: A Potential Role of Stretch-Activated Ion Channels

Tyganov¹,

Mirzoev²,

Шенкман³

2019

IJMS

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Mechanisms that convert a mechanical signal into a biochemical response in an atrophied skeletal muscle remain poorly understood. The aims of the study were to evaluate a temporal response of anabolic signaling and protein synthesis (PS) to eccentric contractions (EC) in rat soleus during hindlimb unloading (HU); and to assess a possible role of stretch-activated ion channels (SAC) in the propagation of a mechanical signal to mTORC1 following HU. Following HU, an isolated soleus was subjected to EC. Upon completion of EC, muscles were collected for western blot analyses to determine the content/phosphorylation of the key anabolic markers. We found that a degree of EC-induced p70S6K phosphorylation and the rate of PS in the soleus of 3- and 7-day unloaded rats was significantly less than that in control. A decrease in EC-induced phosphorylation of p70S6K, RPS6 and PS in the 7-day unloaded soleus treated with SAC inhibitor did not differ from that of the 7-day unloaded soleus without SAC blockade. The results of the study suggest that (i) HU results in a blunted anabolic response to a bout of EC, (ii) attenuation of mTORC1-signaling and PS in response to EC in unloaded soleus may be associated with inactivation of SAC.

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“…It is possible that deposition of calsarcin in the structure of α-actinin-2 plays an important role in these processes. In our laboratory, a decreased content of α-actinin-2 in samples of murine soleus muscle was observed after a 7-day suspension of rats [ 72 ]. Therefore, it can be expected that bound calsarcin-2 is released due to alpha-actinin-2 degradation during simulated gravitational unloading.…”

Section: Expression Of Myosin Genes Under Conditions Of Gravitational Unloadingmentioning

confidence: 99%

From Slow to Fast: Hypogravity-Induced Remodeling of Muscle Fiber Myosin Phenotype

2016

Acta Naturae

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Skeletal muscle consists of different fiber types arranged in a mosaic pattern. These fiber types are characterized by specific functional properties. Slow-type fibers demonstrate a high level of fatigue resistance and prolonged contraction duration, but decreased maximum contraction force and velocity. Fast-type fibers demonstrate high contraction force and velocity, but profound fatigability. During the last decades, it has been discovered that all these properties are determined by the predominance of slow or fast myosin-heavy-chain (MyHC) isoforms. It was observed that gravitational unloading during space missions and simulated microgravity in ground-based experiments leads to the transformation of some slow-twitch muscle fibers into fast-twitch ones due to changes in the patterns of MyHC gene expression in the postural soleus muscle. The present review covers the facts and mechanistic speculations regarding myosin phenotype remodeling under conditions of gravitational unloading. The review considers the neuronal mechanisms of muscle fiber control and molecular mechanisms of regulation of myosin gene expression, such as inhibition of the calcineurin/NFATc1 signaling pathway, epigenomic changes, and the behavior of specific microRNAs. In the final portion of the review, we discuss the adaptive role of myosin phenotype transformations.

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Desmin and α-actinin-2 content in rat soleus muscle in the dynamics of gravitational unloading and subsequent reloading

Cited by 11 publications

References 15 publications

Akt-dependent and Akt-independent pathways are involved in protein synthesis activation during reloading of disused soleus muscle

Akt-dependent and Akt-independent pathways are involved in protein synthesis activation during reloading of disused soleus muscle

An Anabolic Signaling Response of Rat Soleus Muscle to Eccentric Contractions Following Hindlimb Unloading: A Potential Role of Stretch-Activated Ion Channels

From Slow to Fast: Hypogravity-Induced Remodeling of Muscle Fiber Myosin Phenotype

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