Redox modification of ryanodine receptor contributes to impaired Ca2+ homeostasis and exacerbates muscle atrophy under high altitude

Agrawal, Akanksha; Rathor, Richa; Kumar, Ravi Shankar; Suryakumar, Geetha; Singh, Som Nath; Kumar, Bhuvnesh

doi:10.1016/j.freeradbiomed.2020.09.001

Cited by 18 publications

(21 citation statements)

References 43 publications

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“…Our previous studies reported that HH‐induced skeletal muscle protein loss is multifaced signaling pathways which include proteome imbalance, free radical medicated oxidative stress and inflammation, oxidative protein modification, enhanced degradative pathway, altered anabolic signaling and apoptosis 2,8,11 …”

Section: Discussionmentioning

confidence: 99%

“…Control group rats were maintained in the normoxic chamber within the same laboratory. The chamber was opened for 15–20 minutes each day to change the bedding, replenish the diet, BW measurement of the rats and UA administration 2,24,25 …”

Section: Methodsmentioning

confidence: 99%

“…The chamber was opened for 15-20 minutes each day to change the bedding, replenish the diet, BW measurement of the rats and UA administration. 2,24,25 2.5 | Blood and tissue collection After 3 days exposure, all the groups were weighed and anesthetized with sodium pentobarbital (50 mg/kg, i.p.) immediately.…”

Section: Hh Exposurementioning

confidence: 99%

“…Skeletal muscle weakness and atrophy are the prime disruptive effects of high altitude‐associated hypobaric hypoxia (HH) 1,2 . This weakness of skeletal muscle leads to decline in the physical performance of soldiers who are deployed at high altitude regions due to military operations.…”

Section: Introductionmentioning

confidence: 99%

“…Skeletal muscle weakness and atrophy are the prime disruptive effects of high altitude-associated hypobaric hypoxia (HH). 1,2 This weakness of skeletal muscle leads to [Corrections added on January 16, 2021, after first online publication. Abbreviations: BNP, brain natriuretic peptide; CPK, creatinine phospho kinase; HH, hypobaric hypoxia; IFN, interferon; IL, interleukin; LDH, lactate dehydrogenase; PBS, phosphate buffered saline; TNF-α, tumor necrosis factor-α; UA, ursolic acid.…”

Section: Introductionmentioning

confidence: 99%

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Ursolic acid ameliorates hypobaric hypoxia‐induced skeletal muscle protein loss via upregulating Akt pathway: An experimental study using rat model

et al. 2020

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Hypobaric hypoxic stress leads to oxidative stress, inflammation, and disturbance in protein turnover rate. Aggregately, this imbalance in redox homeostasis is responsible for skeletal muscle protein loss and a decline in physical performance. Hence, an urgent medical need is required to ameliorate skeletal muscle protein loss. The present study investigated the efficacy of ursolic acid (UA), a pentacyclic triterpene acid to ameliorate hypobaric hypoxia (HH)induced muscle protein loss. UA is a naturally occurring pentacyclic triterpene acid present in several edible herbs and fruits such as apples. It contains skeletal muscle hypertrophy activity; still its potential against HH-induced muscle protein loss is unexplored. To address this issue, an in vivo study was planned to examine the beneficial effect of UA supplementation on HH-induced skeletal muscle loss. Male Sprague Dawley rats were exposed to HH with and without UA supplementation (20 mg/kg; oral) for 3 continuous days. The results described the beneficial role of UA as supplementation of UA with HH exposure attenuated reactive oxygen species production and oxidative protein damage, which indicate the potent antioxidant activity. Furthermore, UA supplementation enhanced Akt, pAkt, and p70S6kinase activity (Akt pathway) and lowered the pro-inflammatory cytokines in HH exposed rats. UA has potent antioxidant and anti-inflammatory activity, and it enhanced the protein content via upregulation of Akt pathway-related proteins against HH exposure. These three biological activities of UA make it a novel candidate for amelioration of HH-induced skeletal muscle damage and protein loss.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Hh Exposurementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Ursolic acid ameliorates hypobaric hypoxia‐induced skeletal muscle protein loss via upregulating Akt pathway: An experimental study using rat model

et al. 2020

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Increased Expression of MiRNA‐1 Contributes to Hypobaric Hypoxia‐Induced Skeletal Muscle Loss

Srivastava,

Mondal,

Rathor

et al. 2023

Advanced Biology

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The present study aims to analyze the role of microRNA‐1 in the regulation of skeletal muscle loss under hypobaric hypoxia (HH). Male Sprague Dawley rats (n = 10) weighing 230–250 g are divided into two groups, control and HH exposure for 7 days at 25 000 ft. After the hypoxia exposure, the animals are sacrificed and hindlimb skeletal muscles are excised for further analysis. Studies found the potential role of miR‐1 (myomiR) as a biomarker under different atrophic conditions. Prolonged exposure to HH leads to enhanced expression of miR‐1 in skeletal muscle as compared to unexposed controls. The Bioinformatics approach is used to identify the validated targets and the biological processes of miR‐1. The target prediction tools identify PAX3 and HSP70 as major targets for miR‐1. Exposure to HH significantly reduces PAX3 and HSP70 expression during 7 days of HH exposure, which further enhances the activity of FOXO3, MSTN, and ATROGIN known for the progression of skeletal muscle atrophy in relation to control rats. This study indicates the increased expressions of miR‐1 and reduced expression of PAX3 and HSP70 lead to impaired myogenesis in skeletal muscle under HH. Further, enhanced expression of muscle degradation genes such as FOXO3, MSTN, and ATROGIN under HH exposure causes skeletal muscle protein loss.

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Myokines: A central point in managing redox homeostasis and quality of life

Rathor,

Suryakumar

2024

BioFactors

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Redox homeostasis is a crucial phenomenon that is obligatory for maintaining the healthy status of cells. However, the loss of redox homeostasis may lead to numerous diseases that ultimately result in a compromised quality of life. Skeletal muscle is an endocrine organ that secretes hundreds of myokines. Myokines are peptides and cytokines produced and released by muscle fibers. Skeletal muscle secreted myokines act as a robust modulator for regulating cellular metabolism and redox homeostasis which play a prime role in managing and improving metabolic function in multiple organs. Further, the secretory myokines maintain redox homeostasis not only in muscles but also in other organs of the body via stabilizing oxidants and antioxidant levels. Myokines are also engaged in maintaining mitochondrial dynamics as mitochondria is a central point for the generation of reactive oxygen species (ROS). Ergo, myokines also act as a central player in communicating signals to other organs, including the pancreas, gut, liver, bone, adipose tissue, brain, and skin via their autocrine, paracrine, or endocrine effects. The present review provides a comprehensive overview of skeletal muscle‐secreted myokines in managing redox homeostasis and quality of life. Additionally, probable strategies will be discussed that provide a solution for a better quality of life.

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Redox modification of ryanodine receptor contributes to impaired Ca2+ homeostasis and exacerbates muscle atrophy under high altitude

Cited by 18 publications

References 43 publications

Ursolic acid ameliorates hypobaric hypoxia‐induced skeletal muscle protein loss via upregulating Akt pathway: An experimental study using rat model

Ursolic acid ameliorates hypobaric hypoxia‐induced skeletal muscle protein loss via upregulating Akt pathway: An experimental study using rat model

Increased Expression of MiRNA‐1 Contributes to Hypobaric Hypoxia‐Induced Skeletal Muscle Loss

Myokines: A central point in managing redox homeostasis and quality of life

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