Reduced metabolic capacity in fast and slow skeletal muscle via oxidative stress and the energy‐sensing of AMPK/SIRT1 in malnutrition

Melatonin is a well-known molecule for its involvement in circadian rhythm regulation and its contribution to protection against oxidative stress in organisms including unicellular alga, animals and plants. Currently, the bio-regulatory effects of melatonin on the physiology of various peripheral tissues have drawn a great attention of scientists. Although melatonin was previously defined as a neurohormone secreted from pineal gland, recently it has been identified that virtually, every cell has the capacity to synthesize melatonin and the locally generated melatonin has multiple pathophysiological functions, including regulations of obesity and metabolic syndromes. Herein, we focus on the effects of melatonin on fat deposition in various peripheral organs/tissues. The two important regulatory mechanisms related to the topic, i.e., the improvements of circadian rhythms and antioxidative capacity will be thoroughly discussed since they are linked to several biomarkers involved in obesity and energy imbalance, including metabolism and immunity. Furthermore, several other functions of melatonin which may serve to prevent or promote obesity and energy dysmetabolism-induced pathological states are also addressed. The organs of special interest include liver, pancreas, skeletal muscle, adipose tissue and the gut microbiota.

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Faculty Opinions recommendation of Little change in markers of protein breakdown and oxidative stress in humans in immobilization-induced skeletal muscle atrophy.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.7808956.8146054 ◽

2011 ◽

Author(s):

Roberto Bottinelli

Keyword(s):

Oxidative Stress ◽

Skeletal Muscle ◽

Muscle Atrophy ◽

Skeletal Muscle Atrophy ◽

Protein Breakdown ◽

And Oxidative Stress

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Faculty Opinions recommendation of Oxidative stress in skeletal muscle stimulates early expression of Rad in a mouse model of amyotrophic lateral sclerosis.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.7576956.7874055 ◽

2011 ◽

Author(s):

Brett Adams ◽

Roger Bannister

Keyword(s):

Oxidative Stress ◽

Skeletal Muscle ◽

Amyotrophic Lateral Sclerosis ◽

Mouse Model ◽

Early Expression ◽

Lateral Sclerosis

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Effect of External Calcium and other Divalent Cations on K+ Contractures in Denervated Slow Skeletal Muscle Fibers of the Frog

Journal of Biomedical and Allied Research ◽

10.37191/mapsci-2582-4937-1(2)-009 ◽

2019 ◽

Author(s):

Leonardo Hernández

Keyword(s):

Skeletal Muscle ◽

Binding Capacity ◽

Divalent Cations ◽

Muscle Fibers ◽

Free Calcium ◽

Slow Skeletal Muscle ◽

Skeletal Muscle Fibers ◽

Free Calcium Concentration ◽

Chronic Denervation ◽

Denervated Muscles

The influence of Ca2+ and other divalent cations on contractile responses of slow skeletal muscle fibers of the frog (Rana pipiens) under conditions of chronic denervation was investigated.Isometric tension was recorded from slow bundles of normal and denervated cruralis muscle in normal solution and in solutions with free calcium concentration solution or in solutions where other divalent cations (Sr2+, Ni2+, Co2+ or Mn2+) substituted for calcium. In the second week after nerve section, in Ca2+-free solutions, we observed that contractures (evoked from 40 to 80 mM-K+) of non-denervated muscles showed significantly higher tensions (p<0.05), than those from denervated bundles. Likewise, in solutions where calcium was substituted by all divalent cations tested, with exception of Mn2+, the denervated bundles displayed lower tension than non-denervated, also in the second week of denervation. In this case, the Ca2+ substitution by Sr2+ caused the higher decrease in tension, followed by Co2+ and Ni2+, which were different to non-denervated bundles, as the lowest tension was developed by Mn2+, followed by Co2+, and then Ni2+ and Sr2+. After the third week, we observed a recovery in tension. These results suggest that denervation altering the binding capacity to divalent cations of the voltage sensor.

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Role of Oxidative Stress and Mitochondrial Dysfunction in Skeletal Muscle in Type 2 Diabetic Patients

Current Pharmaceutical Design ◽

10.2174/1381612822666160217142949 ◽

2016 ◽

Vol 22 (18) ◽

pp. 2650-2656 ◽

Cited By ~ 5

Author(s):

Noelia Diaz-Morales ◽

Susana Rovira-Llopis ◽

Irene Escribano-Lopez ◽

Celia Bañuls ◽

Sandra Lopez-Domenech ◽

...

Keyword(s):

Oxidative Stress ◽

Skeletal Muscle ◽

Mitochondrial Dysfunction ◽

Diabetic Patients ◽

Type 2 Diabetic Patients ◽

Type 2 Diabetic

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Oxidative Stress and Skeletal Muscle Dysfunction with Aging

Current Aging Science ◽

10.2174/1874609811104020101 ◽

2011 ◽

Vol 4 (2) ◽

pp. 101-109 ◽

Cited By ~ 26

Author(s):

Wataru Aoi ◽

Kunihiro Sakuma

Keyword(s):

Oxidative Stress ◽

Skeletal Muscle ◽

Muscle Dysfunction ◽

Skeletal Muscle Dysfunction

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Slow skeletal muscle myosin-binding protein-C (MyBPC1) mediates recruitment of muscle-type creatine kinase (CK) to myosin

Biochemical Journal ◽

10.1042/bj20102007 ◽

2011 ◽

Vol 436 (2) ◽

pp. 437-445 ◽

Cited By ~ 31

Author(s):

Zhe Chen ◽

Tong-Jin Zhao ◽

Jie Li ◽

Yan-Song Gao ◽

Fan-Guo Meng ◽

...

Keyword(s):

Skeletal Muscle ◽

Creatine Kinase ◽

Muscle Contraction ◽

Binding Protein ◽

High Energy ◽

Functional Coupling ◽

Muscle Type ◽

Myosin Binding Protein ◽

Slow Skeletal Muscle ◽

Myosin Binding

Muscle contraction requires high energy fluxes, which are supplied by MM-CK (muscle-type creatine kinase) which couples to the myofibril. However, little is known about the detailed molecular mechanisms of how MM-CK participates in and is regulated during muscle contraction. In the present study, MM-CK is found to physically interact with the slow skeletal muscle-type MyBPC1 (myosin-binding protein C1). The interaction between MyBPC1 and MM-CK depended on the creatine concentration in a dose-dependent manner, but not on ATP, ADP or phosphocreatine. The MyBPC1–CK interaction favoured acidic conditions, and the two molecules dissociated at above pH 7.5. Domain-mapping experiments indicated that MM-CK binds to the C-terminal domains of MyBPC1, which is also the binding site of myosin. The functional coupling of myosin, MyBPC1 and MM-CK is further corroborated using an ATPase activity assay in which ATP expenditure accelerates upon the association of the three proteins, and the apparent Km value of myosin is therefore reduced. The results of the present study suggest that MyBPC1 acts as an adaptor to connect the ATP consumer (myosin) and the regenerator (MM-CK) for efficient energy metabolism and homoeostasis.

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