Differential Regulation of MAPK Isoforms during Cast-Immobilization -Induced Atrophy in Rat Gastrocnemius Muscle

Kim, Junghwan

doi:10.1589/jpts.22.217

Cited by 10 publications

(35 citation statements)

References 30 publications

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“…Mitogen-activated protein kinases, such as extracellular signal-regulated kinase 1/2, stress-activated protein kinase/ c-Jun NH 2 -terminal kinase, and p38 mitogen-activated protein kinase, are simultaneously involved in muscle atrophy induced by immobilization and cell starvation12, 13 ) . Furthermore, in another study, we demonstrated that cast immobilization increases the expression of myoglobin in rat gastrocnemius muscles15 ) .…”

Section: Discussionmentioning

confidence: 99%

Decrease of Both Cofilin and LIM Kinase Phosphorylation in the Skeletal Muscles of Immobilization-induced Atrophy Rats

Kim

Lee

et al. 2014

J Phys Ther Sci

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[Purpose] Immobilization-induced atrophy is a general phenomenon caused by prolonged muscle disuse associated with orthopaedic conditions. However, changes in the phosphorylation of atrophy-related cofilin and LIM kinases are still poorly understood. In this study, we examined whether or not phosphorylation of cofilin and LIM kinases is altered in the skeletal muscles of rats after 3, 7, 14, and 21 days of cast immobilization. [Methods] We used two-dimensional gel electrophoresis, mass spectrometry, and western blotting to examine protein expression and phosphorylation in atrophied rat gastrocnemius muscles. [Results] The expression of the cofilin was detected in gastrocnemius muscle strips using proteomic analysis. Cast immobilization after 3, 7, 14, and 21 days significantly diminished the phosphorylation of cofilin and LIM kinases. [Conclusion] The present results suggest that cast immobilization-induced atrophy may be in part related to changes in the phosphorylation of cofilin and LIM kinases in rat skeletal muscles.

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Section: Discussionmentioning

confidence: 99%

Decrease of Both Cofilin and LIM Kinase Phosphorylation in the Skeletal Muscles of Immobilization-induced Atrophy Rats

Kim

Lee

et al. 2014

J Phys Ther Sci

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“…Maintenance of muscle mass and of muscle function are important for healthy life, and is important in the rehabilitation of musculoskeletal disease in the field of physical therapy 1 , 7 , 13 , 14 ) . The maintenance mechanisms of muscle mass include anabolic and catabolic signal transductions via PKB/Akt, a protein with a critical role 1 , 5 , 10 , 11 ) .…”

Section: Discussionmentioning

confidence: 99%

“…The homogenate was centrifuged and the supernatant was collected. Proteins, 30–45 μg/lane, were separated on 12% polyacrylamide sodium dodecylsulfate gels and then transferred electrophoretically to a polyvinylidene fluoride membrane (Millipore; Bedford, MA, USA) 1 ) . Anti-PKB/Akt antibody was purchased from Santa Cruz (Santa Cruz, CA, USA).…”

Section: Methodsmentioning

confidence: 99%

“…Akt, also called protein kinase B (PKB/Akt), is a pleckstrin homology domain-containing serine/threonine kinase which is activated by various stimuli, such as growth factors and agonists 1 , 2 , 3 , 4 ) . Akt has also been widely reported to have key roles in muscle hypertrophy and the prevention of atrophy 1 , 3 , 5 ) . Our previous study demonstrated that the phosphorylation of PKB/Akt in atrophied muscle tissues significantly diminishes in a time-dependent manner in cast-immobilized rats 1 ) .…”

Section: Introductionmentioning

confidence: 99%

“…Akt has also been widely reported to have key roles in muscle hypertrophy and the prevention of atrophy 1 , 3 , 5 ) . Our previous study demonstrated that the phosphorylation of PKB/Akt in atrophied muscle tissues significantly diminishes in a time-dependent manner in cast-immobilized rats 1 ) . Starvation in culture induces loss of muscle mass 6 , 7 , 8 ) .…”

Section: Introductionmentioning

confidence: 99%

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Decrease of PKB/Akt Phosphorylation is Partially Mediated by SAPK/JNK Activation in Serum-free L6 Myoblasts Starved with Low Glucose

et al. 2014

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[Purpose] Studies have been using cell cultures of muscle cells to mimic atrophy in in vivo and in vitro tests. However, changes in the activation of atrophy-related PKB/Akt is not fully understood in serum-free starved skeletal muscle cells. The purpose of the present study was to determine the change of PKB/Akt phosphorylation in L6 myoblasts under serum-free starvation conditions. [Methods] We used western blotting to examine PKB/Akt expression and phosphorylation in atrophied L6 myoblasts. [Results] The phosphorylation of PKB/Akt was significantly lower in L6 myoblasts under serum-free starvation than that of the control group. Serum-free starvation for 6, 12, 24, 36, 48, 72, 96, and 120 hours significantly decreased the phosphorylation of PKB/Akt. Furthermore, the decrease of PKB/Akt phosphorylation under serum-free starvation was partially restored by SP600125, an inhibitor of SAPK/JNK. [Conclusion] These results suggest that decrease of PKB/Akt phosphorylation due to serum-free starvation with low glucose is partially related to the activity of SAPK/JNK in L6 myoblasts.

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Identification of atrophy-related proteins produced in response to cast immobilization in rat gastrocnemius muscle

Kim

2010

Mol. Cell. Toxicol.

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Prolonged disuse of skeletal muscle causes atrophy, which is a universal phenomenon induced by various factors such as cast immobilization and space flight. However, the identity of proteins produced in atrophying skeletal muscle cells is poorly understood, especially during a period of cast immobilization. In the present study, we used 2-dimensional gel electrophoresis and matrix-assisted laser desorption ionization time-of-flight/time-of-flight mass spectrometry to investigate protein expression in rat gastrocnemius subjected to cast immobilization for 7 and 21 days. Gastrocnemius muscle mass was lost continuously throughout the 21 days of cast immobilization. Proteomic analysis of silver-stained gels of whole-protein extracts from rat gastrocnemius muscle strips detected 48 proteins. Of these proteins, the expression of 6 proteins changed during cast immobilization; these proteins are involved in metabolic, contraction, and chaperone activities. These results suggest that cast immobilization-induced skeletal muscle atrophy is related to changes in the defense and contractile apparatus proteins in rat gastrocnemius muscle.

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Differential Regulation of MAPK Isoforms during Cast-Immobilization -Induced Atrophy in Rat Gastrocnemius Muscle

Cited by 10 publications

References 30 publications

Decrease of Both Cofilin and LIM Kinase Phosphorylation in the Skeletal Muscles of Immobilization-induced Atrophy Rats

Decrease of Both Cofilin and LIM Kinase Phosphorylation in the Skeletal Muscles of Immobilization-induced Atrophy Rats

Decrease of PKB/Akt Phosphorylation is Partially Mediated by SAPK/JNK Activation in Serum-free L6 Myoblasts Starved with Low Glucose

Identification of atrophy-related proteins produced in response to cast immobilization in rat gastrocnemius muscle

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