Effect of Contraction on Mitogen-activated Protein Kinase Signal Transduction in Skeletal Muscle

Ryder, Jeffrey W.; Fahlman, Roger; Wallberg-Henriksson, Harriet; Alessi, Dario R.; Krook, Anna; Zierath, Juleen R.

doi:10.1074/jbc.275.2.1457

Cited by 142 publications

(153 citation statements)

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“…Muscle contraction was induced via electrical stimulation. Muscles were stimulated at 100 Hz (0.2-ms pulse duration, 20 V), at a rate of one 0.2-s contraction every 2 s for 10 min, as previously described (27). Muscles were frozen immediately for AMPK or PI 3-kinase activity measurements or further incubated for the assessment of glucose transport activity.…”

Section: Animalsmentioning

confidence: 99%

Isoform-Specific Regulation of 5′ AMP-Activated Protein Kinase in Skeletal Muscle From Obese Zucker (fa/fa) Rats in Response to Contraction

et al. 2002

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Glucose transport can be activated in skeletal muscle in response to insulin via activation of phosphoinositide (PI) 3-kinase and in response to contractions or hypoxia, presumably via activation of 5 AMP-activated protein kinase (AMPK). We determined the effects of insulin and muscle contraction/hypoxia on PI 3-kinase, AMPK, and glucose transport activity in epitrochlearis skeletal muscle from insulin-resistant Zucker (fa/fa) rats. Insulin-stimulated glucose transport in isolated skeletal muscle was reduced 47% in obese versus lean rats, with a parallel 42% reduction in tyrosine-associated PI 3-kinase activity. Contraction and hypoxia elicited normal responses for glucose transport in skeletal muscle from insulin-resistant obese rats. Isoformspecific AMPK activity was measured in skeletal muscle in response to insulin, contraction, or hypoxia. Contraction increased AMPK␣1 activity 2.3-fold in lean rats, whereas no effect was noted in obese rats. Hypoxia increased AMPK␣1 activity to a similar extent (more than sixfold) in lean and obese rats. Regardless of genotype, contraction, and hypoxia, each increased AMPK␣2 activity more than fivefold, whereas insulin did not alter either AMPK␣1 or -␣2 activity in skeletal muscle. In conclusion, obesity-related insulin resistance is associated with an isoform-specific impairment in AMPK␣1 in response to contraction. However, this impairment does not appear to affect contraction-stimulated glucose transport. Activation of AMPK␣2 in response to muscle contraction/exercise is associated with a parallel and normal increase in glucose transport in insulin-resistant skeletal muscle. Diabetes 51: 2703-2708, 2002

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Section: Animalsmentioning

confidence: 99%

Isoform-Specific Regulation of 5′ AMP-Activated Protein Kinase in Skeletal Muscle From Obese Zucker (fa/fa) Rats in Response to Contraction

et al. 2002

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“…Emerging evidence suggests that muscle contraction through exercise increases ERK1/2, JNK, and p38 MAPK signaling directly in skeletal muscle (13)(14)(15)(16)(17)(18)(19)(20). ERK1/2, JNK, and p38 MAPK phosphorylation is increased in human skeletal muscle after exercise (17,19,20) and in rat skeletal muscle in response to contraction (18,21,22), exercise (13), muscle overload (23), and mechanical stretch (21).…”

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confidence: 99%

Effects of Insulin, Contraction, and Phorbol Esters on Mitogen-Activated Protein Kinase Signaling in Skeletal Muscle From Lean and ob/ob Mice

2004

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Effects of diverse stimuli, including insulin, muscle contraction, and phorbol 12-myristate-13-acetate (PMA), were determined on phosphorylation of mitogen-activated protein kinase (MAPK) signaling modules (c-Jun NH 2 -terminal kinase [JNK], p38 MAPK, and extracellular signal-related kinase [ERK1/2]) in skeletal muscle from lean and ob/ob mice. Insulin increased phosphorylation of JNK, p38 MAPK, and ERK1/2 in isolated extensor digitorum longus (EDL) and soleus muscle from lean mice in a time-and dose-dependent manner. Muscle contraction and PMA also elicited robust effects on these parallel MAPK modules. Insulin action on JNK, p38 MAPK, and ERK1/2 phosphorylation was significantly impaired in EDL and soleus muscle from ob/ob mice. In contrast, muscle contraction-mediated JNK, p38 MAPK, and ERK1/2 phosphorylation was preserved. PMA effects on phosphorylation of JNK and ERK1/2 were normal in ob/ob mice, whereas effects on p38 MAPK were abolished. In conclusion, insulin, contraction, and PMA activate MAPK signaling in skeletal muscle. Insulin-mediated responses on MAPK signaling are impaired in skeletal muscle from ob/ob mice, whereas the effect of contraction is generally well preserved. In addition, PMA-induced phosphorylation of JNK and ERK1/2 are preserved, whereas p38 MAPK pathways are impaired in skeletal muscle from ob/ob mice. Thus, appropriate MAPK responses can be elicited in insulinresistant skeletal muscle via an insulin-independent mechanism.

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“…Although, recently it has been established that mechanical stress activates the ERK1/2, JNKs, and p38 MAP kinases in skeletal muscle cells (22)(23)(24)(25)(26)(27)(28)(29)(30), the pathways that are involved in the activation of these kinases in response to mechanical stress remain unknown. Furthermore, most of the studies on the activation of MAP kinases were carried out in vitro using hind limb muscle cells, which are loaded in vivo along the direction of the long axis of the muscle fibers.…”

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Distinct Signaling Pathways Are Activated in Response to Mechanical Stress Applied Axially and Transversely to Skeletal Muscle Fibers

Kumar

Chaudhry

Reid

et al. 2002

Journal of Biological Chemistry

112

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In the diaphragm muscle we tested the hypothesis that MAP kinase signaling pathways are activated by mechanical stress and such signaling pathways are dependent on the direction in which mechanical stress is applied. Although equal magnitudes of mechanical stress were applied axially and transversely a greater level of activation of ERK1/2, p38, Raf-1, p90 RSK, Elk-1, and the DNA binding activity of AP-1 transcription factor was produced when the muscle was stretched transversely than when stretched axially. A significant up-regulation in protein tyrosine phosphorylation was observed in axially or transversely loaded diaphragm muscles and the activation of ERK1/2 was completely inhibited by genistein (protein-tyrosine kinase inhibitor). Pretreatment of muscles with wortmannin (phosphoinositide 3-kinase inhibitor), TMB-8 (antagonist of intracellular calcium release), GF109203X (PKC inhibitor), or PD98059 (MEK1/2 inhibitor) blocked the activation of ERK1/2 kinases in response to axial but not to transverse loading. On the other hand, pretreatment of muscles with protein kinase A inhibitors H-7 and KT5720 completely suppressed the activation of ERK1/2 in response to transverse loading only. Taken together with the alterations of MAP kinases and the findings of elevations of downstream transcription targets, our data are consistent with two distinct MAP kinase signal transduction pathways in response to mechanical stress.

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Effect of Contraction on Mitogen-activated Protein Kinase Signal Transduction in Skeletal Muscle

Abstract: MAPK . These data demonstrate that muscle contraction, separate from systemic influence, activates MAPK signaling. Furthermore, we are the first to show that contractile activity stimulates MAPKAP-K2 and MSK1.

Cited by 142 publications

References 32 publications

Isoform-Specific Regulation of 5′ AMP-Activated Protein Kinase in Skeletal Muscle From Obese Zucker (fa/fa) Rats in Response to Contraction

Isoform-Specific Regulation of 5′ AMP-Activated Protein Kinase in Skeletal Muscle From Obese Zucker (fa/fa) Rats in Response to Contraction

Effects of Insulin, Contraction, and Phorbol Esters on Mitogen-Activated Protein Kinase Signaling in Skeletal Muscle From Lean and ob/ob Mice

Distinct Signaling Pathways Are Activated in Response to Mechanical Stress Applied Axially and Transversely to Skeletal Muscle Fibers

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