Effect of exercise on activation of the p38 mitogen-activated protein kinase pathway, c-Jun NH2 terminal kinase, and heat shock protein 27 in equine skeletal muscle

Ginneken, M. M. E. van; Graaf-Roelfsema, Ellen de; Keizer, H. A.; Dam, Klien G. van; Wijnberg, Inge D.; Kolk, Johannes H. van der; Breda, Eric van

doi:10.2460/ajvr.67.5.837

Cited by 24 publications

(17 citation statements)

References 39 publications

(31 reference statements)

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“…Literature supports a differential response of these kinases after exercise, although most authors report transient activations following either resistance or endurance exercise (van Ginneken et al 2006;Kramer and Goodyear 2007). Our data support this differential activation state between p38 and ERK1/2.…”

Section: Discussionsupporting

confidence: 79%

Role of Toll-like receptor 2 and 4 signaling pathways on the inflammatory response to resistance training in elderly subjects

Rodriguez‐Miguelez

Fernandez‐Gonzalo

Almar

et al. 2014

AGE

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This study assessed the effects of a resistance exercise training program on the inflammatory response associated with Toll-like receptor (TLR) 2 and TLR4 signaling pathways in senior participants. Twenty-six healthy subjects (age, 69.5±1.3) were randomized to a training (TG; n=16) or a control (CG; n=10) group. TG performed an 8-week resistance training program, while CG followed their daily routines. Peripheral blood mononuclear cells were isolated from blood samples obtained before and after the intervention, and levels of proteins involved in the TLR2, TLR4, and myeloid differentiation primary response gene 88 (MyD88)-dependent and MyD88-independent pathways were analyzed. The inflammatory status was evaluated through messenger RNA (mRNA) and protein content of interleukin (IL)-10 and tumor necrosis factor alpha (TNF-α) and plasma levels of C-reactive protein (CRP). After the 8-week resistance training, TLR2 and TLR4 protein expression was reduced in TG. MyD88, p65, phosphop38, TIR domain-containing adaptor inducing interferon (TRIF), IKKi/IKKε, phospho-interferon regulatory factor (IRF) 3, and phosho-IRF7 were also downregulated in TG after the intervention. The training program induced an increase of phospho-extracellular signal-regulated kinases 1 and 2 (ERK1/2) and Hsp70 and a reduction of Hsp60. While TNF-α mRNA and protein values remained unchanged in both TG and CG, IL-10 mRNA and protein content were upregulated in TG after the intervention. CRP values decreased in TG only. The increase in Hsp70 negatively correlated with TLR2 and TLR4 downregulation. These data suggest that resistance exercise may represent an effective tool to ameliorate the pro-inflammatory status of old participants through an attenuation of MyD88-dependent and MyD88-independent TLR2 and TLR4 signaling pathways.

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Section: Discussionsupporting

confidence: 79%

Role of Toll-like receptor 2 and 4 signaling pathways on the inflammatory response to resistance training in elderly subjects

Rodriguez‐Miguelez

Fernandez‐Gonzalo

Almar

et al. 2014

AGE

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“…Increased staining for phosphorylated HSP27 in biopsies from horses obtained within 10 min after apparently nondamaging aerobic exercise is reported by Von Ginneken et al (53). However, Koh and Escobedo (23) found Fig.…”

Section: Discussionmentioning

confidence: 62%

Maximal eccentric exercise induces a rapid accumulation of small heat shock proteins on myofibrils and a delayed HSP70 response in humans

Paulsen¹,

Vissing²,

Kalhovde³

et al. 2007

American Journal of Physiology-Regulatory, Integrative and Comp

135

154

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In this study the stress protein response to unaccustomed maximal eccentric exercise in humans was investigated. Eleven healthy males performed 300 maximal eccentric actions with the quadriceps muscle. Biopsies from vastus lateralis were collected at 30 min and 4, 8, 24, 96, and 168 h after exercise. Cellular regulation and localization of heat shock protein (HSP) 27, αB-crystallin, and HSP70 were analyzed by immunohistochemistry, ELISA technique, and Western blotting. Additionally, mRNA levels of HSP27, αB-crystallin, and HSP70 were quantified by Northern blotting. After exercise (30 min), 81 ± 8% of the myofibers showed strong HSP27 staining ( P < 0.01) that gradually decreased during the following week. αB-Crystallin mimicked the changes observed in HSP27. After exercise (30 min), the ELISA analysis showed a 49 ± 13% reduction of the HSP27 level in the cytosolic fraction ( P < 0.01), whereas Western blotting revealed a 15-fold increase of the HSP27 level in the myofibrillar fraction ( P < 0.01). The cytosolic HSP70 level increased to 203 ± 37% of the control level 24 h after exercise ( P < 0.05). After 4 days, myofibrillar-bound HSP70 had increased ∼10-fold ( P < 0.01) and was accompanied by strong staining on cross sections. mRNA levels of HSP27, αB-crystallin, and HSP70 were all elevated the first day after exercise ( P < 0.01); HSP70 mRNA showed the largest increase (20-fold at 8 h). HSP27 and αB-crystallin seemed to respond immediately to maximal eccentric exercise by binding to cytoskeletal/myofibrillar proteins, probably to function as stabilizers of disrupted myofibrillar structures. Later, mRNA and total HSP protein levels, especially HSP70, increased, indicating that HSPs play a role in skeletal muscle recovery and remodeling/adaptation processes to high-force exercise.

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“…Although the precise function of a majority of these induced proteins is still unclear, many Hsps, as molecular chaperones, provide cells with a mechanism to prevent damage caused by misfolded, damaged, aggregated proteins (Hightower 1991). Several studies have shown that earlier experience with the stressor helps to improve induction (Donnelly et al 1992;Marber et al 1993;Yellon et al 1992;Walker et al 1993;van Ginneken et al 2006), transfection (Suzuki et al 1997), or overexpression of Hsp proteins if the stressor occurs again (Marber et al 1995;Ooie et al 2005;Gauthaman et al 2005;Chiu et al 2003). It is known that Hsp induction, and particularly Hsp70, can protect the myocardium from ischemia and reduces the infarction size in mice (Wu and Tanguay 2006;Seok et al 2007).…”

Section: Discussionmentioning

confidence: 99%

Expression and distribution of heat shock proteins in the heart of transported pigs

Bao

Sultan

Nowak

et al. 2008

Cell Stress and Chaperones

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Effect of exercise on activation of the p38 mitogen-activated protein kinase pathway, c-Jun NH2 terminal kinase, and heat shock protein 27 in equine skeletal muscle

Abstract: The p38 pathway and JNK are activated in the vastus lateralis muscle after a single 20-minute bout of submaximal exercise in trained horses. Phosphorylation of HSP27 as detected in the study reported here is most likely induced through the p38 signaling pathway.

Cited by 24 publications

References 39 publications

Role of Toll-like receptor 2 and 4 signaling pathways on the inflammatory response to resistance training in elderly subjects

Role of Toll-like receptor 2 and 4 signaling pathways on the inflammatory response to resistance training in elderly subjects

Maximal eccentric exercise induces a rapid accumulation of small heat shock proteins on myofibrils and a delayed HSP70 response in humans

Expression and distribution of heat shock proteins in the heart of transported pigs

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