p38 MAP kinases: beyond the stress response

Nebreda, Ángel R.; Porrás, Almudena

doi:10.1016/s0968-0004(00)01595-4

Cited by 511 publications

(409 citation statements)

References 27 publications

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“…Either way, the correlation disappeared in postintervention biopsies, pointing towards a complex training-associated manner of transcriptional regulation, which may be related to body mass composition, as previously discussed. Moreover, regulation of FNDC5 expression seems to encompass p38 mitogen-activated protein kinase (MAPK), which in turn is known to be controlled through a range of cellular stressors such as proinflammatory cytokines (Nebreda and Porras 2000). This essentially puts FNDC5 expression under control of a range of physiological cues, not only exercise.…”

Section: Discussionmentioning

confidence: 99%

Irisin and FNDC5: effects of 12-week strength training, and relations to muscle phenotype and body mass composition in untrained women

Ellefsen¹,

Vikmoen²,

Slettaløkken³

et al. 2014

Eur J Appl Physiol

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This file was dowloaded from the institutional repository Brage NIH -brage.bibsys.no/nih Ellefsen, S., Vikmoen, O., Slettaløkken, G., Whist, J. E., Nygård, H., Hollan, I.... Rønnestad, B. (2014). Irisin and FNDC5: effects of 12-week strength training, and relations to muscle phenotype and body mass composition in untrained women. MethodsEighteen untrained women performed 12 weeks of progressive whole body heavy strength training, with measurement of strength, body composition, expression of irisin-related genes (FNDC5 and PGC1α) in two different skeletal muscles, and levels of serum-irisin and -thyroid hormones, before and after the training intervention. ResultsThe strength training intervention did not result in changes in serum-irisin or muscle FNDC5 expression, despite considerable effects on strength, lean body mass (LBM) and skeletal muscle phenotype. However, our data indicate that training affects irisin biology in a LBM-dependent

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Section: Discussionmentioning

confidence: 99%

Irisin and FNDC5: effects of 12-week strength training, and relations to muscle phenotype and body mass composition in untrained women

Ellefsen¹,

Vikmoen²,

Slettaløkken³

et al. 2014

Eur J Appl Physiol

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“…There are three major sub-groups that include extracellular signal-regulated kinase (ERK1/2), p38 MAPK, and c-jun-N-terminal kinase (JNK). P38 MAPK is a subfamily of the stress-activated MAPKs (SAPKs) [40][41][42]. In isolated rat hearts, drugs like ketamine and imipramine have been shown to activate the MAPK/ERK (extracellular signal-regulated kinase), which is accompanied by an increase in Mg 2+ that results in decreased heart rate [18,43].…”

Section: Introductionmentioning

confidence: 99%

l-Carnitine rescues ketamine-induced attenuated heart rate and MAPK (ERK) activity in zebrafish embryos

Kanungo

Cuevas

Ali

et al. 2012

Reproductive Toxicology

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Ketamine, an antagonist of the N-methyl-D-aspartate (NMDA)-type glutamate receptors, is a pediatric anesthetic. Ketamine has been shown to be neurotoxic and cardiotoxic in mammals. Here, we show that after 2 h of exposure, 5 mM ketamine significantly reduced heart rate in 26 h old zebrafish embryos. In 52 h old embryos, 1 mM ketamine was effective after 2 h and 0.5 mM ketamine at 20 h of exposure. Ketamine also induced significant reductions in activated MAPK (ERK) levels. Treatment of the embryos with the ERK inhibitor, PD 98059, also significantly reduced heart rate whereas the p38/SAPK inhibitor, SB203580, was ineffective. Ketamine is known to inhibit lipolysis and a decrease of ATP content in the heart. Co-treatment with Lcarnitine that enhances fatty acid metabolism effectively rescued ketamine-induced attenuated heart rate and ERK activity. These findings demonstrate that L-carnitine counteracts ketamine's negative effects on heart rate and ERK activity in zebrafish embryos.

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“…Mitogen-activated protein kinases (MAPKs) are activated in response to a variety of extracellular stimuli (Nishida and Gotoh, 1993;Davis, 1994;Waskiewicz and Cooper, 1995;Cohen, 1996;Kyriakis and Avruch, 1996;Su and Karin, 1996;Brunet and Pouyssegur, 1997;Robinson and Cobb, 1997;Nebreda and Porras, 2000). The p38 group of kinases belongs to the MAPK family and plays an important role in cell proliferation, cell differentiation, cell death, development, and immune responses (Ono and Han, 2000).…”

Section: Introductionmentioning

confidence: 99%

Regulation of PRAK Subcellular Location by p38 MAP Kinases

New

Jiang

Han

2003

MBoC

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The p38 mitogen-activated protein kinase (MAPK) pathway plays an important role in cellular responses to inflammatory stimuli and environmental stress. p38 regulated/activated protein kinase (PRAK, also known as mitogen-activated protein kinase activated protein kinase 5 [MAP-KAPK5]) functions downstream of p38␣ and p38␤ in mediating the signaling of the p38 pathway. Immunostaining revealed that endogenous PRAK was predominantly localized in the cytoplasm. Interestingly, ectopically expressed PRAK was localized in the nucleus and can be redistributed by coexpression of p38␣ or p38␤ to the locations of p38␣ and p38␤. Mutations in the docking groove on p38␣/p38␤, or the p38-docking site in PRAK, disrupted the PRAK-p38 interaction and impaired the ability of p38␣ and p38␤ to redistribute ectopically expressed PRAK, indicating that the location of PRAK could be controlled by its docking interaction with p38␣ and p38␤. Although the majority of PRAK molecules were detected in the cytoplasm, PRAK is consistently shuttling between the cytoplasm and the nucleus. A sequence analysis of PRAK shows that PRAK contains both a putative nuclear export sequence (NES) and a nuclear localization sequence (NLS). The shuttling of PRAK requires NES and NLS motifs in PRAK and can be regulated through cellular activation induced by stress stimuli. The nuclear content of PRAK was reduced after stimulation, which resulted from a decrease in the nuclear import of PRAK and an increase in the nuclear export of PRAK. The nuclear import of PRAK is independent from p38 activation, but the nuclear export requires p38-mediated phosphorylation of PRAK. Thus, the subcellular distribution of PRAK is determined by multiple factors including its own NES and NLS, docking interactions between PRAK and docking proteins, phosphorylation of PRAK, and cellular activation status. The p38 MAPKs not only regulate PRAK activity and PRAK activation-related translocation, but also dock PRAK to selected subcellular locations in resting cells.

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p38 MAP kinases: beyond the stress response

Cited by 511 publications

References 27 publications

Irisin and FNDC5: effects of 12-week strength training, and relations to muscle phenotype and body mass composition in untrained women

Irisin and FNDC5: effects of 12-week strength training, and relations to muscle phenotype and body mass composition in untrained women

l-Carnitine rescues ketamine-induced attenuated heart rate and MAPK (ERK) activity in zebrafish embryos

Regulation of PRAK Subcellular Location by p38 MAP Kinases

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