New Insights into the Control of MAP Kinase Pathways

English, Jessie M.; Pearson, Gray W.; Wilsbacher, Julie L.; Swantek, Jennifer L.; Karandikar, Mahesh; Xu, Shuichan; Cobb, Melanie H.

doi:10.1006/excr.1999.4687

Cited by 391 publications

(305 citation statements)

References 191 publications

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“…MKP-1 is an endogenous inhibitor of the MAPK and is a dual-specificity phosphatase (Camps et al 2000;English et al 1999). As such, MKP-1 acts to inactivate the main members of the MAPK family such as ERK, P38, and JNK.…”

Section: Anxa1 Regulates Tnfα Mrna Stabilitymentioning

confidence: 99%

The regulation of TNFα production after heat and endotoxin stimulation is dependent on Annexin-A1 and HSP70

Nair

Arora

Lim

et al. 2015

Cell Stress and Chaperones

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Febrile temperatures can induce stress responses which protect cells from damage and can reduce inflammation during infections and sepsis. However, the mechanisms behind the protective functions of heat in response to the bacterial endotoxin LPS are unclear. We have recently shown that Annexin-1 (ANXA1)-deficient macrophages exhibited higher TNFα levels after LPS stimulation. Moreover, we have previously reported that ANXA1 can function as a stress protein.Therefore in this study, we determined if ANXA1 is involved in the protective effects of heat on cytokine levels in macrophages after heat and LPS. Exposure of macrophages to 42°C for 1 h prior to LPS results in an inhibition of TNFα production, which was not evident in ANXA1 −/− macrophages. We show that this regulation involves primarily MYD88-independent pathways. ANXA1 regulates TNFα mRNA stability after heat and LPS, and this is dependent on endogenous ANXA1 expression and not exogenously secreted factors. Further mechanistic studies revealed the possible involvement of the heat shock protein HSP70 and JNK in the heat and inflammatory stress response regulated by ANXA1. This study shows that ANXA1, an immunomodulatory protein, is critical in the heat stress response induced after heat and endotoxin stimulation.

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Section: Anxa1 Regulates Tnfα Mrna Stabilitymentioning

confidence: 99%

The regulation of TNFα production after heat and endotoxin stimulation is dependent on Annexin-A1 and HSP70

Nair

Arora

Lim

et al. 2015

Cell Stress and Chaperones

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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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“…The mitogen-activated protein kinases (MAPK) transduce extracellular signals into cellular responses, and so they play important roles in proliferation, apoptosis, differentiation, migration and cytoskeleton remodeling of cells (English et al, 1999;Widmann et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Regulation of hepatocyte growth factor-mediated urokinase plasminogen activator secretion by MEK/ERK activation in human stomach cancer cell lines

Lee

Choi²,

Kim³

et al. 2006

Exp Mol Med

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The regulatory mechanisms for the proliferation and the particular invasive phenotypes of stomach cancers are not still fully understood. Up-regulations of hepatocytes growth factor (HGF), its receptor (cMet), and urokinase-type plasminogen activator (uPA) are correlated with the development and metastasis of cancers. In order to investigate roles of HGF/c-Met signaling in tumor progression and metastasis in stomach cancers, we determined effects of a specific MEK1 inhibitor (PD098059) and a p38 kinase inhibitor (SB203580) on HGF-mediated cell proliferation and uPA expression in stomach cancer cell lines (NUGC-3 and MKN-28). HGF treatment induced the phosphorylations of ERK and p38 kinase in time-and dose-dependent manners. Pre-treatment with PD098059 reduced HGF-mediated cell proliferation and uPA secretion. In contrast, SB203580 pre-treatment enhanced cell proliferation and uPA secretion due to induction of ERK phosphorylation. Stable expression of dominant negative-MEK1 in NUGC-3 cells showed a decrease in HGF-mediated uPA secretion. These results suggest that interaction of a MEK/ERK and a p38 kinase might play an important role in proliferation and invasiveness of stomach cancer cells.

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New Insights into the Control of MAP Kinase Pathways

Cited by 391 publications

References 191 publications

The regulation of TNFα production after heat and endotoxin stimulation is dependent on Annexin-A1 and HSP70

The regulation of TNFα production after heat and endotoxin stimulation is dependent on Annexin-A1 and HSP70

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

Regulation of hepatocyte growth factor-mediated urokinase plasminogen activator secretion by MEK/ERK activation in human stomach cancer cell lines

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