ERK1/2 and p38-MAPK signalling pathways, through MSK1, are involved in NF-κB transactivation during oxidative stress in skeletal myoblasts

Kefaloyianni, Eirini; Gaitanaki, Catherine; Beis, Isidoros

doi:10.1016/j.cellsig.2006.05.004

Cited by 244 publications

(208 citation statements)

References 55 publications

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“…Most reports state that p38 MAPK can positively regulate NF-B activity, albeit through various mechanisms (62)(63)(64). In contrast, inhibition of p38 MAPK in our system caused a significant increase in NF-B activity in HeLa cells.…”

Section: Discussioncontrasting

confidence: 48%

Sphingosine Kinase 1 Regulates Tumor Necrosis Factor-mediated RANTES Induction through p38 Mitogen-activated Protein Kinase but Independently of Nuclear Factor κB Activation

Adada

Orr-Gandy

Snider

et al. 2013

Journal of Biological Chemistry

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Background: SK1 is widely involved in promoting inflammatory diseases. Results: Unexpectedly, loss of SK1 caused an increase in chemokines upon TNF stimulation. This occurred through regulation of p38 MAPK but independently of NF-B. Conclusion: SK1 negatively regulates RANTES expression through the p38 MAPK pathway. Significance: Targeting SK1 in therapy may affect inflammatory conditions by up-regulating chemokines independently of NF-B.

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Section: Discussioncontrasting

confidence: 48%

Sphingosine Kinase 1 Regulates Tumor Necrosis Factor-mediated RANTES Induction through p38 Mitogen-activated Protein Kinase but Independently of Nuclear Factor κB Activation

Adada

Orr-Gandy

Snider

et al. 2013

Journal of Biological Chemistry

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“…The present findings with BM-ca corroborate these findings in the Ramos B-NHL cell line. Inhibition of p38 MAPK and NF-κB activities has been shown to be mediated by upstream inhibition of Src kinases (22,31). The present findings corroborate these studies and demonstrate that treatment of Ramos cells with BM-ca inhibited the phosphorylation of p38 and inhibited the transcription factor NF-κB leading to inhibition of Mcl-1 and induction of Bax.…”

Section: Discussionsupporting

confidence: 81%

Dysregulation of the cell survival/anti-apoptotic NF-κB pathway by the novel humanized BM-ca anti-CD20 mAb: Implication in chemosensitization

et al. 2009

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Abstract. Treatment of patients with relapsed or refractory low grade follicular B-NHL lymphoma with rituximab (chimeric anti-CD20 mAb) has resulted in ~50% response rate. The mechanism underlying the failure of rituximab to affect the remaining 50% of the patients is not clear, though their tumors express CD20. The in vivo effector functions of rituximab include ADCC, CDC and seldom apoptosis. In addition, we have reported that rituximab signals the cells and inhibits several intracellular cell survival pathways that are responsible for the immuno and chemo-sensitizing effects of rituximab on resistant B-NHL cell lines. The objective of this study was to develop novel and fully humanized anti-CD20 monoclonal antibodies with enhanced effector functions and molecular signaling that may potentiate their therapeutic efficacy. Novel humanized anti-CD20 monoclonal antibodies were derived from a chimerized form of murine anti-CD20 1K11791, shown to exert a more potent ADCC, CDC and apoptotic activities compared to rituximab. A representative humanized monoclonal antibody, BM-ca was used to examine its biological effect and molecular signaling using Ramos B-NHL cell line as a model. The studies were also performed in parallel with rituximab treatment for comparison. Ramos cells were treated with various concentrations of BM-ca monoclonal antibody. Inhibition of cell proliferation was observed in a concentration-dependent manner, suggesting cell signal perturbations must have occurred. Compared to untreated cells, treatment with BM-ca inhibited both the constitutively activated NF-κB and p38 MAPK pathways, as assessed by inhibition of both phosphop65 and phospho-IκB· and phospho-p38, respectively, but not the unphosphorylated forms. BM-ca significantly induced the expression of the metastasis suppressor and immune surveillance cancer gene product, Raf-1 kinase inhibitor protein (RKIP). These alterations resulted in inhibition of antiapoptotic gene products and sensitized Ramos cells to apoptosis by CDDP. In comparison with rituximab, BM-ca showed qualitative and quantitative differences in the above analyses. These findings demonstrate that BM-ca triggers CD20 expressing B-NHL cells resulting in a significant alteration of several gene products that regulate cell growth and chemoresistance.

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“…Activated dimers containing p65 have previously been reported to participate in cachexia (Guttridge et al 2000), oxidative stress (Kefaloyianni et al 2006), and age-related atrophy (Phillips and Leeuwenburgh 2005). In addition, elevated contents of p65 have been reported in smooth muscle cells cultured in a high glucose environment, which led to increased p65-mediated tran- Fig.…”

Section: Nf-κb Subunit Quantificationmentioning

confidence: 99%

Diabetes-induced atrophy is associated with a muscle-specific alteration in NF-κB activation and expression

Frier

Noble

Locke

2008

Cell Stress and Chaperones

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NF-κB is a transcription factor implicated in pathological responses that develop during diabetes mellitus, including skeletal muscle atrophy. Given that NF-κB activation, protein composition, and content within diabetic skeletal muscle remain generally uncharacterized, a streptozotocin (STZ) model was used to assess NF-κB activation, composition, and content. Sprague-Dawley rats were injected with STZ (55 mg/kg) and after 30 days the soleus (SOL), plantaris (PL), red gastrocnemius (RG), and white gastrocnemius (WG) muscles were assessed by electrophoresis mobility shift assay and western blotting. NF-κB activation was detected in all muscles examined, but was reduced in RG muscles from diabetic animals. Supershifts indicated NF-κB was composed primarily of p50 in diabetic and control animals. The content of both p65 and p52 was elevated in SOL and PL muscles, while p52 was decreased in RG. The coactivating protein, Bcl-3, was increased in WG and RG, but decreased in PL. Both p50 and RelB remained unchanged in all tissues examined. All muscles from diabetic animals demonstrated reduced mass when compared to controls, but only the gastrocnemius demonstrated atrophy as reflected by a reduced muscle-to-body mass ratio. In conclusion, diabetic alterations to the contents and activation of the NF-κB protein were tissue-specific, but did not appear to alter dimer composition of constitutively bound NF-κB. These results indicate that diabetes may alter NF-κB activity and expression in a musclespecific manner.

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ERK1/2 and p38-MAPK signalling pathways, through MSK1, are involved in NF-κB transactivation during oxidative stress in skeletal myoblasts

Cited by 244 publications

References 55 publications

Sphingosine Kinase 1 Regulates Tumor Necrosis Factor-mediated RANTES Induction through p38 Mitogen-activated Protein Kinase but Independently of Nuclear Factor κB Activation

Sphingosine Kinase 1 Regulates Tumor Necrosis Factor-mediated RANTES Induction through p38 Mitogen-activated Protein Kinase but Independently of Nuclear Factor κB Activation

Dysregulation of the cell survival/anti-apoptotic NF-κB pathway by the novel humanized BM-ca anti-CD20 mAb: Implication in chemosensitization

Diabetes-induced atrophy is associated with a muscle-specific alteration in NF-κB activation and expression

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