Electrical stimulation with periodic alternating intervals stimulates neuronal cells to produce neurotrophins and cytokines through activation of mitogen-activated protein kinase pathways

2015 ◽  
Vol 123 (6) ◽  
pp. 403-408 ◽  
Author(s):  
Kenta Yamamoto ◽  
Toshiro Yamamoto ◽  
Kenichi Honjo ◽  
Hiroaki Ichioka ◽  
Fumishige Oseko ◽  
...  
Keyword(s):  
Electrical Stimulation ◽  
Protein Kinase ◽  
Neuronal Cells ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein

scholarly journals Phosphorylation of Ago2 and Subsequent Inactivation of let-7a RNP-Specific MicroRNAs Control Differentiation of Mammalian Sympathetic Neurons

2016 ◽  
Vol 36 (8) ◽  
pp. 1260-1271 ◽  
Author(s):  
Somi Patranabis ◽  
Suvendra Nath Bhattacharyya
Keyword(s):  
Protein Kinase ◽  
Neuronal Differentiation ◽  
Sympathetic Neurons ◽  
Neuronal Cells ◽  
Cellular Level ◽  
Mitogen Activated Protein Kinase ◽  
Animal Cells ◽  
Mitogen Activated Protein ◽  
Small Regulatory Rnas ◽  
Necessary And Sufficient

MicroRNAs (miRNAs) are small regulatory RNAs that regulate gene expression posttranscriptionally by base pairing to the target mRNAs in animal cells.KRas, an oncogene known to be repressed by let-7a miRNAs, is expressed and needed for the differentiation of mammalian sympathetic neurons and PC12 cells. We documented a loss of let-7a activity during this differentiation process without any significant change in the cellular level of let-7a miRNA. However, the level of Ago2, an essential component that is associated with miRNAs to form RNP-specific miRNA (miRNP) complexes, shows an increase with neuronal differentiation. In this study, differentiation-induced phosphorylation and the subsequent loss of miRNA from Ago2 were noted, and these accounted for the loss of miRNA activity in differentiating neurons. Neuronal differentiation induces the phosphorylation of mitogen-activated protein kinase p38 and the downstream kinase mitogen- and stress-activated protein kinase 1 (MSK1). This in turn upregulates the phosphorylation of Ago2 and ensures the dissociation of miRNA from Ago2 in neuronal cells. MSK1-mediated miRNP inactivation is a prerequisite for the differentiation of neuronal cells, where let-7a miRNA gets unloaded from Ago2 to ensure the upregulation ofKRas, a target of let-7a. We noted that the inactivation of let-7a is both necessary and sufficient for the differentiation of sympathetic neurons.

scholarly journals Rapid Membrane Effects of Steroids in Neuroblastoma Cells: Effects of Estrogen on Mitogen Activated Protein Kinase Signalling Cascade and c-fos Immediate Early Gene Transcription

Endocrinology ◽  
1997 ◽  
Vol 138 (9) ◽  
pp. 4030-4033 ◽  
Author(s):  
Jyoti J. Watters ◽  
Jean S. Campbell ◽  
Matthew J. Cunningham ◽  
Edwin G. Krebs ◽  
Daniel M. Dorsa
Keyword(s):  
Estrogen Receptor ◽  
Protein Kinase ◽  
Neuronal Cells ◽  
Mitogen Activated Protein Kinase ◽  
Early Gene ◽  
Human Neuroblastoma Cell ◽  
Human Neuroblastoma ◽  
Mitogen Activated Protein ◽  
Membrane Effects ◽  
17Β Estradiol

Abstract Rapid effects of steroid hormones have been observed in neuronal cells for many years. We show here, that in the human neuroblastoma cell line SK-N-SH, the membrane impermeable conjugated 17β-estradiol (E2BSA) activates mitogen activated protein kinase kinase (MAPKK or MEK) and induces the phosphorylation and activation of both ERK-1 and ERK-2 (mitogen activated protein kinase or MAPK). Additionally, E2BSA induces the transcription of a reporter gene construct driven by the promoter of the mouse c-fos proto-oncogene. The effects of this membrane impermeable estrogen on c-fos transcription are not inhibited by the estrogen receptor antagonists. Tamoxifen or ICI 182,780, further excluding the involvement of the intracellular estrogen receptor. This is also illustrated by the observation that E2BSA does not activate estrogen response element (ERE) mediated transcription. This is the first report of rapid membrane effects of 17β-estradiol on growth factor related signalling pathways in neuronal cells, and indicates a potential mechanism by which 17β-estradiol might affect the expression of genes whose promoters do not contain EREs but are responsive to factors acting through other response elements such as AP-1 and SRE sites.

scholarly journals Novel Mechanism for Gonadotropin-Releasing Hormone Neuronal Migration Involving Gas6/Ark Signaling to p38 Mitogen-Activated Protein Kinase

2002 ◽  
Vol 22 (2) ◽  
pp. 599-613 ◽  
Author(s):  
Melissa P. Allen ◽  
Daniel A. Linseman ◽  
Hiroshi Udo ◽  
Mei Xu ◽  
Jerome B. Schaack ◽  
...  
Keyword(s):  
Protein Kinase ◽  
P38 Mapk ◽  
Neuronal Migration ◽  
Neuronal Cells ◽  
Gonadotropin Releasing Hormone ◽  
Dominant Negative ◽  
Mitogen Activated Protein Kinase ◽  
Gnrh Neuron ◽  
Releasing Hormone ◽  
Mitogen Activated Protein

ABSTRACT Gonadotropin-releasing hormone (GnRH) is the central regulator of the reproductive axis. Normal sexual maturation depends on the migration of GnRH neurons from the olfactory placode to the hypothalamus during development. Previously, we showed restricted expression of the membrane receptor adhesion-related kinase (Ark) in immortalized cell lines derived from migratory but not postmigratory GnRH neurons. In addition, Ark and GnRH transcripts were detected along the GnRH neuron migratory route in the E13 mouse cribriform plate. In the present study, we examined the role of Ark and its ligand, Gas6 (encoded by growth arrest-specific gene 6), in GnRH neuron migration. Gas6 stimulated lamellipodial extension, membrane ruffling, and chemotaxis of immortalized NLT GnRH neuronal cells via the Ark receptor. Gas6/Ark signaling promoted activation of the Rho family GTPase Rac, and adenoviral-mediated expression of dominant negative N17Rac abolished Gas6/Ark-induced actin cytoskeletal reorganization and migration of GnRH neuronal cells. In addition, p38 MAPK was activated downstream of Ark and Rac, and inhibition of p38 MAPK with either SB203580 or adenoviral dominant negative p38α also blocked Gas6/Ark-mediated migration. Finally, downstream of Rac and p38 mitogen-activated protein kinase (MAPK), Gas6/Ark signaling promoted activation of MAPK-activated protein kinase 2 and induced phosphorylation of HSP25, a known regulator of cortical actin remodeling. The data are the first to demonstrate a migratory signaling pathway downstream of Ark/Axl family receptors and suggest a previously unidentified role for p38 MAPK in neuronal migration. Furthermore, these studies support a potential role for Ark in the regulation of GnRH neuronal migration.

Age-Related Changes in Activation of Mitogen-Activated Protein Kinase Cascades by Oxidative Stress

1998 ◽  
Vol 3 (1) ◽  
pp. 23-27 ◽  
Author(s):  
Kathryn Z Guyton ◽  
Myriani Gorospe ◽  
Xiantao Wang ◽  
Yolanda D Mock ◽  
Gertrude C Kokkonen ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Protein Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Age Related ◽  
Mitogen Activated Protein ◽  
Age Related Changes
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