Effects of sub-lethal neurite outgrowth inhibitory concentrations of chlorpyrifos oxon on cytoskeletal proteins and acetylcholinesterase in differentiating N2a cells

2011 ◽  
Vol 256 (3) ◽  
pp. 330-336 ◽  
Author(s):  
J. Flaskos ◽  
E. Nikolaidis ◽  
W. Harris ◽  
M. Sachana ◽  
A.J. Hargreaves
Keyword(s):  
Neurite Outgrowth ◽  
Cytoskeletal Proteins ◽  
N2a Cells

scholarly journals Expression of MicroRNA-29a Regulated by Yes-Associated Protein Modulates the Neurite Outgrowth in N2a Cells

2017 ◽  
Vol 2017 ◽  
pp. 1-13 ◽  
Author(s):  
Chunye Tan ◽  
Changlin Yu ◽  
Zhiwen Song ◽  
Hongjun Zou ◽  
Xu Xu ◽  
...  
Keyword(s):  
Neurite Outgrowth ◽  
Strong Association ◽  
In Silico Analysis ◽  
Luciferase Reporter ◽  
N2a Cells ◽  
Chip Experiment ◽  
High Level ◽  
Phosphatase And Tensin Homologue ◽  
Opposite Tendency ◽  
Silico Analysis

Yes-associated protein (YAP) is proved to increase miR-29a in the present study, but the relevant molecular mechanism is not clear. Also, growing evidence indicates that the high-level miR-29a promotes the neurite outgrowth by decreasing PTEN (phosphatase and tensin homologue deleted on chromosome 10). Results show that the expression of miR-29a increases but the PTEN decreases during transfecting the N2a cells with the YAP plasmid. Meanwhile, the advancement of neurite outgrowth is presented via using multiple methods to detect the expression of GAP-43 and NF-200, which have a strong association with neurite outgrowth. The expression of miR-29a, GAP-43, and NF-200 shows an opposite tendency compared to the PTEN when YAP is downregulated. By treating N2a cells with miR-29a mimic and inhibitor, we also find the same conclusion. For in silico analysis of miR-29a, its promoter may have a binding site for YAP. Based on a luciferase reporter assay and a chromatin immunoprecipitation (ChIP) experiment, we demonstrate that YAP could increase the expression of miR-29a by targeting the promoter of miR-29a. In conclusion, the results identify that YAP promotes the neurite outgrowth via targeting the promoter of miR-29a, and it may be an effective therapeutic medicine for the neural disease.

Characterization of a PC12 cell sub-clone (PC12-C41) with enhanced neurite outgrowth capacity: implications for a modulatory role of high molecular weight tau in neuritogenesis

1993 ◽  
Vol 106 (2) ◽  
pp. 611-626 ◽  
Author(s):  
K.K. Teng ◽  
I.S. Georgieff ◽  
J.M. Aletta ◽  
J. Nunez ◽  
M.L. Shelanski ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Neurite Outgrowth ◽  
Pc12 Cell ◽  
Cell Types ◽  
Neuronal Morphology ◽  
Cytoskeletal Proteins ◽  
Parental Line ◽  
Pheochromocytoma Cells ◽  
Tau Expression

To address the means by which diversity of neuronal morphology is generated, we have isolated and characterized naturally occurring variants of rat PC12 pheochromocytoma cells that exhibit altered neurite outgrowth properties in response to nerve growth factor (NGF). We describe here a PC12 cell sub-clone, designated PC12-clone 41 (PC12-C41), that displays significant increases in neurite abundance and stability when compared with the parental line. This difference does not appear to be due to an altered sensitivity or responsiveness to NGF or to a more rapid rate of neurite extension. Because of the role of the cytoskeleton in neuritogenesis, we examined a panel of the major cytoskeletal proteins (MAP 1.2/1B, beta-tubulin, chartins, peripherin, and high and low molecular weight (HMW and LMW) taus) whose levels and/or extent of phosphorylation are regulated by NGF in PC12 cultures. Although most cytoskeletal proteins showed little difference between PC12 and PC12-C41 cells (+/- NGF treatment), there was a significant contrast between the two lines with respect to tau expression. In particular, while NGF increases the total specific levels of tau in both cell types to similar extents (by about twofold), the proportion comprising HMW tau is threefold higher in the PC12-C41 clone than in PC12 cells. A comparable difference was observed under substratum conditions that were non-permissive for neurite outgrowth and so this effect was not merely a consequence of the differential neuritogenic capacities of the two lines. The distinction between the expression of HMW and LMW taus in PC12 and PC12-C41 cells (+/- NGF) was also observed at the level of the messages encoding these proteins. Such findings indicate that initiation of neurite outgrowth in PC12 cultures does not require a massive induction of tau expression and raise the possibility that HMW and LMW taus may have differential capacities for modulating neuronal morphology.

GSK-3β activation mediates Nogo-66-induced inhibition of neurite outgrowth in N2a cells

2011 ◽  
Vol 505 (2) ◽  
pp. 165-170 ◽  
Author(s):  
Jian-ying Shen ◽  
Xu-xia Yi ◽  
Nan-xiang Xiong ◽  
Hai-jun Wang ◽  
Xiao-wei Duan ◽  
...  
Keyword(s):  
Neurite Outgrowth ◽  
N2a Cells ◽  
Gsk 3Β

scholarly journals Protease Omi facilitates neurite outgrowth in mouse neuroblastoma N2a cells by cleaving transcription factor E2F1

2015 ◽  
Vol 36 (8) ◽  
pp. 966-975 ◽  
Author(s):  
Qi Ma ◽  
Qing-song Hu ◽  
Ran-jie Xu ◽  
Xue-chu Zhen ◽  
Guang-hui Wang
Keyword(s):  
Transcription Factor ◽  
Neurite Outgrowth ◽  
Mouse Neuroblastoma ◽  
N2a Cells ◽  
Transcription Factor E2f1

Effects of avermectins on neurite outgrowth in differentiating mouse neuroblastoma N2a cells

2010 ◽  
Vol 192 (2) ◽  
pp. 206-211 ◽  
Author(s):  
Ying-Jian Sun ◽  
Ding-Xin Long ◽  
Wei Li ◽  
Wei-Yuan Hou ◽  
Yi-Jun Wu ◽  
...  
Keyword(s):  
Neurite Outgrowth ◽  
Mouse Neuroblastoma ◽  
N2a Cells

scholarly journals Duloxetine-Induced Neural Cell Death and Promoted Neurite Outgrowth in N2a Cells

2020 ◽  
Vol 38 (4) ◽  
pp. 859-870
Author(s):  
Wanli Gao ◽  
Rui Chen ◽  
Nan Xie ◽  
Daolin Tang ◽  
Borong Zhou ◽  
...  
Keyword(s):  
Cell Death ◽  
Neurite Outgrowth ◽  
Drug Effects ◽  
Annexin V ◽  
Neural Cell ◽  
Metabolic Enzyme ◽  
Tunel Staining ◽  
Neurite Length ◽  
N2a Cells ◽  
Biochemical Testing

Abstract Duloxetine is a clinical drug that is primarily used for treatment of depression and pain, but it has side effects of addiction and tolerance. Cytochrome P450 (CYP) is its metabolic enzyme, and the drug’s biofunction results from its neuro-protective effect in animal and cell models. We aimed to investigate the duloxetine-induced neural cytotoxicity effect and its performance in an N2a cell neurite outgrowth model. Cell death was assessed as cell viability using a Cell Count Kit-8 and further evaluated using bright-field images, propidium iodide (PI) and annexin V staining, colony-formation analysis, TUNEL staining of the cells, and biochemical testing. N2a cells were committed to differentiation by serum withdrawal and RA induction, and the neurite outgrowth was evaluated as the number of differentiated cells, longest neurite length, and average neurite length. Cell cycle analysis, PI and annexin V staining, mRNA expression, and biochemical testing were used to evaluate the drug effects on differentiation. The induction of neural cell death by duloxetine was not affected by classic cell death inhibitors but was promoted by the CYP inducer rifampicin. N2a cell neurite outgrowth was promoted by duloxetine via reduction of the CYP2D6 and MDA levels and induction of Bdnf protein levels. Duloxetine induces neural cell death through effects on CYP and promotes N2a cell neurite outgrowth by regulating CYP, Bdnf protein, and the intracellular lipid peroxidation level.

scholarly journals Neurite outgrowth inhibitory levels of organophosphates induce tissue transglutaminase activity in differentiating N2a cells: evidence for covalent adduct formation

2020 ◽  
Vol 94 (11) ◽  
pp. 3861-3875
Author(s):  
Ibtesam S. Almami ◽  
Maha A. Aldubayan ◽  
Shatha G. Felemban ◽  
Najiah Alyamani ◽  
Richard Howden ◽  
...  
Keyword(s):  
Neurite Outgrowth ◽  
Tissue Transglutaminase ◽  
Neuroblastoma Cells ◽  
Cytoskeletal Proteins ◽  
Direct Role ◽  
Cell Monolayers ◽  
Cell Lysates ◽  
Sds Page ◽  
Covalent Adduct

Abstract Organophosphate compounds (OPs) induce both acute and delayed neurotoxic effects, the latter of which is believed to involve their interaction with proteins other than acetylcholinesterase. However, few OP-binding proteins have been identified that may have a direct role in OP-induced delayed neurotoxicity. Given their ability to disrupt Ca2+ homeostasis, a key aim of the current work was to investigate the effects of sub-lethal neurite outgrowth inhibitory levels of OPs on the Ca2+-dependent enzyme tissue transglutaminase (TG2). At 1–10 µM, the OPs phenyl saligenin phosphate (PSP) and chlorpyrifos oxon (CPO) had no effect cell viability but induced concentration-dependent decreases in neurite outgrowth in differentiating N2a neuroblastoma cells. The activity of TG2 increased in cell lysates of differentiating cells exposed for 24 h to PSP and chlorpyrifos oxon CPO (10 µM), as determined by biotin-cadaverine incorporation assays. Exposure to both OPs (3 and/or 10 µM) also enhanced in situ incorporation of the membrane permeable substrate biotin-X-cadaverine, as indicated by Western blot analysis of treated cell lysates probed with ExtrAvidin peroxidase and fluorescence microscopy of cell monolayers incubated with FITC-streptavidin. Both OPs (10 µM) stimulated the activity of human and mouse recombinant TG2 and covalent labelling of TG2 with dansylamine-labelled PSP was demonstrated by fluorescence imaging following SDS-PAGE. A number of TG2 substrates were tentatively identified by mass spectrometry, including cytoskeletal proteins, chaperones and proteins involved protein synthesis and gene regulation. We propose that the elevated TG2 activity observed is due to the formation of a novel covalent adduct between TG2 and OPs.

Rosiglitazone promotes neurite outgrowth and mitochondrial function in N2A cells via PPARgamma pathway

Mitochondrion ◽  
2014 ◽  
Vol 14 ◽  
pp. 7-17 ◽  
Author(s):  
Ming-Chang Chiang ◽  
Yi-Chuan Cheng ◽  
Han-Min Chen ◽  
Yao-Jen Liang ◽  
Chia-Hui Yen
Keyword(s):  
Neurite Outgrowth ◽  
Mitochondrial Function ◽  
N2a Cells

P4-166 Overexpression of CDK-5 induces hyperphosphorylation of cytoskeletal proteins and impairment of axonal transport in N2A cells

2004 ◽  
Vol 25 ◽  
pp. S522-S523
Author(s):  
Juan Chen ◽  
Honglian Yipeng ◽  
Youmei Jianzhi ◽  
Li Wang ◽  
Feng Wang
Keyword(s):  
Axonal Transport ◽  
Cytoskeletal Proteins ◽  
N2a Cells
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