scholarly journals Involvement of histone H3 phosphorylation through p38 MAPK pathway activation in casticin-induced cytocidal effects against the human promyelocytic cell line HL-60

2013 ◽  
Vol 43 (6) ◽  
pp. 2046-2056 ◽  
Author(s):  
HIDETOMO KIKUCHI ◽  
BO YUAN ◽  
EISUKE YUHARA ◽  
NORIO TAKAGI ◽  
HIROO TOYODA
Keyword(s):  
Cell Line ◽  
P38 Mapk ◽  
Mapk Pathway ◽  
Histone H3 ◽  
P38 Mapk Pathway ◽  
H3 Phosphorylation ◽  
Pathway Activation ◽  
Histone H3 Phosphorylation

scholarly journals Intracellular albumin overload elicits endoplasmic reticulum stress and PKC-delta/p38 MAPK pathway activation to induce podocyte apoptosis

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Guilherme Lopes Gonçalves ◽  
Juliana Martins Costa-Pessoa ◽  
Karina Thieme ◽  
Bruna Bezerra Lins ◽  
Maria Oliveira-Souza
Keyword(s):  
Endoplasmic Reticulum ◽  
Endoplasmic Reticulum Stress ◽  
P38 Mapk ◽  
Mapk Pathway ◽  
Pkc Delta ◽  
P38 Mapk Pathway ◽  
Pathway Activation

Glypican-3 (GPC3) inhibits metastasis development promoting dormancy in breast cancer cells by p38 MAPK pathway activation

2020 ◽  
Vol 99 (6) ◽  
pp. 151096 ◽  
Author(s):  
Macarena Guereño ◽  
Magali Delgado Pastore ◽  
Ana Clara Lugones ◽  
Magalí Cercato ◽  
Laura Todaro ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
P38 Mapk ◽  
Breast Cancer Cells ◽  
Mapk Pathway ◽  
P38 Mapk Pathway ◽  
Pathway Activation ◽  
Metastasis Development

Cadmium induced apoptosis in mouse primary hepatocytes: the role of oxidative stress-mediated ERK pathway activation and the involvement of histone H3 phosphorylation

RSC Advances ◽  
2015 ◽  
Vol 5 (40) ◽  
pp. 31798-31806 ◽  
Author(s):  
Jing Wang ◽  
Minglu Hao ◽  
Chunguang Liu ◽  
Rutao Liu
Keyword(s):  
Oxidative Stress ◽  
Histone H3 ◽  
Erk Signaling ◽  
Erk Pathway ◽  
Primary Hepatocytes ◽  
H3 Phosphorylation ◽  
Pathway Activation ◽  
Induced Apoptosis ◽  
Histone H3 Phosphorylation

Time-delayed apoptosis induced by cadmium in primary hepatocytes through DNA damage, histone modification and ERK signaling cascade, which are all mediated by oxidative stress.

scholarly journals MKK6/3 and p38 MAPK Pathway Activation Is Not Necessary for Insulin-induced Glucose Uptake but Regulates Glucose Transporter Expression

2001 ◽  
Vol 276 (23) ◽  
pp. 19800-19806 ◽  
Author(s):  
Midori Fujishiro ◽  
Yukiko Gotoh ◽  
Hideki Katagiri ◽  
Hideyuki Sakoda ◽  
Takehide Ogihara ◽  
...  
Keyword(s):  
Glucose Uptake ◽  
P38 Mapk ◽  
Glucose Transporter ◽  
Mapk Pathway ◽  
P38 Mapk Pathway ◽  
Pathway Activation ◽  
Transporter Expression

EGFR-independent activation of p38 MAPK and EGFR-dependent activation of ERK1/2 are required for ROS-induced renal cell death

2004 ◽  
Vol 287 (5) ◽  
pp. F1049-F1058 ◽  
Author(s):  
Jing Dong ◽  
Sampath Ramachandiran ◽  
Kulbhushan Tikoo ◽  
Zhe Jia ◽  
Serrine S. Lau ◽  
...  
Keyword(s):  
Cell Death ◽  
P38 Mapk ◽  
Egf Receptor ◽  
Histone H3 ◽  
Dominant Negative ◽  
Mapk Activation ◽  
Transfected Cells ◽  
H3 Phosphorylation ◽  
Hsp27 Phosphorylation ◽  
Histone H3 Phosphorylation

2,3,5-Tris-(glutathion- S-yl)hydroquinone (TGHQ), a reactive metabolite of the nephrotoxicant hydroquinone, induces the ROS-dependent activation of MAPKs, followed by histone H3 phosphorylation and oncotic cell death in renal proximal tubule epithelial cells (LLC-PK1). Cell death and histone H3 phosphorylation are attenuated by pharmacological inhibition of p38 MAPK or ERK1/2 pathways. Because TGHQ, but not epidermal growth factor (EGF), induces histone H3 phosphorylation and cell death in LLC-PK1 cells, we hypothesized that there are differences in the mechanisms by which TGHQ and EGF induce activation of the EGF receptor (EGFR). We therefore compared the relative ability of TGHQ, H2O2, and EGF to activate EGFR and MAPKs and found that p38 MAPK activation is EGFR independent, whereas ERK1/2 activation occurs mainly through EGFR activation. TGHQ, H2O2, and EGF induce different EGFR tyrosine phosphorylation profiles that likely influence the subsequent differential kinetics of MAPK activation. We next transfected LLC-PK1 cells with a dominant negative p38 MAPK-expressing plasmid (pcDNA3-DNp38). TGHQ failed to induce phosphorylation of p38 MAPK and its substrate, MK-2, in pcDNA3-DNp38-transfected cells, indicating loss of function of p38 MAPK. In untransfected, pcDNA3 or pcDNA3-p38 (native)-transfected LLC-PK1 cells, Hsp27 was intensively phosphorylated after TGHQ treatment, whereas in pcDNA3-DNp38-transfected cells, TGHQ failed to induce Hsp27 phosphorylation. Thus EGFR-independent p38 MAPK and EGFR-dependent ERK1/2 activation by TGHQ lead to the activation of two downstream signaling factors, i.e., histone H3 and Hsp27 phosphorylation, which have in common the potential ability to remodel chromatin.

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