scholarly journals ATP Depletion-induced Actin Rearrangement Reduces Cell Adhesion via p38 MAPK-HSP27 Signaling in Renal Proximal Tubule Cells

2010 ◽  
Vol 25 (4-5) ◽  
pp. 501-510 ◽  
Author(s):  
Jun Du ◽  
Lijia Zhang ◽  
Yu Yang ◽  
Weixing Li ◽  
Ling Chen ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Proximal Tubule ◽  
P38 Mapk ◽  
Renal Proximal Tubule ◽  
Atp Depletion ◽  
Proximal Tubule Cells ◽  
Tubule Cells ◽  
Renal Proximal Tubule Cells ◽  
Actin Rearrangement

Oxalate inhibits renal proximal tubule cell proliferation via oxidative stress, p38 MAPK/JNK, and cPLA2 signaling pathways

2004 ◽  
Vol 287 (4) ◽  
pp. C1058-C1066 ◽  
Author(s):  
Ho Jae Han ◽  
Min Jin Lim ◽  
Yun Jung Lee
Keyword(s):  
Oxidative Stress ◽  
Proximal Tubule ◽  
Signaling Pathways ◽  
P38 Mapk ◽  
Thymidine Incorporation ◽  
Renal Proximal Tubule ◽  
Proximal Tubule Cells ◽  
Tubule Cells ◽  
Renal Proximal Tubule Cells ◽  
Mapk Inhibitor

Exposure of renal proximal tubule cells to oxalate may play an important role in cell proliferation, but the signaling pathways involved in this effect have not been elucidated. Thus the present study was performed to examine the effect of oxalate on 3H-labeled thymidine incorporation and its related signal pathway in primary cultured rabbit renal proximal tubule cells (PTCs). The effects of oxalate on [3H]thymidine incorporation, lactate dehydrogenase (LDH) release, Trypan blue exclusion, H2O2 release, activation of mitogen-activated protein kinases (MAPKs), and 3H-labeled arachidonic acid (AA) release were examined in primary cultured renal PTCs. Oxalate inhibited [3H]thymidine incorporation in a time- and dose-dependent manner. However, its analogs did not affect [3H]thymidine incorporation. Oxalate (1 mM) significantly increased H2O2 release, which was blocked by N-acetyl-l-cysteine (NAC) and catalase (antioxidants). Oxalate significantly increased p38 MAPK and stress-activated protein kinase (SAPK)/c-Jun NH2-terminal kinase (JNK) activity, not p44/42 MAPK. Oxalate stimulated [3H]AA release and translocation of cytosolic phospholipase A2 (cPLA2) from the cytosolic fraction to the membrane fraction. Indeed, oxalate significantly increased prostaglandin E2 (PGE2) production compared with control. Oxalate-induced inhibition of [3H]thymidine incorporation and increase of [3H]AA release were prevented by antioxidants (NAC), a p38 MAPK inhibitor (SB-203580), a SAPK/JNK inhibitor (SP-600125), or PLA2 inhibitors [mepacrine and arachidonyl trifluoromethyl ketone (AACOCF3)], but not by a p44/42 MAPK inhibitor (PD-98059). These findings suggest that oxalate inhibits renal PTC proliferation via oxidative stress, p38 MAPK/JNK, and cPLA2 signaling pathways.

scholarly journals ERK and p38 MAPK inhibition controls NF-E2 degradation and profibrotic signaling in renal proximal tubule cells

Life Sciences ◽  
2021 ◽  
pp. 120092
Author(s):  
Jia Li ◽  
Shunying Jin ◽  
Michelle T. Barati ◽  
Sanjana Rane ◽  
Qian Lin ◽  
...  
Keyword(s):  
Proximal Tubule ◽  
P38 Mapk ◽  
Renal Proximal Tubule ◽  
Proximal Tubule Cells ◽  
Tubule Cells ◽  
Renal Proximal Tubule Cells

Effect of adenosine triphosphate on phosphate uptake in renal proximal tubule cells: Involvement of PKC and p38 MAPK

2005 ◽  
Vol 205 (1) ◽  
pp. 68-76 ◽  
Author(s):  
Yun Jung Lee ◽  
Soo Hyun Park ◽  
Tae Oh Jeung ◽  
Kee Won Kim ◽  
Jang Hern Lee ◽  
...  
Keyword(s):  
Proximal Tubule ◽  
P38 Mapk ◽  
Adenosine Triphosphate ◽  
Phosphate Uptake ◽  
Renal Proximal Tubule ◽  
Proximal Tubule Cells ◽  
Tubule Cells ◽  
Renal Proximal Tubule Cells

Effects of TCDD and estradiol-17β on the proliferation and Na+/glucose cotransporter in renal proximal tubule cells

2005 ◽  
Vol 19 (1) ◽  
pp. 21-30 ◽  
Author(s):  
Ho Jae Han ◽  
Min Jin Lim ◽  
Yun Jung Lee ◽  
Eun Jung Kim ◽  
Young Jin Jeon ◽  
...  
Keyword(s):  
Proximal Tubule ◽  
Renal Proximal Tubule ◽  
Proximal Tubule Cells ◽  
Tubule Cells ◽  
Renal Proximal Tubule Cells ◽  
Estradiol 17Β

Abstract P238: Regulation Of G Protein-coupled Receptor Kinase 4 Expression By Serum In Breast Cancer And Renal Proximal Tubule Cells

Hypertension ◽  
2021 ◽  
Vol 78 (Suppl_1) ◽  
Author(s):  
Wei Yue ◽  
Peng Xu ◽  
John J Gildea ◽  
Robin A Felder
Keyword(s):  
Breast Cancer ◽  
Protein Synthesis ◽  
Proximal Tubule ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Renal Proximal Tubule ◽  
Proximal Tubule Cells ◽  
Tubule Cells ◽  
Renal Proximal Tubule Cells ◽  
G Protein Coupled

G protein-coupled receptor kinase 4 (GRK4) is a member of the GRK family which play critical role in regulation of the function of G protein-coupled receptors. Our previous studies have shown that GRK4 not only plays a role in regulating sodium excretion in renal proximal tubule cells but also acts as a stimulator on proliferation of breast cancer cells. Uncontrolled proliferation is a characteristics of cancer cells and GRK4 is upregulated in breast cancer cells. We hypothesized that expression of GRK4 may be regulated differently in cancer and non-cancer cells. To test this hypothesis, expression of GRK4 in response to serum was compared in breast cancer cells and renal proximal tubule cells by Western analysis. In three breast cancer cell lines serum withdrawal caused rapid reduction in the levels of GRK4 which occurred as early as 15 min. GRK4 levels correlated with the concentrations of serum added to the culture media. To determine if growth factors were a critical element for maintaining GRK4 levels in the cells, EGF (10-20 ng/ml) was added to serum free medium for 24 h. There was no increase in GRK4 levels in the cells treated with EGF compared with the serum starvation control. Similarly, serum withdrawal (16 h) led to 40-80% decrease of GRK4 levels in renal proximal tubule cells even in the presence of EFG supplement. Serum feeding for 30 min after starvation dramatically increased the levels of GRK4 in both breast cancer cells and RPTC which exceeded the steady state levels. This rapid recovery of GRK4 protein do not need de novo protein synthesis because pretreatment of the cells with protein synthesis inhibitor, cycloheximide (10 μg/ml, 24 h), did not prevent this event. Expression of GRK2, another member of the GRK family, was not affected by serum starvation. Our results have shown that GRK4 is very sensitive to serum concentration in breast cancer cells as well as in RPTC. Preliminary studies suggest that rapid protein degradation rather than shutting down the protein synthesis plays a major role in this kind of GRK4 regulation. The biological significance of serum regulation of GRK4 in cancer and non-cancerous cells needs further investigation.

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