scholarly journals New view in cell death mode: effect of crystal size in renal epithelial cells

2015 ◽  
Vol 6 (12) ◽  
pp. e2013-e2013 ◽  
Author(s):  
X-Y Sun ◽  
J-M Ouyang
Keyword(s):  
Cell Death ◽  
Epithelial Cells ◽  
Crystal Size ◽  
Renal Epithelial Cells ◽  
Mode Effect ◽  
New View

scholarly journals Increased Hexokinase Activity, of Either Ectopic or Endogenous Origin, Protects Renal Epithelial Cells against Acute Oxidant-induced Cell Death

2001 ◽  
Vol 277 (13) ◽  
pp. 11392-11400 ◽  
Author(s):  
Jane M. Bryson ◽  
Platina E. Coy ◽  
Kathrin Gottlob ◽  
Nissim Hay ◽  
R. Brooks Robey
Keyword(s):  
Cell Death ◽  
Epithelial Cells ◽  
Renal Epithelial Cells ◽  
Hexokinase Activity

scholarly journals ERK pathway mediates P2X7 expression and cell death in renal interstitial fibroblasts exposed to necrotic renal epithelial cells

2011 ◽  
Vol 301 (3) ◽  
pp. F650-F659 ◽  
Author(s):  
Murugavel Ponnusamy ◽  
Na Liu ◽  
Rujun Gong ◽  
Haidong Yan ◽  
Shougang Zhuang
Keyword(s):  
Cell Death ◽  
Epithelial Cells ◽  
Signaling Pathway ◽  
P2x7 Receptor ◽  
Transcriptional Factor ◽  
Erk Pathway ◽  
Signaling Mechanism ◽  
Renal Epithelial Cells ◽  
Extracellular Signal ◽  
Dose Dependent

We recently reported that necrotic renal proximal epithelial cells (RPTC) stimulate the expression of P2X7 receptor in renal fibroblasts and that P2X7 receptor mediates deleterious epithelial-fibroblast cross talk. The present study was carried out to investigate the signaling mechanism of necrotic RPTC-induced P2X7 expression in cultured renal interstitial fibroblasts (NRK-49F). Exposure of NRK-49F to necrotic RPTC supernatant (RPTC-Sup) induced a time- and dose-dependent phosphorylation of several signaling pathways including extracellular signal-regulated kinases (ERK1/2), p38, c-Jun N-terminal kinases (JNKs), and AKT in NRK-49F. Pharmacological inhibition of ERK1/2, but not p38, JNK, and AKT pathways, blocked RPTC-Sup-induced P2X7 expression and renal interstitial fibroblast death. Knockdown of ERK1/2 or MEK1, a direct upstream activator of ERK1/2, also reduced RPTC-Sup-induced P2X7 expression and cell death of renal fibroblasts. Conversely, overexpression of MEK1 enhanced these responses. Upon necrotic RPTC exposure, phosphorylation of Elk1, a transcriptional factor targeted by ERK1/2, was increased in NRK-49F, and knockdown of Elk1 by siRNA remarkably reduced RPTC-Sup-induced P2X7 expression as well as renal fibroblast death. Furthermore, silencing of MEK1 inhibited Elk1 phosphorylation in response to necrotic RPTC, whereas overexpression of MEK1 increased Elk1 phosphorylation. Taken together, these data reveal that necrotic RPTC induces P2X7 expression in renal fibroblasts through activation of the MEK1-ERK1/2-Elk1 signaling pathway.

scholarly journals A role for c-myc in chemically induced renal-cell death.

1997 ◽  
Vol 17 (11) ◽  
pp. 6755-6764 ◽  
Author(s):  
Y Zhan ◽  
J L Cleveland ◽  
J L Stevens
Keyword(s):  
Cell Death ◽  
Epithelial Cells ◽  
Apoptotic Cell ◽  
Tubular Damage ◽  
Transactivation Domain ◽  
Apoptotic Pathway ◽  
Toxicant Exposure ◽  
Renal Epithelial Cells ◽  
Cell Death Pathway

A variety of genes, including c-myc, are activated by chemical toxicants in vivo and in vitro. Although enforced c-myc expression induces apoptosis after withdrawing survival factors, it is not clear if activation of the endogenous c-myc gene is an apoptotic signal after toxicant exposure. The renal tubular epithelium is a target for many toxicants. c-myc expression is activated by tubular damage. In quiescent LLC-PK1 renal epithelial cells, c-myc but not max or mad mRNA is induced by the nephrotoxicant S-(1,2-dichlorovinyl)-L-cysteine (DCVC). The kinetics of DCVC-induced c-myc expression and apoptosis suggested an association between cell death and prolonged activation of c-myc expression after toxicant exposure. Accordingly, prolonged activation of an estrogen receptor-Myc fusion construct, but not a construct in which a c-Myc transactivation domain had been deleted, was sufficient to induce apoptosis in LLC-PK1 cells. Moreover, under conditions in which necrosis was the predominant cell death pathway caused by DCVC in parental cells, overexpressing c-myc biased the cell death pathway toward apoptosis. DCVC also induced ornithine decarboxylase (odc) mRNA and activated the odc promoter. Activation of the odc promoter by DCVC required consensus c-Myc-Max binding sites in odc intron 1. Inhibiting ODC activity with alpha-difluoromethylornithine delayed DCVC-induced cell death. Therefore, odc is a target gene in the DCVC apoptotic pathway involving c-myc activation and contributes to apoptosis. Finally, a structurally related cytotoxic but nongenotoxic analog of DCVC did not induce c-myc and did not activate the odc promoter or induce apoptosis. The data support the hypothesis that activation of apoptotic cell death in quiescent renal epithelial cells involves induction of c-myc. This is the first study to demonstrate that c-myc induction by a specific nephrotoxicant leads to gene activation and cell death.

Multiple cell death pathways are independently activated by lethal hypertonicity in renal epithelial cells

2013 ◽  
Vol 305 (10) ◽  
pp. C1011-C1020 ◽  
Author(s):  
Soo Youn Choi ◽  
Whaseon Lee-Kwon ◽  
Hwan Hee Lee ◽  
Jun Ho Lee ◽  
Satoru Sanada ◽  
...  
Keyword(s):  
Cell Death ◽  
Epithelial Cells ◽  
Cytochrome C ◽  
Cathepsin B ◽  
Extrinsic Pathway ◽  
Renal Epithelial Cells ◽  
Caspase Inhibitors ◽  
Cell Death Pathways ◽  
Cell Death Pathway ◽  
Multiple Cell

When hypertonicity is imposed with sufficient intensity and acuteness, cells die. Here we investigated the cellular pathways involved in death using a cell line derived from renal epithelium. We found that hypertonicity rapidly induced activation of an intrinsic cell death pathway—release of cytochrome c and activation of caspase-3 and caspase-9—and an extrinsic pathway—activation of caspase-8. Likewise, a lysosomal pathway of cell death characterized by partial lysosomal rupture and release of cathepsin B from lysosomes to the cytosol was also activated. Relationships among the pathways were examined using specific inhibitors. Caspase inhibitors did not affect cathepsin B release into the cytosol by hypertonicity. In addition, cathepsin B inhibitors and caspase inhibitors did not affect hypertonicity-induced cytochrome c release, suggesting that the three pathways were independently activated. Combined inhibition of caspases and cathepsin B conferred significantly more protection from hypertonicity-induced cell death than inhibition of caspase or cathepsin B alone, indicating that all the three pathways contributed to the hypertonicity-induced cell death. Similar pattern of sensitivity to the inhibitors was observed in two other cell lines derived from renal epithelia. We conclude that multiple cell death pathways are independently activated early in response to lethal hypertonic stress in renal epithelial cells.

scholarly journals Endoplasmic Reticulum Chaperones GRP78 and Calreticulin Prevent Oxidative Stress, Ca2+Disturbances, and Cell Death in Renal Epithelial Cells

1997 ◽  
Vol 272 (35) ◽  
pp. 21751-21759 ◽  
Author(s):  
Hong Liu ◽  
Russell C. Bowes ◽  
Bob van de Water ◽  
Christopher Sillence ◽  
J. Fred Nagelkerke ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Endoplasmic Reticulum ◽  
Cell Death ◽  
Epithelial Cells ◽  
Renal Epithelial Cells

scholarly journals Enhanced apoptotic cell death of renal epithelial cells in mice lacking transcription factor AP-2beta

1997 ◽  
Vol 11 (15) ◽  
pp. 1938-1948 ◽  
Author(s):  
M. Moser ◽  
A. Pscherer ◽  
C. Roth ◽  
J. Becker ◽  
G. Mucher ◽  
...  
Keyword(s):  
Cell Death ◽  
Transcription Factor ◽  
Epithelial Cells ◽  
Apoptotic Cell ◽  
Apoptotic Cell Death ◽  
Renal Epithelial Cells
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