scholarly journals Simvastatin attenuates oleic acid-induced oxidative stress through CREB-dependent induction of heme oxygenase-1 in renal proximal tubule cells

2015 ◽  
Vol 79 (2) ◽  
pp. 243-250 ◽  
Author(s):  
Meaghan Barnett ◽  
Samuel Hall ◽  
Mehul Dixit ◽  
Istvan Arany
Keyword(s):  
Oxidative Stress ◽  
Oleic Acid ◽  
Proximal Tubule ◽  
Heme Oxygenase ◽  
Renal Proximal Tubule ◽  
Heme Oxygenase 1 ◽  
Proximal Tubule Cells ◽  
Tubule Cells ◽  
Renal Proximal Tubule Cells

Mechanism of heme oxygenase-1 gene induction by curcumin in human renal proximal tubule cells

2001 ◽  
Vol 281 (5) ◽  
pp. F851-F859 ◽  
Author(s):  
Nathalie Hill-Kapturczak ◽  
Vijayalaksmi Thamilselvan ◽  
Feiyan Liu ◽  
Harry S. Nick ◽  
Anupam Agarwal
Keyword(s):  
Proximal Tubule ◽  
Heme Oxygenase ◽  
Gene Induction ◽  
Renal Proximal Tubule ◽  
Heme Oxygenase 1 ◽  
Proximal Tubule Cells ◽  
Tubule Cells ◽  
Renal Proximal Tubule Cells

Mechanism of heme oxygenase-1 gene induction by curcumin in human renal proximal tubule cells

2001 ◽  
Vol 281 (5) ◽  
pp. F851-F859 ◽  
Author(s):  
Nathalie Hill-Kapturczak ◽  
Vijayalaksmi Thamilselvan ◽  
Feiyan Liu ◽  
Harry S. Nick ◽  
Anupam Agarwal
Keyword(s):  
Transcription Factor ◽  
Proximal Tubule ◽  
Heme Oxygenase ◽  
Nuclear Factor Κb ◽  
Renal Proximal Tubule ◽  
Heme Oxygenase 1 ◽  
Potent Inducer ◽  
Proximal Tubule Cells ◽  
Tubule Cells ◽  
Renal Proximal Tubule Cells

First published August 9, 2001; 10.1152/ajprenal.00140.2001.—Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, releasing iron, carbon monoxide, and biliverdin. Induction of HO-1 occurs as an adaptive and protective response to several inflammatory stimuli. The transcription factor activator protein-1 (AP-1) has been implicated in the activation of the HO-1 gene. To elucidate the molecular mechanism of HO-1 induction, we examined the effects of diferuloylmethane (curcumin), an inhibitor of the transcription factor AP-1. Surprisingly, curcumin by itself was a very potent inducer of HO-1. Curcumin has anti-inflammatory, antioxidant, and renoprotective effects. To evaluate the mechanism of curcumin-mediated induction of HO-1, confluent human renal proximal tubule cells were exposed to curcumin (1–8 μM). We observed a time- and dose-dependent induction of HO-1 mRNA that was associated with increased HO-1 protein. Coincubation of curcumin with actinomycin D completely blocked the upregulation of HO-1 mRNA. Blockade of nuclear factor-κB (NF-κB) with an IκBα phosphorylation inhibitor attenuated curcumin-mediated induction of HO-1 mRNA and protein. These data demonstrate that curcumin induces HO-1 mRNA and protein in renal proximal tubule cells. HO-1 induction by curcumin is mediated, at least in part, via transcriptional mechanisms and involves the NF-κB pathway.

p66SHC-mediated mitochondrial dysfunction in renal proximal tubule cells during oxidative injury

2010 ◽  
Vol 298 (5) ◽  
pp. F1214-F1221 ◽  
Author(s):  
Istvan Arany ◽  
Amir Faisal ◽  
Jeb S. Clark ◽  
Trinity Vera ◽  
Radhakrishna Baliga ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Cytochrome C ◽  
Proximal Tubule ◽  
Mitochondrial Dysfunction ◽  
Oxidative Injury ◽  
Renal Proximal Tubule ◽  
Mitochondrial Depolarization ◽  
Proximal Tubule Cells ◽  
Tubule Cells ◽  
Renal Proximal Tubule Cells

Mitochondrial dysfunction is involved in pathopysiology of ischemia-reperfusion-induced acute kidney injury (AKI). The p66shc adaptor protein is a newly recognized mediator of mitochondrial dysfunction, which might play a role in AKI-induced renal tubular injury. Oxidative stress-mediated Serine36 phosphorylation of p66shc facilitates its transportation to the mitochondria where it oxidizes cytochrome c and generates excessive amount of reactive oxygen species (ROS). The consequence is mitochondrial depolarization and injury. Earlier we determined that p66shc plays an essential role in injury of cultured mouse renal proximal tubule cells during oxidative stress. Here, we studied the role of p66shc in ROS generation and consequent mitochondrial dysfunction during oxidative injury in renal proximal tubule cells. We employed p66shc knockdown renal proximal tubule cells and cells that overexpress wild-type, Serine phosphorylation (S36A), or cytochrome c-binding (W134F) mutants of p66shc. Inhibition of the mitochondrial electron transport chain or the mitochondrial permeability transition revealed that hydrogen peroxide-induced injury is mitochondrial ROS and consequent mitochondrial depolarization dependent. We also found that through Ser36 phosphorylation and mitochondria/cytochrome c binding, p66shc mediates those effects. We propose a similar mechanism in vivo as we demonstrated mitochondrial binding of p66shc as well as its association with cytochrome c in the postischemic kidneys of mice. Thus, manipulating p66shc might offer a new therapeutic modality to ameliorate renal ischemic injury.

Effect of Caffeic Acid on Apical Transporters’ Dysfunction of Renal Proximal Tubule Cells under Oxidative Stress in vitro

Planta Medica ◽  
2002 ◽  
Vol 68 (6) ◽  
pp. 483-486 ◽  
Author(s):  
Ho Jae Han ◽  
Soo Hyun Park ◽  
Kwon Moo Park ◽  
Byung Cheol Yoon ◽  
Tae Sung Kim ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Proximal Tubule ◽  
Caffeic Acid ◽  
Renal Proximal Tubule ◽  
Proximal Tubule Cells ◽  
Tubule Cells ◽  
Renal Proximal Tubule Cells

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.

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