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

In vitro effects of Npt2a inhibition in renal proximal tubule cells

2020 ◽  
Vol 34 (S1) ◽  
pp. 1-1
Author(s):  
Linto Thomas ◽  
Jianxiang Xue ◽  
Jessica Dominguez Rieg ◽  
Timo Rieg
Keyword(s):  
Proximal Tubule ◽  
Renal Proximal Tubule ◽  
Proximal Tubule Cells ◽  
Tubule Cells ◽  
Renal Proximal Tubule Cells ◽  
In Vitro Effects

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.

scholarly journals Transcriptomic alterations induced by Monuron in rat and human renal proximal tubule cells in vitro and comparison to rat renal-cortex in vivo

2015 ◽  
Vol 4 (2) ◽  
pp. 423-431 ◽  
Author(s):  
Katarzyna M. Bloch ◽  
Noreen Yaqoob ◽  
Sikander Sharma ◽  
Andrew Evans ◽  
Lydia Aschauer ◽  
...  
Keyword(s):  
Developing Countries ◽  
Proximal Tubule ◽  
Renal Cortex ◽  
Renal Proximal Tubule ◽  
Proximal Tubule Cells ◽  
Tubule Cells ◽  
Renal Proximal Tubule Cells

Monuron (1,1-dimethyl-3-(4-chlorophenyl)urea) is a widely used herbicide in developing countries although concerns have been raised about its toxicity and carcinogenicity.

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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