scholarly journals Aristolochic acids — Induced transcriptomic responses in rat renal proximal tubule cells in vitro

Genomics Data ◽  
2015 ◽  
Vol 5 ◽  
pp. 254-256
Author(s):  
Katarzyna M. Bloch ◽  
Andrew Evans ◽  
Edward A. Lock
Keyword(s):  
Proximal Tubule ◽  
Renal Proximal Tubule ◽  
Proximal Tubule Cells ◽  
Aristolochic Acids ◽  
Rat Renal Proximal Tubule ◽  
Tubule Cells ◽  
Transcriptomic Responses ◽  
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

Negative reciprocity between angiotensin II type 1 and dopamine D1 receptors in rat renal proximal tubule cells

2008 ◽  
Vol 295 (4) ◽  
pp. F1110-F1116 ◽  
Author(s):  
Farah Khan ◽  
Zuzana Špicarová ◽  
Sergey Zelenin ◽  
Ulla Holtbäck ◽  
Lena Scott ◽  
...  
Keyword(s):  
Angiotensin Ii ◽  
Proximal Tubule ◽  
Sodium Excretion ◽  
Renal Proximal Tubule ◽  
D1 Receptors ◽  
Short Term ◽  
Proximal Tubule Cells ◽  
Rat Renal Proximal Tubule ◽  
Tubule Cells ◽  
Renal Proximal Tubule Cells

Sodium excretion is bidirectionally regulated by dopamine, acting on D1-like receptors (D1R) and angiotensin II, acting on AT1 receptors (AT1R). Since sodium excretion has to be regulated with great precision within a short frame of time, we tested the short-term effects of agonist binding on the function of the reciprocal receptor within the D1R-AT1R complex in renal proximal tubule cells. Exposure of rat renal proximal tubule cells to a D1 agonist was found to result in a rapid partial internalization of AT1R and complete abolishment of AT1R signaling. Similarly, exposure of rat proximal tubule cells and renal tissue to angiotensin II resulted in a rapid partial internalization of D1R and abolishment of D1R signaling. D1R and AT1R were, by use of coimmunoprecipitation studies and glutathione- S-transferase pull-down assays, shown to be partners in a multiprotein complex. Na+-K+-ATPase, the target for both receptors, was included in this complex, and a region in the COOH-terminal tail of D1R (residues 397-416) was found to interact with both AT1R and Na+-K+-ATPase. Results indicate that AT1R and D1R function as a unit of opposites, which should provide a highly versatile and sensitive system for short-term regulation of sodium excretion.

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