Primary cultures of normal rat kidney proximal tubule epithelial cells for studies of renal cell injury

1991 ◽  
Vol 27 (9) ◽  
pp. 739-748 ◽  
Author(s):  
Kathryn A. Elliget ◽  
Benjamin F. Trump
Pathobiology ◽  
1994 ◽  
Vol 62 (5-6) ◽  
pp. 298-310 ◽  
Author(s):  
Kathryn A. Elliget ◽  
Patricia C. Phelps ◽  
Benjamin F. Trump

2010 ◽  
Vol 2010 ◽  
pp. 1-10 ◽  
Author(s):  
Suzanne Heemskerk ◽  
Janny G. P. Peters ◽  
Jochem Louisse ◽  
Seil Sagar ◽  
Frans G. M. Russel ◽  
...  

During endotoxemia, the ATP-dependent drug efflux pump P-glycoprotein (Abcb1/P-gp) is upregulated in kidney proximal tubule epithelial cells. The signaling pathway through which lipopolysaccharide (LPS) or tumor necrosis factor-α(TNF-α) regulates P-gp expression and activity was investigated further in the present study. Exposure of rat kidney proximal tubule cells to TNF-αalone or TNF-αand LPS increased P-gp gene and protein expression levels and efflux activity, suggesting de novo P-gp synthesis. Upon exposure to TNF-αin combination with LPS, P-gp activity in renal proximal tubule cells is increased under influence of nitric oxide (NO) produced by inducible NO synthase. Upon exposure to TNF-αalone, P-gp upregulation seems to involve TLR4 activation and nuclear factor kappaB (NF-κB) translocation, a pathway that is likely independent of NO. These findings indicate that at least two pathways regulate P-gp expression in the kidney during endotoxemia.


2011 ◽  
Vol 36 (1) ◽  
pp. 127-129 ◽  
Author(s):  
Maki Tokumoto ◽  
Tomoaki Ohtsu ◽  
Akiko Honda ◽  
Yasuyuki Fujiwara ◽  
Hisamitsu Nagase ◽  
...  

2003 ◽  
Vol 285 (3) ◽  
pp. C608-C617 ◽  
Author(s):  
Snezana Petrovic ◽  
Liyun Ma ◽  
Zhaohui Wang ◽  
Manoocher Soleimani

SLC26A6 (or putative anion transporter 1, PAT1) is located on the apical membrane of mouse kidney proximal tubule and mediates [Formula: see text] exchange in in vitro expression systems. We hypothesized that PAT1 along with a [Formula: see text] exchange is present in apical membranes of rat kidney proximal tubules. Northern hybridizations indicated the exclusive expression of SLC26A6 (PAT1 or CFEX) in rat kidney cortex, and immunocytochemical staining localized SLC26A6 on the apical membrane of proximal tubules, with complete prevention of the labeling with the preadsorbed serum. To examine the functional presence of apical [Formula: see text] exchanger, proximal tubules were isolated, microperfused, loaded with the pH-sensitive dye BCPCF-AM, and examined by digital ratiometric imaging. The pH of the perfusate and bath was kept at 7.4. Buffering capacity was measured, and transport rates were calculated as equivalent base flux. The results showed that in the presence of basolateral DIDS (to inhibit [Formula: see text] cotransporter 1) and apical EIPA (to inhibit Na+/H+ exchanger 3), the magnitude of cell acidification in response to addition of luminal Cl– was ∼5.0-fold higher in the presence than in the absence of [Formula: see text]. The Cl–-dependent base transport was inhibited by ∼61% in the presence of 0.5 mM luminal DIDS. The presence of physiological concentrations of oxalate in the lumen (200 μM) did not affect the [Formula: see text] exchange activity. These results are consistent with the presence of SLC26A6 (PAT1) and [Formula: see text] exchanger activity in the apical membrane of rat kidney proximal tubule. We propose that SLC26A6 is likely responsible for the apical [Formula: see text] (and Cl–/OH–) exchanger activities in kidney proximal tubule.


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