Glomerular Epithelial Cells-Targeted Heme Oxygenase-1 Over Expression in the Rat: Attenuation of Proteinuria in Secondary But Not Primary Injury

Nephron ◽  
2016 ◽  
Vol 133 (4) ◽  
pp. 270-278 ◽  
Author(s):  
Vassilios Atsaves ◽  
Panagiota Makri ◽  
Maria G. Detsika ◽  
Alexandra Tsirogianni ◽  
Elias A. Lianos
Keyword(s):  
Epithelial Cells ◽  
Heme Oxygenase ◽  
Heme Oxygenase 1 ◽  
Over Expression ◽  
Glomerular Epithelial Cells ◽  
Primary Injury

scholarly journals Glomerular Proteinuria Induces Heme Oxygenase-1 Gene Expression within Renal Epithelial Cells

2005 ◽  
Vol 58 (4) ◽  
pp. 666-671 ◽  
Author(s):  
Masaki Shimizu ◽  
Kazuhide Ohta ◽  
Yonghong Yang ◽  
Akiko Nakai ◽  
Tomoko Toma ◽  
...  
Keyword(s):  
Gene Expression ◽  
Epithelial Cells ◽  
Heme Oxygenase ◽  
Heme Oxygenase 1 ◽  
Renal Epithelial Cells ◽  
Glomerular Proteinuria

scholarly journals Mechanism of Heme Oxygenase-1 Gene Activation by Cadmium in MCF-7 Mammary Epithelial Cells

2000 ◽  
Vol 275 (36) ◽  
pp. 27694-27702 ◽  
Author(s):  
Jawed Alam ◽  
Claire Wicks ◽  
Daniel Stewart ◽  
Pengfei Gong ◽  
Cheri Touchard ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Heme Oxygenase ◽  
Mammary Epithelial Cells ◽  
Gene Activation ◽  
Mammary Epithelial ◽  
Heme Oxygenase 1 ◽  
Mcf 7

Heme activates the heme oxygenase-1 gene in renal epithelial cells by stabilizing Nrf2

2003 ◽  
Vol 284 (4) ◽  
pp. F743-F752 ◽  
Author(s):  
Jawed Alam ◽  
Erin Killeen ◽  
Pengfei Gong ◽  
Ryan Naquin ◽  
Bin Hu ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Heme Oxygenase ◽  
Dominant Negative ◽  
Heme Oxygenase 1 ◽  
Mobility Shift ◽  
Multiple Copies ◽  
Proximal Tubular Epithelial Cells ◽  
Proximal Tubular ◽  
Electrophoretic Mobility Shift Assays ◽  
Nrf2 Protein

The mechanism of heme oxygenase-1 gene ( ho-1) activation by heme in immortalized rat proximal tubular epithelial cells was examined. Analysis of the ho-1promoter identified the heme-responsive sequences as the stress-response element (StRE), multiple copies of which are present in two enhancer regions, E1 and E2. Electrophoretic mobility shift assays identified Nrf2, MafG, ATF3, and Jun and Fos family members as StRE-binding proteins; binding of Nrf2, MafG, and ATF3 was increased in response to heme. Dominant-negative mutants of Nrf2 and Maf, but not of c-Fos and c-Jun, inhibited basal and heme-induced expression of an E1-controlled luciferase gene. Heme did not affect the transcription activity of Nrf2, dimerization between Nrf2 and MafG, or the level of MafG, but did stimulate expression of Nrf2. Heme did not influence the level of Nrf2 mRNA but increased the half-life of Nrf2 protein from ∼10 min to nearly 110 min. These results indicate that heme promotes stabilization of Nrf2, leading to accumulation of Nrf2 · MafG dimers that bind to StREs to activate the ho-1 gene.

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