Regulation of HA14-1 mediated oxidative stress, toxic response, and autophagy by curcumin to enhance apoptotic activity in human embryonic kidney cells

BioFactors ◽  
2013 ◽  
Vol 40 (1) ◽  
pp. 157-169 ◽  
Author(s):  
Kishu Ranjan ◽  
Anupama Sharma ◽  
Avadhesha Surolia ◽  
Chandramani Pathak
Keyword(s):  
Oxidative Stress ◽  
Kidney Cells ◽  
Human Embryonic Kidney ◽  
Toxic Response ◽  
Human Embryonic Kidney Cells ◽  
Apoptotic Activity

scholarly journals Heme oxygenase-2 (HO-2) binds and buffers labile heme, which is largely oxidized, in human embryonic kidney cells

2021 ◽  
Author(s):  
David A Hanna ◽  
Courtney M Moore ◽  
Liu Liu ◽  
Xiaojing Yuan ◽  
Angela S Fleischhacker ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Physiological Function ◽  
Hek293 Cells ◽  
Kidney Cells ◽  
Human Embryonic Kidney ◽  
Human Embryonic Kidney Cells ◽  
Heme Oxygenases ◽  
Heme Trafficking ◽  
Ferrous Heme

Heme oxygenases (HO) detoxify heme by oxidatively degrading it into carbon monoxide, iron, and biliverdin, which is reduced to bilirubin and excreted. Humans express two isoforms: inducible HO-1, which is up-regulated in response to various stressors, including excess heme, and constitutive HO-2. While much is known about the regulation and physiological function of HO-1, comparatively little is known about the role of HO-2 in regulating heme homeostasis. The biochemical necessity for expressing constitutive HO-2 is largely dependent on whether heme is sufficiently abundant and accessible as a substrate under conditions in which HO-1 is not induced. By measuring labile heme, total heme, and bilirubin in human embryonic kidney HEK293 cells with silenced or over-expressed HO-2, and various HO-2 mutant alleles, we found that endogenous heme is too limiting to support HO-2 catalyzed heme degradation. Rather, we discovered that a novel role for HO-2 is to bind and buffer labile heme. Taken together, in the absence of excess heme, we propose that HO-2 regulates heme homeostasis by acting as a heme buffering factor in control of heme bioavailability. When heme is in excess, HO-1 is induced and both HO-2 and HO-1 can provide protection from heme toxicity by enzymatically degrading it. Our results explain why catalytically inactive mutants of HO-2 are cytoprotective against oxidative stress. Moreover, the change in bioavailable heme due to HO-2 overexpression, which selectively binds ferric over ferrous heme, is consistent with the labile heme pool being oxidized, thereby providing new insights into heme trafficking and signaling.

scholarly journals Induction of CMV-1 promoter by 4-hydroxy-2-nonenal in human embryonic kidney cells.

2010 ◽  
Vol 57 (2) ◽  
Author(s):  
Morana Jaganjac ◽  
Tanja Matijevic ◽  
Marina Cindric ◽  
Ana Cipak ◽  
Lidija Mrakovcic ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Hydrogen Peroxide ◽  
Lipid Peroxidation ◽  
Free Radicals ◽  
Yellow Fluorescent Protein ◽  
Viral Reactivation ◽  
Kidney Cells ◽  
Human Embryonic Kidney ◽  
Human Embryonic Kidney Cells ◽  
Reactive Aldehydes

Oxidative stress, i.e., excessive production of oxygen free radicals and reactive oxygen species, leads to lipid peroxidation and to formation of reactive aldehydes which act as second messengers of free radicals. It has previously been shown that oxidative stress may be involved in the transcriptional regulation of cytomegalovirus (CMV) immediate early promoter, involved in viral reactivation from latency. In the current study we used a plasmid containing the yellow fluorescent protein (YFP) gene under the control of CMV-1 promoter to monitor the influence of hydrogen peroxide and reactive aldehydes, 4-hydroxy-2-nonenal (HNE) and acrolein, on CMV-1 promoter activation in human embryonic kidney cells (HEK293). While acrolein was ineffective, hydrogen peroxide slightly (50 %) stimulated the CMV promoter. In contrast, HNE had a strong, up to 3-fold, enhancing effect on the CMV-1 promoter within four as well as after 24h of treatment. The most effective was the treatment with 24 microM HNE. This effect of HNE suggests that stressful conditions associated with lipid peroxidation could lead to CMV activation.

Oxidative stress contributes to silica nanoparticle-induced cytotoxicity in human embryonic kidney cells

2009 ◽  
Vol 23 (5) ◽  
pp. 808-815 ◽  
Author(s):  
Fen Wang ◽  
Feng Gao ◽  
Minbo Lan ◽  
Huihui Yuan ◽  
Yongping Huang ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Silica Nanoparticle ◽  
Kidney Cells ◽  
Human Embryonic Kidney ◽  
Human Embryonic Kidney Cells

scholarly journals Functional Comparison between VP64-dCas9-VP64 and dCas9-VP192 CRISPR Activators in Human Embryonic Kidney Cells

2021 ◽  
Vol 22 (1) ◽  
pp. 397
Author(s):  
Nasir Javaid ◽  
Thuong L. H. Pham ◽  
Sangdun Choi
Keyword(s):  
Protein Level ◽  
Reference Genes ◽  
Mrna Level ◽  
High Specificity ◽  
Kidney Cells ◽  
Human Embryonic Kidney ◽  
Human Embryonic Kidney Cells ◽  
Sox2 Expression

Reversal in the transcriptional status of desired genes has been exploited for multiple research, therapeutic, and biotechnological purposes. CRISPR/dCas9-based activators can activate transcriptionally silenced genes after being guided by gene-specific gRNA(s). Here, we performed a functional comparison between two such activators, VP64-dCas9-VP64 and dCas9-VP192, in human embryonic kidney cells by the concomitant targeting of POU5F1 and SOX2. We found 22- and 6-fold upregulations in the mRNA level of POU5F1 by dCas9-VP192 and VP64-dCas9-VP64, respectively. Likewise, SOX2 was up-regulated 4- and 2-fold using dCas9-VP192 and VP64dCas9VP64, respectively. For the POU5F1 protein level, we observed 3.7- and 2.2-fold increases with dCas9-VP192 and VP64-dCas9-VP64, respectively. Similarly, the SOX2 expression was 2.4- and 2-fold higher with dCas9-VP192 and VP64-dCas9-VP64, respectively. We also confirmed that activation only happened upon co-transfecting an activator plasmid with multiplex gRNA plasmid with a high specificity to the reference genes. Our data revealed that dCas9-VP192 is more efficient than VP64-dCas9-VP64 for activating reference genes.

Fenton Reaction-Generated Advanced Oxidation Protein Products Induces Inflammation in Human Embryonic Kidney Cells

Inflammation ◽  
2016 ◽  
Vol 39 (4) ◽  
pp. 1285-1290 ◽  
Author(s):  
Guilherme Vargas Bochi ◽  
Vanessa Dorneles Torbitz ◽  
Roberto Christ Vianna Santos ◽  
Monica Cubillos-Rojas ◽  
José Luis Rosa López ◽  
...  
Keyword(s):  
Fenton Reaction ◽  
Advanced Oxidation ◽  
Kidney Cells ◽  
Human Embryonic Kidney ◽  
Advanced Oxidation Protein Products ◽  
Human Embryonic Kidney Cells
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