scholarly journals Ischaemia and reperfusion injury of rat liver increases expression of glutathione S-transferase A1/A2 in zone 3 of the hepatic lobule

1998 ◽  
Vol 330 (1) ◽  
pp. 73-79 ◽  
Author(s):  
D. Gene BRANUM ◽  
Niazy SELIM ◽  
Xia LIU ◽  
Richard WHALEN ◽  
D. Thomas BOYER
Keyword(s):  
Reperfusion Injury ◽  
Fold Increase ◽  
Glutathione S Transferase ◽  
Hepatic Lobule ◽  
Ischaemia Reperfusion Injury ◽  
Transcript Levels ◽  
Protein Levels ◽  
Run Off ◽  
Liver Ischaemia

Effects of ischaemia-reperfusion injury (I/R) of liver on expression of rat glutathione S-transferase (rGST) isoenzymes that metabolize products of oxidative stress were examined. Rats underwent lobar liver ischaemia for 30 min followed by reperfusion. In ischaemic lobes, rGSTA1/A2 transcript levels increased significantly 12 h after I/R (2.94-fold) and protein levels increased significantly at 24 h (1.45-fold); increased transcript levels were also observed in nonischaemic lobes (1.78-fold). Superoxide dismutase prevented I/R and the increases in transcript and protein levels in ischaemic and non-ischaemic lobes. By in-situ hybridization, increases in transcript levels at 6 h were present in zones 2 and 3 of the ischaemic lobes and peaked at 12 h (2.5-fold zone 2, 4.5-fold zone 3). Significant increases in transcript levels also were observed at 24 h in zones 2 (2.0-fold) and 3 (2.9-fold) of non-ischaemic lobes. Nuclear run-off assays showed a 1.8-fold increase in rGSTA1/A2 transcription rates in ischaemic lobes at 3 h. We conclude that I/R causes increased rGSTA1/A2 expression in the zone of the hepatic lobule most susceptible to oxidative injury and that this expression may be an important defence against injury.

Differential lobular induction in rat liver of glutathioneS-transferase A1/A2 by phenobarbital

2000 ◽  
Vol 278 (4) ◽  
pp. G542-G550 ◽  
Author(s):  
Niazy Selim ◽  
Gene D. Branum ◽  
Xia Liu ◽  
Richard Whalen ◽  
Thomas D. Boyer
Keyword(s):  
Transcriptional Activity ◽  
Drug Metabolizing Enzymes ◽  
Glutathione S Transferase ◽  
Hepatic Lobule ◽  
Metabolizing Enzymes ◽  
Transcript Levels ◽  
Mrna Transcripts ◽  
Phenobarbital Administration ◽  
Rat Livers

Phenobarbital and other xenobiotics induce drug-metabolizing enzymes, including glutathione S-transferase A1/A2 (rGSTA1/A2). We examined the mechanism of induction of rGSTA1/A2 in rat livers after phenobarbital treatment. The induction of rGSTA1/A2 was not uniform across the hepatic lobule; steady-state transcript levels were threefold higher in perivenous hepatocytes relative to periportal hepatocytes when examined by in situ hybridization 12 h after a single dose of phenobarbital. Administration of a second dose of phenobarbital 12 or 24 h after the first dose did not equalize the induction of rGSTA1/A2 across the lobule. The transcriptional activity of the rGSTA1/A2 gene was increased 3.5- to 5.5-fold in whole liver by phenobarbital, but activities were the same in enriched periportal and perivenous subpopulations of hepatocytes from phenobarbital-treated animals. The half-life of rGSTA1/A2 mRNA in control animals was 3.6 h, whereas it was 10.2 h in phenobarbital-treated animals. We conclude that phenobarbital induces rGSTA1/A2 expression by increasing transcriptional activity across the lobule but induction of rGSTA1/A2 is greater in perivenous hepatocytes due to localized stabilization of mRNA transcripts.

scholarly journals Changes of cellular stress response related hsp70 and abcb1 transcript and Hsp70 protein levels in Siberian freshwater amphipods upon exposure to cadmium chloride in the lethal concentration range

PeerJ ◽  
2020 ◽  
Vol 8 ◽  
pp. e8635
Author(s):  
Marina V. Protopopova ◽  
Vasiliy V. Pavlichenko ◽  
Till Luckenbach
Keyword(s):  
Stress Response ◽  
Cadmium Chloride ◽  
Fold Increase ◽  
Cellular Stress Response ◽  
Lethal Concentration ◽  
Amphipod Species ◽  
Sensitive Species ◽  
Transcript Levels ◽  
Protein Levels ◽  
Hsp70 Protein

The induction of cellular stress response systems, heat shock protein hsp70/Hsp70 and multixenobiotic transporter abcb1, by cadmium chloride (CdCl2) was explored in amphipod species with different stress adaptation strategies from the Lake Baikal area. Based on the lethal concentrations (LC) of CdCl2, the sensitivities of the different species to CdCl2 were ranked (24 hr LC50 in mg/L CdCl2 (mean/95% confidence interval)): Gammarus lacustris (1.7/1.3–2.4) < Eulimnogammarus cyaneus (2.9/2.1–4.0) < Eulimnogammarus verrucosus (5.7/3.8–8.7) < Eulimnogammarus vittatus (18.1/12.4–26.6). Conjugated dienes, indicating lipid peroxidation, were significantly increased after 24 hr exposures to 5 mg/L CdCl2 only in the more CdCl2-sensitive species G. lacustris and E. cyaneus. Upon treatment with 0.54 to 5.8 mg/L CdCl2 for 1, 6 and 24 hrs, hsp70 transcript levels were generally more increased after the longer exposure times and in the more CdCl2-sensitive species. Relating the CdCl2 exposure concentrations to LCx values revealed that across the species the increases of hsp70 transcript levels were comparatively low (up to 2.6-fold) at CdCl2 concentrations ≤LC50. Relative hsp70 transcript levels were maximally increased in E. cyaneus by 5 mg/L CdCl2 ($\hat {=}$LC70) at 24 hrs (9.1-fold increase above the respective control). When G. lacustris was exposed to 5 mg/L CdCl2 ($\hat {=}$LC90) for 24 hrs, the increase in hsp70 was in comparison to E. cyaneus considerably less pronounced (3.0-fold increase in hsp70 levels relative to control). Upon exposure of amphipods to 5 mg/L CdCl2, increases in Hsp70 protein levels compared to untreated controls were highest in E. cyaneus at 1 and 6 hrs (5 mg/L CdCl2 $\hat {=}$ LC70) and in E. verrucosus at 24 hrs (5 mg/L CdCl2 $\hat {=}$ LC45). Thus, when the fold increases in Hsp70 protein levels in the different amphipod species were related to the respective species-specific LCx values a similar bell-shaped trend as for hsp70 transcript levels was seen across the species. Transcript levels of abcb1 in CdCl2exposed individuals of the different amphipod species varied up to 4.7-fold in relation to the respective controls. In contrast to hsp70/Hsp70, abcb1 transcripts in CdCl2 exposed individuals of the different amphipod species did not indicate similar levels of induction of abcb1 at equal LCx levels across the species. Induction of hsp70 and abcb1 genes and Hsp70 proteins by CdCl2 in the lethal concentration range shows that these cellular responses are rather insensitive to CdCl2 stress in the examined amphipod species. Furthermore, the increase of expression of these cellular defense systems at such high stress levels suggests that induction of these genes is not related to the maintenance of normal metabolism but to mitigation of the effects of severe toxic stress.

THE EFFECT OF 5-AIQ ON THE LIVER ISCHAEMIA/REPERFUSION INJURY

Shock ◽  
2002 ◽  
Vol 18 (Supplement) ◽  
pp. 23
Author(s):  
B. Sepodes ◽  
M. C. McDonald ◽  
R. Pinto ◽  
R. Maio ◽  
M. Caneira-da-Silva ◽  
...  
Keyword(s):  
Reperfusion Injury ◽  
Ischaemia Reperfusion Injury ◽  
Ischaemia Reperfusion ◽  
Liver Ischaemia

Expression of bcl-2 and bax in regenerating rat renal tubules following ischemic injury

1997 ◽  
Vol 272 (5) ◽  
pp. F640-F647 ◽  
Author(s):  
D. P. Basile ◽  
H. Liapis ◽  
M. R. Hammerman
Keyword(s):  
Proximal Tubule ◽  
Ischemic Injury ◽  
Fold Increase ◽  
Renal Tubules ◽  
Proximal Tubule Cells ◽  
Protein Levels ◽  
Bax Protein ◽  
Adult Kidney ◽  
Predictable Pattern

To define potential roles for bcl-2 and bax in adult kidney as regulators of regeneration, their expressions were characterized postischemic injury. A 2.1-fold increase in levels of renal bcl-2 mRNA occurred within 24 h of injury relative to levels in kidney of sham-operated control rats. The levels of bcl-2 mRNA remained elevated for 3 days but returned to baseline by day 5 postischemia. In situ hybridization of kidneys from sham-operated rats demonstrated faint expression of bcl-2 mRNA localized diffusely throughout the nephron. After renal injury, the expression of bcl-2 mRNA was markedly enhanced in regenerating proximal tubule cells relining the basement membrane. Immunohistochemistry showed a similar localization for bcl-2 protein. Levels of bax mRNA in kidney were elevated beginning at 24 h postischemia and remained elevated for 7 days postinjury. Bax mRNA and bax protein were colocalized to regenerating proximal tubules postischemia and were prominently expressed in papillary proliferations. We conclude that the expressions of bcl-2 and bax in kidney are enhanced in a predictable pattern following acute ischemic injury. Our findings suggest that these regulators of apoptosis play key roles in the process of repair of the damaged proximal tubule postischemia.

scholarly journals The Protective Effect of Zinc Against Liver Ischaemia Reperfusion Injury in a Rat Model of Global Ischaemia

2020 ◽  
Vol 10 (3) ◽  
pp. 228-235 ◽  
Author(s):  
Ernest Cheung ◽  
Mehrdad Nikfarjam ◽  
Louise Jackett ◽  
Damien M. Bolton ◽  
Joseph Ischia ◽  
...  
Keyword(s):  
Protective Effect ◽  
Reperfusion Injury ◽  
Rat Model ◽  
Ischaemia Reperfusion Injury ◽  
Global Ischaemia ◽  
Ischaemia Reperfusion ◽  
Liver Ischaemia

Liver Ischaemia-Reperfusion Injury

2020 ◽  
pp. 129-141
Author(s):  
Farid Froghi ◽  
Saied Froghi ◽  
Brian R. Davidson
Keyword(s):  
Reperfusion Injury ◽  
Ischaemia Reperfusion Injury ◽  
Ischaemia Reperfusion ◽  
Liver Ischaemia
Sign in / Sign up

Export Citation Format

Share Document