Effect of purified rat and hamster hepatic glutathione S-transferases on the microsome mediated binding of aflatoxin B1 to DNA

1986 ◽  
Vol 33 (1) ◽  
pp. 1-9 ◽  
Author(s):  
H.G. Raj ◽  
H.R. Prasanna ◽  
P.N. Magee ◽  
P.D. Lotlikar
Keyword(s):  
Aflatoxin B1 ◽  
Hepatic Glutathione ◽  
Glutathione S Transferases

scholarly journals The Mechanism Underlying the Extreme Sensitivity of Duck to Aflatoxin B1

2021 ◽  
Vol 2021 ◽  
pp. 1-8
Author(s):  
Kuntan Wu ◽  
Minjie Liu ◽  
Huanbin Wang ◽  
Shahid Ali Rajput ◽  
Yajing Shan ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Aflatoxin B1 ◽  
High Sensitivity ◽  
Metabolic Activation ◽  
Cytochrome P450s ◽  
Economic Losses ◽  
Metabolic Detoxification ◽  
Glutathione S Transferases ◽  
Extreme Sensitivity ◽  
Mutual Conversion

Most metabolites of aflatoxin B1 (AFB1), especially exo-AFB1-8,9-epoxide (AFBO), can induce the production of reactive oxygen species (ROS) to vary degrees, causing oxidative stress and liver damage, and ultimately induce liver cancer in humans and animals. Duck is one of the most sensitive animals to AFB1, and severe economic losses are caused by duck AFB1 poisoning every year, but the exact mechanism of this high sensitivity is still unclear. This review highlights significant advances in our understanding of the AFB1 metabolic activation, like cytochrome P450s (CYPs), and AFB1 metabolic detoxification, like glutathione S-transferases (GSTs) in poultry. In addition, AFB1 may have other metabolic pathways in poultry, such as the mutual conversion of AFB1 and aflatoxicol (AFL) and the process of AFBO to produce AFB1-8,9-dihydrodiol (AFB1-dhd) and further metabolize it into detoxification substances. This review also summarized some exogenous regulatory substances that can alleviate AFB1-induced oxidative stress.

scholarly journals Drug induction of hepatic glutathione S-transferases in male and female rats*

1975 ◽  
Vol 146 (2) ◽  
pp. 351-356 ◽  
Author(s):  
N Kaplowitz ◽  
J Kuhlekamp ◽  
G Clifton
Keyword(s):  
Female Rats ◽  
Metabolizing Enzymes ◽  
Male And Female ◽  
Male And Female Rats ◽  
Hepatic Glutathione ◽  
Drug Induction ◽  
Glutathione S Transferases ◽  
Proportional Increase ◽  
Males And Females ◽  
Specific Activities

The induction of the glutathione S-transferases by phenobarbital and polycyclic hydrocarbons was studied in male and female rats. Administration of phenobarbital resulted in 60-80% increase in S-aryl and S-aralkyl enzyme specific activities, whereas the S-epoxide and S-alkyl activities were increased by 30-40%. In following the sequence of induction, the former two activities were noted to reach peak activities before an increase in the latter two activities was observed. Both 3-methylcholanthrene and 3,4-benzopyrene were shown toi nduce these four enzymic activities, although without the discrimination between pairs of activities noted with phenobarbital. No change in Km accompanied the increase in Vmax. after induction by drugs, and no change occurred in Ki for sulphobromophthalein inhibition. Significantly lower enzyme specific activities were found for three of the activities studied in female rats but no difference was observed in the S-alkyltransferase activity. However, the proportional increase in the enzymic activities in response to phenobarbital was the same in males and females. These studies demonstrate the drug induction of a group of cytosolic drug-metabolizing enzymes as well as the identification of sex differences in these activities.

scholarly journals Alpha-Class Glutathione S-Transferases in Wild Turkeys (Meleagris gallopavo): Characterization and Role in Resistance to the Carcinogenic Mycotoxin Aflatoxin B1

PLoS ONE ◽  
2013 ◽  
Vol 8 (4) ◽  
pp. e60662 ◽  
Author(s):  
Ji Eun Kim ◽  
Brett R. Bunderson ◽  
Amanda Croasdell ◽  
Kent M. Reed ◽  
Roger A. Coulombe
Keyword(s):  
Aflatoxin B1 ◽  
Meleagris Gallopavo ◽  
Glutathione S Transferases ◽  
Wild Turkeys

scholarly journals Characterization of hepatic glutathione S-transferases in coho salmon (Oncorhynchus kisutch)

2007 ◽  
Vol 81 (2) ◽  
pp. 126-136 ◽  
Author(s):  
M TRUTE ◽  
B GALLIS ◽  
C DONEANU ◽  
S SHAFFER ◽  
D GOODLETT ◽  
...  
Keyword(s):  
Coho Salmon ◽  
Oncorhynchus Kisutch ◽  
Hepatic Glutathione ◽  
Glutathione S Transferases

scholarly journals Purification and characterization of hepatic glutathione S-transferases of rhesus monkeys. A family of enzymes similar to the human hepatic glutathione S-transferases

1988 ◽  
Vol 251 (1) ◽  
pp. 81-88 ◽  
Author(s):  
R M Hoesch ◽  
T D Boyer
Keyword(s):  
Peroxidase Activity ◽  
Rhesus Monkeys ◽  
Affinity Column ◽  
Terminal Sequence ◽  
Glutathione S Transferase ◽  
Substrate Specificities ◽  
High Affinity ◽  
Human Enzyme ◽  
Hepatic Glutathione ◽  
Glutathione S Transferases

Thirteen forms of glutathione S-transferase were purified from the livers of female rhesus monkeys (Macaque mulatta). Most (74.7%) of the activity in the hepatic cytosol adhered well to the GSH affinity column and could be eluted only with the addition of GSH to the eluting buffer. The predominant isoenzymes (n = 5) in this ‘high-affinity’ fraction had alkaline pI values (greater than 9.0) and contained a subunit with an Mr value of 24,000. All of these isoenzymes had high organic peroxidase activity and, on the basis of amino acid analysis, substrate specificities and affinity for non-substrate ligands, appear to belong to the family of glutathione S-transferases that have been termed alpha [Mannervik, Alin, Guthenberg, Jensson, Tahir, Warholm & Jörnvall (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 7202-7206]. Also within the high-affinity fraction was an isoenzyme with an acidic (5.8) pI value. This acidic isoenzyme was composed of a unique subunit (Mr 23,000). The N-terminal sequence (ten residues) of this acidic enzyme was identical with that of a human form that is referred to as pi. The predominant form of enzyme in the ‘low-affinity’ (eluted from the GSH affinity column with an increase in buffer pH) fraction was a homodimer of a 26,000-Mr subunit. It had an alkaline pI (greater than 9.0) but it lacked organic peroxidase activity. The N-terminal sequence (ten residues) of this enzyme was identical with that of a human enzyme referred to as mu. The substrate specificities and affinity for non-substrate ligands of this monkey enzyme also were similar to those of the human enzyme. In conclusion, the liver cytosol of rhesus monkeys contains a number of glutathione S-transferase isoenzymes that are very similar to the human hepatic enzymes.

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