(S)-Preferential detoxification of 4-hydroxy-2(E)-nonenal enantiomers by hepatic glutathione S-transferase isoforms in guinea-pigs and rats

2001 ◽  
Vol 355 (1) ◽  
pp. 237-244 ◽  
Author(s):  
Akira HIRATSUKA ◽  
Kouichi TOBITA ◽  
Hiroshi SAITO ◽  
Yasuhiro SAKAMOTO ◽  
Hiroaki NAKANO ◽  
...  
Keyword(s):  
Guinea Pig ◽  
Guinea Pigs ◽  
High Catalytic Activity ◽  
Glutathione S Transferase ◽  
Pig Liver ◽  
Liver Cytosol ◽  
Glutathione S Transferases ◽  
Human Livers ◽  
A Minor ◽  
Guinea Pig Liver

In guinea-pig liver cytosol, racemic 4-hydroxy-2(E)-nonenal (HNE), a reactive and highly toxic product released from biomembranes by lipid peroxidation, was detoxified (S)-preferentially by GSH conjugation mediated by glutathione S-transferases (GSTs) and (R)-preferentially by NAD+-dependent oxidation mediated by aldehyde dehydrogenase (ALDH). The GST-mediated detoxification of the HNE enantiomers proceeded at much higher rates than that mediated by ALDH in guinea-pig liver cytosol. All the major guinea-pig GSTs, A1-1, M1-1, M1-2 and M1-3*, isolated from guinea-pig liver cytosol also catalysed the (S)-preferential conjugation of the HNE enantiomers. The liver and other major tissues of guinea-pigs had no immunologically detectable level of a putative GSTA4-4 orthologue, which exists as a minor GST protein in rat, mouse and human livers and exhibits extremely high catalytic activity towards HNE. All the hepatic rat GSTs, A1-1(2), A1-3, A4-4, M1-1, M1-2 and M2-2, also catalysed the (S)-preferential conjugation of HNE enantiomers.

Glutathione peroxidase II of guinea pig liver cytosol: Relationship to glutathione S-transferases

1980 ◽  
Vol 205 (1) ◽  
pp. 122-131 ◽  
Author(s):  
Carl Irwin ◽  
Judy K. O'Brien ◽  
Peter Chu ◽  
Janis K. Townsend-Parchman ◽  
Pat O'Hara ◽  
...  
Keyword(s):  
Glutathione Peroxidase ◽  
Guinea Pig ◽  
Pig Liver ◽  
Liver Cytosol ◽  
Glutathione S Transferases ◽  
Guinea Pig Liver ◽  
Glutathione Peroxidase Ii

Glucocorticoid receptors in the guinea pig

1978 ◽  
Vol 235 (3) ◽  
pp. R115-R120 ◽  
Author(s):  
A. J. Hodgson ◽  
J. W. Funder
Keyword(s):  
Guinea Pig ◽  
Inhibitory Activity ◽  
Guinea Pigs ◽  
Glucocorticoid Receptors ◽  
Metabolizing Enzymes ◽  
Pig Liver ◽  
Liver And Kidney ◽  
Guinea Pig Liver

In cytoplasmic fractions of liver and kidney prepared from adrenalectomized guinea pigs, tritiated dexamethasone ([3H]DM) is bound with a very low affinity (Kd 4 degrees C greater than or equal to 2 X 10(-7) M). By competition studies, the specificity of this binding was shown to be comparable with that for [3H]DM binding to glucocorticoid receptors in other species. In addition, cytoplasmic preparations from guinea pig liver and kidney appear to inhibit the binding of [3H]DM to rat glucocorticoid receptors under a variety of experimentally determined circumstances. It is proposed that such inhibitory activity may reflect a system of [3H]DM sequestration, perhaps by metabolizing enzymes with a high combining power for glucocorticoids. Both low affinity glucocorticoid receptors and avid binding to sites of metabolism may represent additive cellular bases for the apparent corticoresistance of the guinea pig.

scholarly journals Guinea-pig liver tryptophan pyrrolase. Absence of detectable apoenzyme activity and of hormonal induction by cortisol and possible regulation by tryptophan

1974 ◽  
Vol 138 (3) ◽  
pp. 445-451 ◽  
Author(s):  
Abdulla A.-B. Badawy ◽  
Myrddin Evans
Keyword(s):  
Guinea Pig ◽  
Liver Enzyme ◽  
Guinea Pigs ◽  
Actinomycin D ◽  
The Other ◽  
Pig Liver ◽  
Latent Form ◽  
Tryptophan Pyrrolase ◽  
Guinea Pig Liver

1. When assayed in fresh homogenates, guinea-pig liver tryptophan pyrrolase exists only as holoenzyme. It does not respond to agents that activate or inhibit the rat liver enzyme in vitro. Only by aging (for 30min at 5°C) does the guinea-pig enzyme develop a requirement for ascorbate. 2. The guinea-pig liver enzyme is activated by the administration of tryptophan but not cortisol, salicylate, ethanol or 5-aminolaevulinate. 3. The tryptophan enhancement of the guinea-pig liver pyrrolase activity is prevented by 0, 34 and 86% by pretreatment with actinomycin D, cycloheximide or allopurinol respectively. 4. The guinea-pig liver tryptophan pyrrolase is more sensitive to tryptophan administration than is the rat enzyme. On the other hand, the concentrations of tryptophan in sera and livers of guinea pigs are 45–52% less than those in rats. 5. It is suggested that tryptophan may regulate the activity of guinea-pig liver tryptophan pyrrolase by mobilizing a latent form of the enzyme whose primary function is the detoxication of its substrate.

SOME PROPERTIES OF APOFERRITIN ISOLATED FROM GUINEA PIG LIVER

1962 ◽  
Vol 40 (1) ◽  
pp. 983-987 ◽  
Author(s):  
Felix Friedberg
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Guinea Pig ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Guinea Pigs ◽  
Dicarboxylic Acids ◽  
Acetate Buffer ◽  
Pig Liver ◽  
Guinea Pig Liver

Apoferritin isolated from livers of guinea pigs and characterized by a s°w,20 of 17.7 and a pI of 4.8 (in acetate buffer Γ/2 0.1) was hydrolyzed with 5.7 N HCl for 22 and 44 hours and its amino acid composition determined. The protein appears rich in dicarboxylic acids and in leucine. The content of sulphur-containing amino acids is fairly small.

Expression and translation of the growth hormone-receptor gene in the guinea-pig

1992 ◽  
Vol 133 (3) ◽  
pp. 357-362 ◽  
Author(s):  
S. Harvey ◽  
R. A. Fraser
Keyword(s):  
Guinea Pig ◽  
Guinea Pigs ◽  
Plasma Membranes ◽  
Growth Hormone Receptor ◽  
Receptor Gene ◽  
Pig Liver ◽  
Gh Receptor ◽  
Growth Hormone Receptor Gene ◽  
Guinea Pig Liver ◽  
Gh Receptors

ABSTRACT The refractoriness of guinea-pigs to the growth-promoting actions of exogenous GH has been suggested to be due to a deficiency or defect in tissue GH receptors or in GH-receptor gene expression. GH-receptor mRNA was, however, demonstrated by Northern blot analysis and by the polymerase chain reaction in extracts of guinea-pig liver, adipose tissue, brain, hypothalamus and pituitary gland. High-affinity, low-capacity binding sites for radio-labelled ovine GH were also demonstrated on the plasma membranes of guinea-pig liver and were similar to those in rat liver. These results demonstrate that the unresponsiveness of guinea-pigs to exogenous GH is not due to the absence of GH receptors. Journal of Endocrinology (1992) 133, 357–362

scholarly journals Guinea-pig liver testosterone 17 β-dehydrogenase (NADP+) and aldehyde reductase exhibit benzene dihydrodiol dehydrogenase activity

1985 ◽  
Vol 225 (1) ◽  
pp. 177-181 ◽  
Author(s):  
A Hara ◽  
M Hayashibara ◽  
T Nakayama ◽  
K Hasebe ◽  
S Usui ◽  
...  
Keyword(s):  
Guinea Pig ◽  
Dehydrogenase Activity ◽  
Aldehyde Reductase ◽  
Pig Liver ◽  
Liver Cytosol ◽  
Dihydrodiol Dehydrogenase ◽  
Guinea Pig Liver ◽  
Oxidation Of Benzene

We have kinetically and immunologically demonstrated that testosterone 17 beta-dehydrogenase (NADP+) isoenzymes (EC 1.1.1.64) and aldehyde reductase (EC 1.1.1.2) from guinea-pig liver catalyse the oxidation of benzene dihydrodiol (trans-1,2-dihydroxycyclohexa-3,5-diene) to catechol. One isoenzyme of testosterone 17 beta-dehydrogenase, which has specificity for 5 beta-androstanes, oxidized benzene dihydrodiol at a 3-fold higher rate than 5 beta-dihydrotestosterone, and showed a more than 4-fold higher affinity for benzene dihydrodiol and Vmax. value than did another isoenzyme, which exhibits specificity for 5 alpha-androstanes, and aldehyde reductase. Immunoprecipitation of guinea-pig liver cytosol with antisera against the testosterone 17 beta-dehydrogenase isoenzymes and aldehyde reductase indicated that most of the benzene dihydrodiol dehydrogenase activity in the tissue is due to testosterone 17 beta-dehydrogenase.

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