scholarly journals Lack of inhibitory effects of the ju-myo protein on development of glutathione S-transferase placental form-positive foci in the male F344 rat liver.

1999 ◽  
Vol 24 (1) ◽  
pp. 27-31 ◽  
Author(s):  
Toshio ICHIHARA ◽  
Hideki WANIBUCHI ◽  
Chyi Chia R. LEE ◽  
Kazuhide NAKAJIMA ◽  
Yoshihisa YANO ◽  
...  
Keyword(s):  
Rat Liver ◽  
Inhibitory Effects ◽  
Glutathione S Transferase ◽  
F344 Rat

scholarly journals The nucleotide sequence of a rat liver glutathione S-transferase subunit cDNA clone.

1984 ◽  
Vol 259 (9) ◽  
pp. 5536-5542
Author(s):  
H C Lai ◽  
N Li ◽  
M J Weiss ◽  
C C Reddy ◽  
C P Tu
Keyword(s):  
Nucleotide Sequence ◽  
Rat Liver ◽  
Cdna Clone ◽  
Glutathione S Transferase ◽  
Liver Glutathione

Interaction of anions with rat liver arginase: specific inhibitory effects of fluoride

2002 ◽  
Vol 88 (3-4) ◽  
pp. 397-402 ◽  
Author(s):  
Stéphanie Pethe ◽  
Jean-Luc Boucher ◽  
Daniel Mansuy
Keyword(s):  
Rat Liver ◽  
Inhibitory Effects

scholarly journals The distribution, induction and isoenzyme profile of glutathione S-transferase and glutathione peroxidase in isolated rat liver parenchymal, Kupffer and endothelial cells

1989 ◽  
Vol 264 (3) ◽  
pp. 737-744 ◽  
Author(s):  
P Steinberg ◽  
H Schramm ◽  
L Schladt ◽  
L W Robertson ◽  
H Thomas ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Glutathione Peroxidase ◽  
Rat Liver ◽  
Peroxidase Activity ◽  
Cell Types ◽  
Transferase Activity ◽  
Glutathione Peroxidase Activity ◽  
Glutathione S Transferase ◽  
Liver Parenchymal ◽  
Parenchymal Cells

The distribution and inducibility of cytosolic glutathione S-transferase (EC 2.5.1.18) and glutathione peroxidase (EC 1.11.1.19) activities in rat liver parenchymal, Kupffer and endothelial cells were studied. In untreated rats glutathione S-transferase activity with 1-chloro-2,4-dinitrobenzene and 4-hydroxynon-2-trans-enal as substrates was 1.7-2.2-fold higher in parenchymal cells than in Kupffer and endothelial cells, whereas total, selenium-dependent and non-selenium-dependent glutathione peroxidase activities were similar in all three cell types. Glutathione S-transferase isoenzymes in parenchymal and non-parenchymal cells isolated from untreated rats were separated by chromatofocusing in an f.p.l.c. system: all glutathione S-transferase isoenzymes observed in the sinusoidal lining cells were also detected in the parenchymal cells, whereas Kupffer and endothelial cells lacked several glutathione S-transferase isoenzymes present in parenchymal cells. At 5 days after administration of Arocolor 1254 glutathione S-transferase activity was only enhanced in parenchymal cells; furthermore, selenium-dependent glutathione peroxidase activity decreased in parenchymal and non-parenchymal cells. At 13 days after a single injection of Aroclor 1254 a strong induction of glutathione S-transferase had taken place in all three cell types, whereas selenium-dependent glutathione peroxidase activity remained unchanged (endothelial cells) or was depressed (parenchymal and Kupffer cells). Hence these results clearly establish that glutathione S-transferase and glutathione peroxidase are differentially regulated in rat liver parenchymal as well as non-parenchymal cells. The presence of glutathione peroxidase and several glutathione S-transferase isoenzymes capable of detoxifying a variety of compounds in Kupffer and endothelial cells might be crucial to protect the liver from damage by potentially hepatotoxic substances.

EFFECTS OF HYPOGLYCIN A ON THE METABOLISM OF AMINO ACIDS BY LIVER SLICES

1964 ◽  
Vol 42 (1) ◽  
pp. 139-142 ◽  
Author(s):  
S. J. Patrick ◽  
L. C. Stewart
Keyword(s):  
Amino Acids ◽  
Fatty Acids ◽  
Fatty Acid ◽  
Glutamic Acid ◽  
Rat Liver ◽  
Inhibitory Effects ◽  
Liver Slices

The effects of hypoglycin A on the metabolism of L-leucine-C14, L-alanine-C14, and L-glutamic-acid-C14 by rat liver slices have been investigated. Hypoglycin exerted markedly inhibitory effects on the conversion of leucine-C14 to fatty acid, cholesterol, and CO2. Conversion of alanine-C14 and glutamic acid-C14 to fatty acids was also inhibited by hypoglycin. No effects of hypoglycin on the conversion of C14-amino acids into protein or glycogen were demonstrated.

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