scholarly journals Phospholipase A2 of rat liver mitochondria in vitamin E deficiency

1978 ◽  
Vol 172 (2) ◽  
pp. 349-352 ◽  
Author(s):  
A. S. Pappu ◽  
P. Fatterpaker ◽  
A. Sreenivasan
Keyword(s):  
Enzyme Activity ◽  
Vitamin E ◽  
Phospholipase A2 ◽  
Rat Liver ◽  
Fold Increase ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Vitamin E Deficiency ◽  
Phospholipase A2 Activity

1. There is a more than 2-fold increase in phospholipase A2 activity (EC 3.1.1.4) of liver mitochondria isolated from vitamin E-deficient rats compared with that in normal rats. 2. α-Tocopherol in lipoprotein-bound form is more effective than free α-tocopherol in restoring the enzyme activity to normal.

Effects of Vitamin E Deficiency on GSH-lnduced Swelling of Rat Liver Mitochondria

1975 ◽  
Vol 148 (3) ◽  
pp. 929-932 ◽  
Author(s):  
S. O. Alozie ◽  
L. C. Ellis ◽  
R. M. Johnson ◽  
J. C. Street
Keyword(s):  
Vitamin E ◽  
Rat Liver ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Vitamin E Deficiency

[34] Phospholipase A2 from rat liver mitochondria

1991 ◽  
pp. 365-373 ◽  
Author(s):  
H. van den Bosch ◽  
J.G.N. de Jong ◽  
A.J. Aarsman
Keyword(s):  
Phospholipase A2 ◽  
Rat Liver ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria

scholarly journals The inhibition of pyruvate and ls(+)-isocitrate oxidation by succinate oxidation in rat liver mitochondria

1969 ◽  
Vol 114 (3) ◽  
pp. 589-596 ◽  
Author(s):  
T. König ◽  
D. G. Nicholls ◽  
P. B. Garland
Keyword(s):  
Cytochrome B ◽  
Rat Liver ◽  
Rat Heart ◽  
Fold Increase ◽  
Liver Mitochondria ◽  
Inhibitory Effect ◽  
The Other ◽  
Rat Liver Mitochondria ◽  
Succinate Oxidation ◽  
Rapid Flow

1. The effects of succinate oxidation on pyruvate and also isocitrate oxidation by rat liver mitochondria were studied. 2. Succinate oxidation was without effect on pyruvate and isocitrate oxidation when respiration was maximally activated with ADP. 3. When respiration was partially inhibited by atractylate, succinate oxidation severely inhibited the oxidation of pyruvate and isocitrate. 4. This inhibitory effect of succinate was associated with a two- to three-fold increase in the reduction of mitochondrial NAD+ but no change in the reduction of cytochrome b. 5. It is concluded that, in the partially energy-controlled state, respiration is more severely inhibited at the first phosphorylating site than at the other two. 6. The effects of succinate oxidation are compared with those of palmitoylcarnitine oxidation. It is concluded that a rapid flow of electrons directly into the respiratory chain at the level of cytochrome b is in itself inadequate to inhibit the oxidation of intramitochondrial NADH. 7. The effects of succinate oxidation on pyruvate oxidation were similar in rat heart and liver mitochondria.

scholarly journals Rat liver mitochondrial phospholipase A2 is an endotoxin-stimulated membrane-associated enzyme of Kupffer cells which is released during liver perfusion

1993 ◽  
Vol 293 (1) ◽  
pp. 143-150 ◽  
Author(s):  
G M Hatch ◽  
D E Vance ◽  
D C Wilton
Keyword(s):  
Enzyme Activity ◽  
Phospholipase A2 ◽  
Rat Liver ◽  
Kupffer Cells ◽  
Hepatic Lipase ◽  
Liver Perfusion ◽  
Elevated Serum ◽  
Physiological Saline ◽  
Group Ii ◽  
Phospholipase A2 Activity

A novel fluorescence assay for phospholipase A2 [Wilton (1990) Biochem. J. 266, 435-439] has been used to study the Group-II rat liver mitochondrial enzyme, and a number of novel properties of this enzyme were identified. (1) The enzyme activity was located in the liver macrophages (Kupffer cells) while negligible activity was associated with hepatocytes. (2) Although subcellular fractionation of whole liver confirmed the predominantly mitochondrial location of this enzyme activity, the analysis of the hepatocyte-free Kupffer-cell-enriched fraction revealed a different enzyme distribution, with the majority of activity being associated with the microsomal membrane fraction. (3) Bacterial endotoxin has been previously shown to be scavenged by Kupffer cells in rats. Treatment of rats with bacterial lipopolysaccharide (endotoxin) resulted in a dramatic time- and dose-dependent increase in liver phospholipase A2 activity. (4) It is known that injection of endotoxin into rodents results in elevated serum phospholipase A2 activity, while a similar phenomenon is seen in the condition of septic shock in man. The source of this serum enzyme was unknown. In this study perfusion of livers from rats pretreated with lipopolysaccharide with physiological saline demonstrated a 6-fold increase in phospholipase A2 activity in the perfusate compared with sham-treated controls, with only minor release of hepatic lipase. (5) Western-blot analysis confirmed an increased release of this Group-II phospholipase A2 into the perfusate of lipopolysaccharide-treated rats compared with sham-treated controls. These results suggest that liver Kupffer cells are a major source of the endotoxin-induced serum Group-II phospholipase A2 activity associated with bacterial infection and trauma.

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