Receptor-mediated uptake of homologous low-density lipoproteins by isolated liver parenchymal cells of fetal rats

1988 ◽  
Vol 254 (1) ◽  
Author(s):  
U. D�rer ◽  
M. Sommer ◽  
H. Franke ◽  
B. Schlag ◽  
R. Dargel
Keyword(s):  
Low Density Lipoproteins ◽  
Low Density ◽  
Liver Parenchymal ◽  
Fetal Rats ◽  
Parenchymal Cells ◽  
Isolated Liver

Cholesteryl esters from oxidized low-density lipoproteins arein vivo rapidly hydrolyzed in rat kupffer cells and transported to liver parenchymal cells and bile

Hepatology ◽  
1994 ◽  
Vol 19 (6) ◽  
pp. 1459-1467
Author(s):  
Moniek N. Pieters ◽  
Sebastiaan Esbach ◽  
Donald Schouten ◽  
Adriaan Brouwer ◽  
Dick L. Knook ◽  
...  
Keyword(s):  
Kupffer Cells ◽  
Low Density Lipoproteins ◽  
Low Density ◽  
Cholesteryl Esters ◽  
Liver Parenchymal ◽  
Oxidized Low Density Lipoproteins ◽  
Parenchymal Cells

scholarly journals No major thermogenic role for (Na+ + K+)-dependent adenosine triphosphatase apparent in hepatocytes from hyperthyroid rats

1982 ◽  
Vol 202 (3) ◽  
pp. 661-665 ◽  
Author(s):  
D G Clark ◽  
M Brinkman ◽  
O H Filsell ◽  
S J Lewis ◽  
M N Berry
Keyword(s):  
Oxygen Consumption ◽  
Oxygen Uptake ◽  
Atpase Activity ◽  
Heat Production ◽  
Adenosine Triphosphatase ◽  
Heat Output ◽  
Liver Parenchymal ◽  
Dependent Atpase ◽  
Parenchymal Cells ◽  
Isolated Liver

(Na+ + K+)-dependent ATPase activity, heat production and oxygen consumption were increased by 59%, 62% and 75% respectively in hepatocytes from tri-iodothyronine-treated rats. Ouabain at concentrations of 1 and 10 mM decreased oxygen uptake by 2-8% in hepatocytes from euthyroid rats and by 5-15% in hepatocytes from hyperthyroid animals. Heat output was decreased by 4-9% with the glycoside in isolated liver parenchymal cells from the control animals and by 11% in the cells from the tri-iodothyronine-treated animals. These results do not support the hypothesis that hepatic (Na+ + K+)-ATPase plays a major role in increased heat production in hepatocytes from hyperthyroid rats.

Regulation of pyruvate kinase by 6-phosphogluconate in isolated hepatocytes

1981 ◽  
Vol 240 (3) ◽  
pp. E279-E285
Author(s):  
S. B. Smith ◽  
R. A. Freedland
Keyword(s):  
Pyruvate Kinase ◽  
Parenchymal Cell ◽  
Isolated Hepatocytes ◽  
Hill Coefficient ◽  
Liver Parenchymal Cell ◽  
Liver Parenchymal ◽  
Highly Correlated ◽  
Parenchymal Cells ◽  
The Hill ◽  
Isolated Liver

Isolated liver parenchymal cells from rats fed a 65% sucrose diet for 14 days were incubated in the presence and absence of 10(-6) M glucagon. The pyruvate kinase obtained from homogenates of the glucagon-treated cells displayed and increased Ks 0.5 for phosphoenolpyruvate (P-enolpyruvate), as well as an increased Ka 0.5 for 6-phosphogluconate (6-P-gluconate), compared to pyruvate kinase from untreated cells. Additionally, glucagon treatment decreased the maximal stimulation of pyruvate kinase by 6-P-gluconate by approximately two-thirds and decreased the Hill coefficient value of pyruvate kinase for 6-P-gluconate from 1.76 to 1.56. 6-Aminonicotinamide, an inhibitor of 6-P-gluconate dehydrogenase, increased 6-P-gluconate levels in isolated liver parenchymal cells three- to sevenfold, depending on the substrates present. The flux of P-enolpyruvate through pyruvate kinase was increased from 18 to 40% in these preparations and was highly correlated with the increase in 6-P-gluconate levels. The results suggest that 6-P-gluconate could regulate pyruvate kinase activity in the intact liver parenchymal cell. Furthermore, the activator would be of greatest importance in the lipogenic animal.

HORMONE SENSITIVITY OF ISOLATED LIVER PARENCHYMAL CELLS

1974 ◽  
Vol 77 (1_Suppl) ◽  
pp. S98 ◽  
Author(s):  
H. Bojar ◽  
K. Balzer ◽  
M. Stannek ◽  
W. Reipen ◽  
W. Staib
Keyword(s):  
Liver Parenchymal ◽  
Hormone Sensitivity ◽  
Parenchymal Cells ◽  
Isolated Liver

scholarly journals Low-density-lipoprotein receptors in different rabbit liver cells

1989 ◽  
Vol 261 (2) ◽  
pp. 587-593 ◽  
Author(s):  
M S Nenseter ◽  
O Myklebost ◽  
R Blomhoff ◽  
C A Drevon ◽  
A Nilsson ◽  
...  
Keyword(s):  
Kupffer Cells ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Binding Activity ◽  
Rabbit Liver ◽  
Low Density ◽  
Apo B ◽  
Liver Parenchymal ◽  
Ldl Binding ◽  
Parenchymal Cells

Receptor-dependent uptake mechanisms for low-density lipoprotein (LDL) were studied in rabbit liver parenchymal and non-parenchymal cells. Hybridization studies with a cDNA probe revealed that mRNA for the apo (apolipoprotein) B,E receptor was present in endothelial and Kupffer cells as well as in parenchymal cells. By ligand-blotting experiments we showed that apo B,E-receptor protein was present in both parenchymal and non-parenchymal cells. Studies of binding of homologous LDL in cultured rabbit parenchymal cells suggested that about 63% of the specific LDL binding was mediated via the apo B,E receptor. Approx. 47% of the specific LDL binding was dependent on Ca2+, suggesting that specific Ca2+-dependent as well as Ca2+-independent LDL-binding sites exist in liver parenchymal cells. Methylated LDL bound to the parenchymal cells in a saturable manner. Taken together, our results showed that apo B,E receptors are present in rabbit liver endothelial and Kupffer cells as well as in the parenchymal cells, and that an additional saturable binding activity for LDL may exist on rabbit liver parenchymal cells. This binding activity was not inhibited by EGTA or reductive methylation of lysine residues in apo B. LDL degradation in parenchymal cells was mainly mediated via the apo B,E receptor.

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