Evidence for the presence of a cell-surface ribonuclease in mechanically prepared rat-liver cells in suspension

1982 ◽  
Vol 2 (10) ◽  
pp. 751-760 ◽  
Author(s):  
R. Sirdeshmukh ◽  
P. M. Bhargava
Keyword(s):  
Escherichia Coli ◽  
Cell Surface ◽  
Rat Liver ◽  
Degradation Products ◽  
Sucrose Density Gradient ◽  
Liver Parenchymal ◽  
Rat Liver Cells ◽  
A Cell ◽  
Parenchymal Cells ◽  
Soluble Material

Rat-liver parenchymal cells obtained in suspension by a mecahnical method are shown to contain a cell-surface nuclease(s) that rapidly degrades exogenously added total Escherichia coli RNA. However, no acid-soluble products are formed; all the degradation products in the incubation medium sediment in the 4–55 RNA region on a sucrose density gradient. A part of the degraded RNA seems to be taken up by the cells; the uptake of the degradation products, presumably derived from rRNAs, is more than that of purified 4–55 RNA. Most of the RNA taken up by the cell sediments in the 4–55 region; only a small proportion is degraded to acid-soluble material within the cell.

scholarly journals Comparison of cadmium-metallothionein synthesis in parenchymal and non-parenchymal rat liver cells

1983 ◽  
Vol 210 (3) ◽  
pp. 769-773 ◽  
Author(s):  
K Cain ◽  
D N Skilleter
Keyword(s):  
Rat Liver ◽  
Cell Separation ◽  
Metal Uptake ◽  
Time Course ◽  
Cell Types ◽  
Separation Technique ◽  
Limiting Factor ◽  
Rat Liver Cells ◽  
A Cell ◽  
Parenchymal Cells

The time course of cadmium-metallothionein synthesis was studied in non-parenchymal and parenchymal cells, isolated by a cell-separation technique from the livers of rats after the simultaneous injection of CdCl2 (0.05 mg of Cd/kg) and a 10-fold molar excess of 2,3-dimercaptopropanol. Under these conditions of dosing, in contrast with the injection of CdCl2 alone, both cell types accumulate similar concentrations of Cd and synthesize equivalent concentrations of metallothionein. It is concluded that both cell types have a similar capacity to synthesize the metalloprotein, and that the limiting factor under normal cadmium exposure is the relatively inefficient metal uptake into the non-parenchymal cells.

scholarly journals Characterization of retroendocytosis in rat liver parenchymal cells and sinusoidal endothelial cells

1992 ◽  
Vol 287 (1) ◽  
pp. 241-246 ◽  
Author(s):  
S Magnusson ◽  
I Faerevik ◽  
T Berg
Keyword(s):  
Endothelial Cells ◽  
Cell Surface ◽  
Rat Liver ◽  
Early Stage ◽  
Cell Types ◽  
Endocytic Pathway ◽  
Sinusoidal Endothelial Cells ◽  
Rat Liver Cells ◽  
Major Factors ◽  
Parenchymal Cells

After receptor-mediated endocytosis, internalized ligands may be recycled to the cell surface instead of being routed to lysosomes for degradation, a process termed retroendocytosis. We have investigated the kinetics and extent of retroendocytosis of neoglycoproteins after internalization via two carbohydrate-specific receptors in rat liver cells: galactose receptors in parenchymal cells (PC) and mannose receptors in sinusoidal endothelial cells (EC). Retroendocytosis in both cell types occurred with first-order kinetics, and the rate of recycling of internalized ligands was about 4 times higher in EC than in PC. As the length of the internalization pulse was increased, the extent of subsequent retroendocytosis decreased, indicating that retroendocytosis takes place from a relatively early stage in the endocytic pathway. Furthermore, as the degree of carbohydrate substitution of the neoglycoprotein ligands increased, the affinities of the receptors for the ligands and the extent of ligand retroendocytosis increased. In the EC, the relationship between degree of substitution and extent of retroendocytosis was not immediately apparent, as some of the neoglycoprotein ligands used may also bind to and be internalized by scavenger receptors on the EC, causing a decreased apparent retroendocytosis. However, when this interaction was inhibited, this relationship was restored. We conclude that retroendocytosis mainly occurs because of incomplete dissociation of ligands from receptors before receptor recycling to the cell surface and that the affinities of a receptor for its ligand at the cell surface and in the endosomal environment are major factors in determining the extent of retroendocytosis.

scholarly journals Induction of amino acid transport in primary cultures of adult rat liver parenchymal cells by insulin.

1976 ◽  
Vol 251 (10) ◽  
pp. 3014-3020 ◽  
Author(s):  
R F Kletzien ◽  
M W Pariza ◽  
J E Becker ◽  
V R Potter ◽  
F R Butcher
Keyword(s):  
Amino Acid ◽  
Rat Liver ◽  
Amino Acid Transport ◽  
Primary Cultures ◽  
Acid Transport ◽  
Liver Parenchymal ◽  
Adult Rat ◽  
Parenchymal Cells

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.

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