scholarly journals Selective uptake of cadmium by the parenchyumal cells of liver

1980 ◽  
Vol 188 (1) ◽  
pp. 285-288 ◽  
Author(s):  
K Cain ◽  
D N Skilleter
Keyword(s):  
Cell Separation ◽  
Separation Technique ◽  
Cadmium Uptake ◽  
Selective Uptake ◽  
Sinusoidal Cells ◽  
Liver Parenchymal ◽  
A Cell ◽  
Parenchymal Cells ◽  
Uptake And Metabolism

The uptake of cadmium in vivo into parenchymal and non-parenchymal (sinusoidal) cells of the liver was studied by a cell-separation technique. Liver parenchymal cells accumulate cadmium more readily than do non-parenchymal cells and synthesize metallothionein. It is proposed that cadmium uptake and metabolism from injected CdCl2, is restricted almost exclusively to the liver parenchymal cells.

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.

Differential abilities of mouse liver parenchymal and nonparenchymal cells in HDL and LDL (native and oxidized) association and cholesterol efflux

2006 ◽  
Vol 84 (2) ◽  
pp. 250-256 ◽  
Author(s):  
Jany Lapointe ◽  
To Quyen Truong ◽  
Louise Falstrault ◽  
Louise Brissette
Keyword(s):  
Mouse Liver ◽  
Cholesterol Efflux ◽  
Oxidized Ldl ◽  
Density Lipoprotein ◽  
Selective Uptake ◽  
Liver Parenchymal ◽  
Nonparenchymal Cells ◽  
Uptake Activity ◽  
Iodine 125 ◽  
Parenchymal Cells

The aim of this study was to quantify the abilities of mouse liver parenchymal and nonparenchymal cells with respect to (i) cholesteryl ester (CE) selective uptake from low-density lipoproteins (LDL), oxidized LDL (OxLDL), and high-density lipoprotein (HDL); and (ii) their free cholesterol efflux to HDL. The preparations of cells were incubated with lipoproteins labelled either in protein with iodine-125 or in CE with 3H-cholesterol oleate, and lipoprotein-protein and lipoprotein-CE associations were measured. The associations of LDL-protein and LDL-CE with nonparenchymal cells were 5- and 2-fold greater, respectively, than with parenchymal cells. However, in terms of CE-selective uptake (CE association minus protein association) both types of cell were equivalent. Similar results were obtained with OxLDL, but both types of cell showed higher abilities in OxLDL-CE than in LDL-CE selective uptake (on average by 3.4-fold). The association of HDL-protein with nonparenchymal cells was 3× that with parenchymal cells; however, nonparenchymal cells associated 45% less HDL-CE. Contrary to parenchymal cells, nonparenchymal cells did not show HDL-CE selective uptake activity. Thus parenchymal cells selectively take CE from the 3 types of lipoproteins, whereas nonparenchymal cells exert this function only on LDL and OxLDL. Efflux was 3.5-fold more important in nonparenchymal than in parenchymal cells.Key words: LDL, HDL, parenchymal, SR-BI, CD36, selective uptake, cholesterol.

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 Uptake of Chylomicron Lipid by Rat Liver Parenchymal Cells in vivo

Nature ◽  
1967 ◽  
Vol 215 (5096) ◽  
pp. 83-83 ◽  
Author(s):  
JOAN A. HIGGINS ◽  
C. GREEN
Keyword(s):  
Rat Liver ◽  
Liver Parenchymal ◽  
Parenchymal Cells

scholarly journals Inhibition by cycloheximide of degradation of cytochrome P-450 in primary cultures of adult rat liver parenchymal cells and in vivo

1979 ◽  
Vol 180 (3) ◽  
pp. 621-630 ◽  
Author(s):  
Philip S. Guzelian ◽  
Joyce L. Barwick
Keyword(s):  
Cell Culture ◽  
Protein Synthesis ◽  
Total Protein ◽  
Cultured Cells ◽  
Liver Parenchymal ◽  
Adult Rat ◽  
Haem Oxygenase ◽  
Parenchymal Cells ◽  
Cytochrome P 450

Degradation of cytochrome P-450 was studied in adult rat liver parenchymal cells in primary monolayer culture. In cells incubated in standard culture medium, the amount of cytochrome P-450 decreased at an accelerated rate relative to either the rate of degradation of total protein in the cells or the turnover of cytochrome P-450 in vivo. This change was succeeded by a spontaneous increase in the activity of haem oxygenase, an enzyme system that converts haem into bilirubin in vitro, measured in extracts from the cultured cells. This finding suggests that the rate of cytochrome P-450 breakdown may be controlled by factor(s) other than the activity of haem oxygenase. The decline in cytochrome P-450 and the subsequent increase in haem oxygenase activity was prevented by incubation of hepatocytes in medium containing an inhibitor of protein synthesis such as cycloheximide, puromycin, actinomycin D, or azaserine. The effect of cycloheximide appeared to be due to decreased breakdown of microsomal 14C-labelled haem. By contrast, cycloheximide was without effect on the degradation of total protein, measured either in homogenates or in microsomal fractions prepared from the cultured cells. These results suggest that the conditions of cell culture stimulate selective degradation of cytochrome P-450 by a process that is inhibited by cycloheximide and hence may require protein synthesis. The findings in culture were verified in parallel studies of cytochrome P-450 degradation in vivo. After administration of bromobenzene, the degradation of the haem moiety of cytochrome P-450 was accelerated in vivo in a manner resembling that observed in cultured hepatocytes. Administration of cycloheximide to either bromobenzene-treated rats or to untreated rats decreased the degradation of the haem moiety of cytochrome P-450. However, the drug failed to affect degradation of haem not associated with cytochrome P-450, suggesting that cycloheximide is not a general inhibitor of haem oxidation in the liver. These findings confirm that the catabolism of hepatic cytochrome P-450 haem is controlled by similar cycloheximide-sensitive processes in the basal steady state in vivo, as stimulated by bromobenzene in vivo, or in hepatocytes under the conditions of cell culture. We conclude that the rate-limiting step in this process appears to require protein synthesis and precedes cleavage of the haem ring.

scholarly journals Human recombinant apolipoprotein E redirects lipopolysaccharide from Kupffer cells to liver parenchymal cells in rats In vivo.

1997 ◽  
Vol 99 (10) ◽  
pp. 2438-2445 ◽  
Author(s):  
P C Rensen ◽  
M Oosten ◽  
E Bilt ◽  
M Eck ◽  
J Kuiper ◽  
...  
Keyword(s):  
Apolipoprotein E ◽  
Kupffer Cells ◽  
Liver Parenchymal ◽  
Parenchymal Cells
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