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 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.

Tissue Plasminogen Activator is Endocytosed by Mannose and Galactose Receptors of Rat Liver Cells

1988 ◽  
Vol 59 (03) ◽  
pp. 480-484 ◽  
Author(s):  
Bård Smedsrød ◽  
Monica Einarsson ◽  
Håkan Pertoft
Keyword(s):  
Endothelial Cells ◽  
Plasminogen Activator ◽  
Tissue Plasminogen Activator ◽  
Rat Liver ◽  
Side Chains ◽  
Diisopropyl Fluorophosphate ◽  
Tissue Plasminogen ◽  
Rat Liver Cells ◽  
Liver Endothelial Cells ◽  
Parenchymal Cells

SummaryExperiments were carried out to charact erize the specificity of uptake of tPA in rat liver cells. Endocytosis in liver endothelial cells of the native carbohydrate variants of tissue plasminogen activator (tPA), and tPA inactivated by diisopropyl fluorophosphate was found to be competitive, suggesting that the determinant being recognized by these cells is different from the active site. Fibronectin and urokinase, which show partial homology with tPA, did not compete with tPA for uptake in liver endothelial cells. Hyaluronic acid, collagen, or IgG, which are endocytosed by specific receptors in liver endothelial cells, did not interfere with the uptake.Reduced endocytosis by liver endothelial cells was observed with tPA modified in the carbohydrate side chains, suggesting that these structures are important for uptake. Ovalbumin, mannan, mannose, fructose, and EDTA, but not galactose, effectively inhibited uptake in liver endothelial cells of both native and diisopropyl fluorophosphate-inhibited tPA, but had very little effect on the uptake of tPA modified in the carbohydrate side chains.Endocytosis of native tPA by parenchymal cells could be inhibited by galactose, ovalbumin, and EDTA, but not by mannose.These results suggest that endocytosis of tPA by liver endothelial cells and parenchymal cells is mediated by the mannose and galactose receptors, respectively.

scholarly journals Endocytosis of ricin by rat liver cells in vivo and in vitro is mainly mediated by mannose receptors on sinusoidal endothelial cells

1993 ◽  
Vol 291 (3) ◽  
pp. 749-755 ◽  
Author(s):  
S Magnússon ◽  
T Berg
Keyword(s):  
Endothelial Cells ◽  
Mannose Receptor ◽  
Cell Types ◽  
Plant Toxin ◽  
Sinusoidal Endothelial Cells ◽  
Liver Uptake ◽  
Parenchymal Cells ◽  
Mannose Receptors

Upon intravenous injection into rats, the plant toxin ricin was rapidly cleared from the circulation by the liver. Among the different liver cell populations, most of the injected ricin associated with the sinusoidal endothelial cells (EC), whereas the liver parenchymal cells (PC) and Kupffer cells (KC) yielded minor contributions to the total liver uptake in vivo. Co-injection of mannan strongly inhibited ricin uptake by the EC, showing that it was mediated by mannose receptors. On the other hand, co-injection of lactose, which inhibits the galactose-specific association of ricin with cells, enhanced ricin uptake by the EC. The carbohydrate-dependency of the EC contribution to the uptake of ricin in vivo was reflected in the carbohydrate-dependency of the uptake in vivo by whole liver. In vitro, the EC also endocytosed ricin more efficiently than did the PC or KC. Whereas uptake in vitro in the EC was mainly mannose-specific, uptake in the two other cell types was mainly galactose-specific. Western blotting showed that the mannose receptors of liver non-parenchymal cells are identical with the mannose receptor previously isolated from alveolar macrophages. The mannose receptors are expressed at a higher level in EC than in KC. Ligand blotting showed that, in the presence of lactose, the mannose receptor is the only protein in the EC that binds ricin, and the binding is mannose-specific and Ca(2+)-dependent.

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 The uptake and metabolism of chylomicron-remnant lipids by rat liver parenchymal and non-parenchymal cells in vitro

1985 ◽  
Vol 232 (2) ◽  
pp. 395-401 ◽  
Author(s):  
P M Lippiello ◽  
P J Sisson ◽  
M Waite
Keyword(s):  
Endothelial Cells ◽  
Rat Liver ◽  
Kupffer Cells ◽  
Liver Cell ◽  
Cholesterol Ester ◽  
Cell Types ◽  
Chylomicron Remnant ◽  
Parenchymal Cells ◽  
Uptake And Metabolism

The uptake and metabolism of chylomicron-remnant lipids by individual liver cell types was examined by incubating remnants with monolayer cultures of hepatocytes, Kupffer cells, and endothelial cells from rat liver. Remnants were prepared in vitro from radiolabelled mesenteric-lymph chylomicra, utilizing either purified lipoprotein lipase from bovine milk, or plasma isolated from heparinized rats. The resulting particles contained [3H]phosphatidylcholine and cholesterol, and [14C]oleate in the acylglycerol, phospholipid, fatty-acid and cholesterol-ester fractions. The capacities of the three cell types for uptake of both [3H]lipids and [14C]lipids were determined to be, on a per-cell basis, in the order: Kupffer greater than hepatocytes greater than endothelial. The relative proportions of [3H]phospholipid and total [3H]cholesterol taken up by hepatocytes and non-parenchymal cells remained constant with time. The uptake of [14C]oleoyl lipids by all three cell types was slightly greater than that of the total [3H]cholesterol and [3H]phospholipid components. There was evidence of cholesterol-ester hydrolysis and turnover of [14C]oleate in the phospholipid fraction in hepatocytes and Kupffer cells, but not endothelial cells, over the first 2 h. With both remnant preparations, these observations indicate that significant differences exist between the three major liver cell types with respect to the uptake and metabolism of remnant lipid components.

Involvement of signaling of VEGF and TGF-β in differentiation of sinusoidal endothelial cells during culture of fetal rat liver cells

2007 ◽  
Vol 329 (2) ◽  
pp. 273-282 ◽  
Author(s):  
Masayuki Yoshida ◽  
Yuji Nishikawa ◽  
Yasufumi Omori ◽  
Toshiaki Yoshioka ◽  
Takuo Tokairin ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Rat Liver ◽  
Liver Cells ◽  
Sinusoidal Endothelial Cells ◽  
Fetal Rat ◽  
Rat Liver Cells ◽  
Fetal Rat Liver

Release of osmolytes induced by phagocytosis and hormones in rat liver

2000 ◽  
Vol 278 (2) ◽  
pp. G227-G233 ◽  
Author(s):  
Matthias Wettstein ◽  
Thorsten Peters-Regehr ◽  
Ralf Kubitz ◽  
Richard Fischer ◽  
Claudia Holneicher ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Cell Volume ◽  
Rat Liver ◽  
Kupffer Cells ◽  
Hepatic Stellate Cells ◽  
Stellate Cells ◽  
Receptor Expression ◽  
Sinusoidal Endothelial Cells ◽  
Fluorescence Measurements ◽  
Parenchymal Cells

Betaine, taurine, and inositol participate as osmolytes in liver cell volume homeostasis and interfere with cell function. In this study we investigated whether osmolytes are also released from the intact liver independent of osmolarity changes. In the perfused rat liver, phagocytosis of carbon particles led to a four- to fivefold stimulation of taurine efflux into the effluent perfusate above basal release rates. This taurine release was inhibited by 70–80% by the anion exchange inhibitor DIDS or by pretreatment of the rats with gadolinium chloride. Administration of vasopressin, cAMP, extracellular ATP, and glucagon also increased release of betaine and/or taurine, whereas insulin, extracellular UTP, and adenosine were without effect. In isolated liver cells, it was shown that parenchymal cells and sinusoidal endothelial cells, but not Kupffer cells and hepatic stellate cells, release osmolytes upon hormone stimulation. This may be caused by a lack of hormone receptor expression in these cells, because single-cell fluorescence measurements revealed an increase of intracellular calcium concentration in response to vasopressin and glucagon in parenchymal cells and sinusoidal endothelial cells but not in Kupffer cells and hepatic stellate cells. The data show that Kupffer cells release osmolytes during phagocytosis via DIDS-sensitive anion channels. This mechanism may be used to compensate for the increase in cell volume induced by the ingestion of phagocytosable material. The physiological significance of hormone-induced osmolyte release remains to be evaluated.

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.

Morphilogy and Ultrastructure of in Vitro Cultures of Aortic Endothelial Cells Interacting with Antibodies

1979 ◽  
Author(s):  
S. Korach ◽  
D. Ngo
Keyword(s):  
Endothelial Cells ◽  
Cell Surface ◽  
Vascular Endothelial Cells ◽  
Intercellular Junctions ◽  
Cell Types ◽  
Endothelial Damage ◽  
Antibody Concentration ◽  
High Yields ◽  
Scanning Em

Adult pig aortas, sectioned longitudinally, were incubated in 0.1% collagenase-PBS (15 mn, 37°C). Gentle scraping of the lumenal surface resulted in high yields (3-4 x 106 cell/aorta) of viable endothelial cells, essentially devoid of other cell types by morphological and immunochemical (F VIII-antigen) criteria. Confluent monolayers were incubated for various times (5 mn to 1 wk) with decomplemented rabbit antisera raised against pig endothelial cells. Changes in cell morphology appeared to depend on antibody concentration rather than on duration of contact with antiserum. High concentrations of antiserum (5 to 20%) led to cytoplasmic shredding, bulging of cells and extensive vacuolization, whereas at lower concentrations, cells appeared almost normal. Transmission EM studies by the indirect immunoperoxydase method showed antibodies reacting with unfixed cells to be distributed all over the upper cell surface, in the outer parts of intercellular junctions, and within numerous pinocytotic vesicles. Much weaker reactions could also be seen at the lower cell surface. When viewed under the Scanning EM, antiserum-treated endothelial cells also disclosed antibody concentration-dependent bulging and release of cells from their substrate. In vitro studies of gradual modifications of vascular endothelial cells acted upon by antibodies should provide a better understanding of the structural and biochemical processes underlying endothelial damage and detachment.

scholarly journals Effects of taurolithocholate, a Ca2+-mobilizing agent, on cell Ca2+ in rat hepatocytes, human platelets and neuroblastoma NG108-15 cell line

1991 ◽  
Vol 273 (1) ◽  
pp. 153-160 ◽  
Author(s):  
J F Coquil ◽  
B Berthon ◽  
N Chomiki ◽  
L Combettes ◽  
P Jourdon ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Bile Acid ◽  
Cell Line ◽  
Rat Liver ◽  
Neuronal Cell ◽  
Rat Hepatocytes ◽  
Cell Types ◽  
Liver Cells ◽  
Human Platelets ◽  
Rat Liver Cells

The monohydroxy bile acid taurolithocholate permeabilizes the endoplasmic reticulum to Ca2+ in rat liver cells. To assess whether this action on the endoplasmic reticulum was restricted to this tissue, the effects of bile acid were investigated in two cell types quite unrelated to rat hepatocyte, namely human platelets and neuronal NG108-15 cell line. The results showed that taurolithocholate (3-100 microM) had no effect on free cytosolic [Ca2+] in human platelets and NG108-15 cells. whereas it increased it from 180 to 520 nM in rat hepatocytes. In contrast, in cells permeabilized by saponin, taurolithocholate initiated a profound release of the stored Ca2+ from the internal Ca2+ pools in the three cell types. The bile acid released 90% of the Ca2+ pools, with rate constants of about 5 min-1 and half-maximal effects at 15-30 microM. The results also showed that, in contrast with liver cells, which displayed an influx of [14C]taurolithocholate of 2 nmol/min per mg, human platelets and the neuronal cell line appeared to be resistant to [14C]taurolithocholate uptake. The influx measured in these latter cells was about 100-fold lower than in rat liver cells. Taken together, these data suggest that human platelets and NG108-15 cells do not possess the transport system for concentrating monohydroxy bile acids into cells. However, they show that human platelets and neuronal NG108-15 possess, in common with liver cells, the intracellular system responsible for taurolithocholate-mediated Ca2+ release from internal stores.

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