Functional and morphological characterization of cultures of Kupffer cells and liver endothelial cells prepared by means of density separation in Percoll, and selective substrate adherence

1985 ◽  
Vol 241 (3) ◽  
Author(s):  
B�rd Smedsr�d ◽  
H�kan Pertoft ◽  
G�sta Eggertsen ◽  
Christer Sundstr�m
Keyword(s):  
Endothelial Cells ◽  
Kupffer Cells ◽  
Morphological Characterization ◽  
Density Separation ◽  
Liver Endothelial Cells

Morphological Characterization of Scavenger Receptor-Mediated Processing of Modified Lipoproteins by Rat Liver Endothelial Cells

1994 ◽  
Vol 210 (1) ◽  
pp. 62-70 ◽  
Author(s):  
Sebastiaan Esbach ◽  
Monique F. Stins ◽  
Adriaan Brouwer ◽  
Paul J.M. Roholl ◽  
Theo J.C. van Berkel ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Rat Liver ◽  
Scavenger Receptor ◽  
Morphological Characterization ◽  
Modified Lipoproteins ◽  
Liver Endothelial Cells

Both Kupffer cells and liver endothelial cells play an important role in the clearance of IgA and IgG immune complexes

1992 ◽  
Vol 143 (2) ◽  
pp. 219-224 ◽  
Author(s):  
W.M.J.M. Bogers ◽  
R.-K. Stad ◽  
L.A. Van Es ◽  
M.R. Daha
Keyword(s):  
Endothelial Cells ◽  
Kupffer Cells ◽  
Immune Complexes ◽  
Liver Endothelial Cells

scholarly journals Evidence for reverse cholesterol transport in vivo from liver endothelial cells to parenchymal cells and bile by high-density lipoprotein

1990 ◽  
Vol 268 (3) ◽  
pp. 685-691 ◽  
Author(s):  
H F Bakkeren ◽  
F Kuipers ◽  
R J Vonk ◽  
T J C Van Berkel
Keyword(s):  
Endothelial Cells ◽  
High Density Lipoprotein ◽  
Kupffer Cells ◽  
Reverse Cholesterol Transport ◽  
Density Lipoprotein ◽  
Cholesterol Transport ◽  
Cholesterol Esters ◽  
Liver Endothelial Cells ◽  
Parenchymal Cells

Acetylated low-density lipoprotein (acetyl-LDL), biologically labelled in the cholesterol moiety of cholesteryl oleate, was injected into control and oestrogen-treated rats. The serum clearance, the distribution among the various lipoproteins, the hepatic localization and the biliary secretion of the [3H]cholesterol moiety were determined at various times after injection. In order to monitor the intrahepatic metabolism of the cholesterol esters of acetyl-LDL in vivo, the liver was subdivided into parenchymal, endothelial and Kupffer cells by a low-temperature cell-isolation procedure. In both control and oestrogen-treated rats, acetyl-LDL is rapidly cleared from the circulation, mainly by the liver endothelial cells. Subsequently, the cholesterol esters are hydrolysed, and within 1 h after injection, about 60% of the cell- associated cholesterol is released. The [3H]cholesterol is mainly recovered in the high-density lipoprotein (HDL) range of the serum of control rats, while low levels of radioactivity are detected in serum of oestrogen-treated rats. In control rats cholesterol is transported from endothelial cells to parenchymal cells (reverse cholesterol transport), where it is converted into bile acids and secreted into bile. The data thus provide evidence that HDL can serve as acceptors for cholesterol from endothelial cells in vivo, whereby efficient delivery to the parenchymal cells and bile is assured. In oestrogen-treated rats the radioactivity from the endothelial cells is released with similar kinetics as in control rats. However, only a small percentage of radioactivity is found in the HDL fraction and an increased uptake of radioactivity in Kupffer cells is observed. The secretion of radioactivity into bile is greatly delayed in oestrogen-treated rats. It is concluded that, in the absence of extracellular lipoproteins, endothelial cells can still release cholesterol, although for efficient transport to liver parenchymal cells and bile, HDL is indispensable.

scholarly journals Studies in vivo and in vitro on the uptake and degradation of soluble collagen α1(I) chains in rat liver endothelial and Kupffer cells

1985 ◽  
Vol 228 (2) ◽  
pp. 415-424 ◽  
Author(s):  
B Smedsrød ◽  
S Johansson ◽  
H Pertoft
Keyword(s):  
Endothelial Cells ◽  
Endothelial Cell ◽  
Kupffer Cell ◽  
Kupffer Cells ◽  
Cultured Cells ◽  
Chondroitin Sulphate ◽  
Liver Cells ◽  
Type I ◽  
Liver Endothelial Cell ◽  
Liver Endothelial Cells

Intravenously administered 125I-labelled monomeric alpha 1 chains (125I-alpha 1) of collagen type I were rapidly cleared and degraded by the liver of rats. Isolation of the liver cells after injection of the label revealed that the uptake per liver endothelial cell equalled the uptake per Kupffer cell, whereas the amount taken up per hepatocyte was negligible. The uptake of 125I-alpha 1 in cultured cells was 10 times higher per liver endothelial cell than per Kupffer cell. The ligand was efficiently degraded by cultures of both cell types. However, spent medium from cultures of Kupffer cells, unlike that from cultures of other cells, contained gelatinolytic activity which degraded 125I-alpha 1. The presence of hyaluronic acid, chondroitin sulphate or mannose/N-acetylglucosamine-terminal glycoproteins, which are endocytosed by the liver endothelial cells via specific receptors, did not interfere with binding, uptake or degradation of 125I-alpha 1 by these cells. Unlabelled alpha 1 and heat-denatured collagen inhibited the binding to a much greater extent than did native collagen. The presence of fibronectin or F(ab')2 fragments of anti-fibronectin antibodies did not affect the interaction of the liver endothelial cells, or of other types of liver cells, with 125I-alpha 1. The accumulation of fluorescein-labelled heat-denatured collagen in vesicles of cultured liver endothelial cells is evidence that the protein is internalized. Moreover, chloroquine, 5-dimethylaminonaphthalene-1-sulphonylcadaverine (dansylcadaverine), monensin and cytochalasin B, which impede one or more steps of the endocytic process, inhibited the uptake of 125I-alpha 1 by the liver endothelial cells. Leupeptin, an inhibitor of cathepsin B and ‘collagenolytic cathepsins’, inhibited the intralysosomal degradation of 125I-alpha 1, but had no effect on the rate of uptake of the ligand. The current data are interpreted as follows. (1) The ability of the liver endothelial cells and the Kupffer cells to sequester circulating 125I-alpha 1 efficiently may indicate a physiological pathway for the breakdown of connective-tissue collagen. (2) The liver endothelial cells express receptors that specifically recognize and mediate the endocytosis of collagen alpha 1(I) monomers. (3) The receptors also recognize denatured collagen (gelatin). (4) Fibronectin is not involved in the binding of alpha 1 to the receptors. (5) Degradation occurs intralysosomally by leupeptin-inhibitable cathepsins.

scholarly journals Morphological Characterization of Kupffer and Endothelial Cells of Rat Liver Isolated By Counterflow Elutriation

1978 ◽  
Vol 75 (1) ◽  
pp. 80-87 ◽  
Author(s):  
Rainer N. Zahlten ◽  
Herbert K. Hagler ◽  
Michael E. Nejtek ◽  
C. Jeffrey Day
Keyword(s):  
Endothelial Cells ◽  
Rat Liver ◽  
Morphological Characterization

scholarly journals Localization of the heparin-releasable lipase in situ in the rat liver

1979 ◽  
Vol 181 (1) ◽  
pp. 245-246 ◽  
Author(s):  
T Kuusi ◽  
E A Nikklä ◽  
I Virtanen ◽  
P K J Kinnunen
Keyword(s):  
Electron Microscopy ◽  
Endothelial Cells ◽  
Rat Liver ◽  
Kupffer Cells ◽  
Hepatic Lipase ◽  
Physiological Significance ◽  
Immuno Electron Microscopy ◽  
Liver Endothelial Cells

Immunofluorescence and immuno-electron microscopy were used for the localization of the heparin-releasable lipase in situ in the rat liver. The lipase is located exclusively on the liver endothelial cells. No labelling could be detected on the parenchymal of Kupffer cells, or in the livers of heparin-pretreated animals. The physiological significance of the endothelial localization of the hepatic lipase is discussed.

Preparation of isolated liver endothelial cells and Kupffer cells in high yield by means of an enterotoxin

1984 ◽  
Vol 150 (1) ◽  
pp. 194-204 ◽  
Author(s):  
Rune Blomhoff ◽  
Bård Smedsrød ◽  
Winnie Eskild ◽  
Per Einar Granum ◽  
Trond Berg
Keyword(s):  
Endothelial Cells ◽  
Kupffer Cells ◽  
High Yield ◽  
Liver Endothelial Cells ◽  
Isolated Liver

scholarly journals New Scavenger Receptor-Like Receptors for the Binding of Lipopolysaccharide to Liver Endothelial and Kupffer Cells

1998 ◽  
Vol 66 (11) ◽  
pp. 5107-5112 ◽  
Author(s):  
Marijke van Oosten ◽  
Erika van de Bilt ◽  
Theo J. C. van Berkel ◽  
Johan Kuiper
Keyword(s):  
Endothelial Cells ◽  
Kupffer Cells ◽  
Binding Sites ◽  
Oxidized Ldl ◽  
Scavenger Receptor ◽  
Scavenger Receptors ◽  
Liver Endothelial Cells ◽  
Parenchymal Cells

ABSTRACT Lipopolysaccharide (LPS) is cleared from the blood mainly by the liver. The Kupffer cells are primarily responsible for this clearance; liver endothelial and parenchymal cells contribute to a lesser extent. Although several binding sites have been described, only CD14 is known to be involved in LPS signalling. Among the other LPS binding sites that have been identified are scavenger receptors. Scavenger receptor class A (SR-A) types I and II are expressed in the liver on endothelial cells and Kupffer cells, and a 95-kDa receptor, identified as macrosialin, is expressed on Kupffer cells. In this study, we examined the role of scavenger receptors in the binding of LPS by the liver in vivo and in vitro. Fucoidin, a scavenger receptor ligand, significantly reduced the clearance of 125I-LPS from the serum and decreased the liver uptake of 125I-LPS about 40%. Within the liver, the in vivo binding of 125I-LPS to Kupffer and liver endothelial cells was decreased 72 and 71%, respectively, while the binding of 125I-LPS to liver parenchymal cells increased 34% upon fucoidin preinjection. Poly(I) inhibited the binding of 125I-LPS to Kupffer and endothelial cells in vitro 73 and 78%, respectively, while poly(A) had no effect. LPS inhibited the binding of acetylated low-density lipoprotein (acLDL) to Kupffer and liver endothelial cells 40 and 55%, respectively, and the binding of oxidized LDL (oxLDL) to Kupffer and liver endothelial cells 65 and 61%, respectively. oxLDL and acLDL did not significantly inhibit the binding of LPS to these cells. We conclude that on both endothelial cells and Kupffer cells, LPS binds mainly to scavenger receptors, but SR-A and macrosialin contribute to a limited extent to the binding of LPS.

Regulation of endothelin synthesis in hepatic endothelial cells

1998 ◽  
Vol 274 (6) ◽  
pp. G1068-G1076 ◽  
Author(s):  
Ann T. Eakes ◽  
Merle S. Olson
Keyword(s):  
Endothelial Cells ◽  
Mrna Expression ◽  
Kupffer Cells ◽  
Transforming Growth Factor ◽  
Culture Media ◽  
Mrna Level ◽  
Endotoxin Challenge ◽  
Endotoxin Exposure ◽  
Tnf Α ◽  
Liver Endothelial Cells

Endothelin (ET) stimulates vasoconstriction and glucose production and mediator synthesis in the liver. Only hepatic endothelial cells express ET-1 mRNA, and during endotoxemia in the intact rat, a ninefold increase in hepatic ET-1 mRNA occurs within 3 h of lipopolysaccharide (LPS) infusion [A. T. Eakes, K. M. Howard, J. E. Miller, and M. S. Olson. Am. J. Physiol. 272 ( Gastrointest. Liver Physiol. 35): G605–G611, 1997]. The present study defines the mechanism by which hepatic ET production is enhanced during endotoxin exposure. Culture media conditioned by exposure to endotoxin-treated Kupffer cells stimulated a twofold increase in immunoreactive ET-1 (irET-1) secretion by liver endothelial cells. Transforming growth factor-β (TGF-β), tumor necrosis factor-α (TNF-α), LPS, and platelet-activating factor (PAF) were tested for their ability to stimulate cultured liver endothelial cells to secrete irET-1. Although TNF-α, LPS, and PAF had no significant effect on ET-1 synthesis, TGF-β increased ET-1 mRNA expression and irET-1 secretion. In coculture experiments, treating Kupffer cells with endotoxin caused a doubling of the ET-1 mRNA level in the liver endothelial cells. This increase in ET-1 mRNA was attenuated by a TGF-β-neutralizing antibody. Hence, a paracrine signaling mechanism operates between Kupffer cells that release TGF-β on endotoxin challenge and hepatic endothelial cells in which TGF-β stimulates ET-1 mRNA expression and ET-1 secretion; this intercellular signaling relationship is an important component in the hepatic responses to endotoxin exposure.

scholarly journals Characterization of a hyaluronan receptor on rat sinusoidal liver endothelial cells and its functional relationship to scavenger receptors

Hepatology ◽  
1999 ◽  
Vol 30 (5) ◽  
pp. 1276-1286 ◽  
Author(s):  
Peter A. G. McCourt ◽  
Bård H. Smedsrød ◽  
Jukka Melkko ◽  
Staffan Johansson
Keyword(s):  
Endothelial Cells ◽  
Functional Relationship ◽  
Scavenger Receptors ◽  
Liver Endothelial Cells ◽  
Hyaluronan Receptor
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