CD36 Is Not Involved in Scavenger Receptor–Mediated Endocytic Uptake of Glycolaldehyde- and Methylglyoxal-Modified Proteins by Liver Endothelial Cells

2005 ◽  
Vol 137 (5) ◽  
pp. 607-616 ◽  
Author(s):  
Keisuke Nakajou ◽  
Seikoh Horiuchi ◽  
Masakazu Sakai ◽  
Kenshiro Hirata ◽  
Makiko Tanaka ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Scavenger Receptor ◽  
Liver Endothelial Cells ◽  
Modified Proteins

scholarly journals Endocytosis of formaldehyde-treated serum albumin via scavenger pathway in liver endothelial cells

1984 ◽  
Vol 218 (1) ◽  
pp. 81-86 ◽  
Author(s):  
R Blomhoff ◽  
W Eskild ◽  
T Berg
Keyword(s):  
Endothelial Cells ◽  
Low Density Lipoprotein ◽  
Scavenger Receptor ◽  
Density Lipoprotein ◽  
Low Density ◽  
Surface Culture ◽  
Rat Liver Cells ◽  
Liver Endothelial Cells ◽  
Isolated Liver

Denatured or modified proteins (including albumin and low-density lipoprotein) are catabolized in vitro via scavenger receptors. We have studied the distribution of formaldehyde-denatured albumin in rat liver cells after intravenous injection of tracer doses of the protein. At 12 min after injection, most of the formaldehyde-denatured albumin (about 70% of the injected dose) was recovered in liver endothelial cells. Furthermore, isolated liver endothelial cells in suspension and in surface culture took up formaldehyde-denatured albumin by receptor-mediated endocytosis. Our data indicate that the scavenger receptor in liver is mainly located on the endothelial cells. Implications for the catabolism of low-density lipoproteins are discussed.

scholarly journals Clearance of NH2-terminal propeptides of types I and III procollagen is a physiological function of the scavenger receptor in liver endothelial cells.

1994 ◽  
Vol 179 (2) ◽  
pp. 405-412 ◽  
Author(s):  
J Melkko ◽  
T Hellevik ◽  
L Risteli ◽  
J Risteli ◽  
B Smedsrød
Keyword(s):  
Endothelial Cells ◽  
Physiological Function ◽  
Scavenger Receptor ◽  
Alpha Phase ◽  
Maximum Diameter ◽  
Type I ◽  
Waste Products ◽  
Type I Procollagen ◽  
Polyinosinic Acid ◽  
Liver Endothelial Cells

This study was undertaken to determine the fate of circulating NH2-terminal propeptide of type I procollagen (PINP) in rats. Radiolabeled PINP showed a biphasic serum decay curve after intravenous injection. 79% of the material disappeared from the blood during the initial alpha-phase (t1/2 alpha = 0.6 min), while the remaining 21% was eliminated with a t1/2 beta of 3.3 min. The major site of uptake was the liver, 78, 1, and 21% of its radioactivity being recovered in isolated liver endothelial cells (LEC), Kupffer cells, and parenchymal cells, respectively. In LEC, fluorescently labeled PINP accumulated in small (0.1 microns) peripheral and larger (> 0.1 microns) perinuclear vesicles within 10 min at 37 degrees C after a binding pulse at 4 degrees C. These grew in size with increasing chasing time, reaching a maximum diameter of 1 microns or more after 30 min, and taking the shape of rings that were stained only along their periphery. At chase intervals exceeding 30 min, the size of the vesicles decreased, and after 60 min the stain appeared in smaller, densely stained perinuclearly located vesicles. Degradation of 125I-PINP to free smaller fragments and 125I- was significant after 30 min. Only formaldehyde-treated albumin, acetylated LDL, polyinosinic acid and NH2-terminal propeptide of type III procollagen (PIIINP) competed with PINP for uptake. These findings indicate that clearance of PINP and PIIINP, which are normal waste products generated in large quantities, is a physiological function of the scavenger receptor in LEC.

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

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.

4.P.314 Nidogen is a physiological ligand for the scavenger receptor in liver endothelial cells

1997 ◽  
Vol 134 (1-2) ◽  
pp. 362
Author(s):  
B. Smedsrød ◽  
J. Melkko ◽  
U. Mayer ◽  
S. Johansson
Keyword(s):  
Endothelial Cells ◽  
Scavenger Receptor ◽  
Liver Endothelial Cells

Scavenger Receptors on Sinusoidal Liver Endothelial Cells Are Involved in the Uptake of Aldehyde-Modified Proteins

2005 ◽  
Vol 68 (5) ◽  
pp. 1423-1430 ◽  
Author(s):  
Michael J. Duryee ◽  
Thomas L. Freeman ◽  
Monte S. Willis ◽  
Carlos D. Hunter ◽  
Bartlett C. Hamilton ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Scavenger Receptors ◽  
Liver Endothelial Cells ◽  
Modified Proteins

Fc receptor mediated endocytosis of small soluble immunoglobulin G immune complexes in Kupffer and endothelial cells from rat liver

2000 ◽  
Vol 113 (18) ◽  
pp. 3255-3266
Author(s):  
T. Lovdal ◽  
E. Andersen ◽  
A. Brech ◽  
T. Berg
Keyword(s):  
Endothelial Cells ◽  
Kupffer Cells ◽  
Immune Complexes ◽  
Scavenger Receptor ◽  
Mannose Receptor ◽  
Endocytic Pathway ◽  
Scavenger Receptors ◽  
Receptor Ligands ◽  
Receptor Ligand ◽  
Liver Endothelial Cells

Soluble circulating immunoglobulin G immune complexes are mainly eliminated by the liver, predominantly by uptake in the Kupffer cells, but also the liver endothelial cells seem to be of importance. In the present study we have followed the intracellular turnover of immune complexes after Fc(gamma) receptor mediated endocytosis in cultured rat liver endothelial cells and Kupffer cells by means of isopycnic centrifugation, DAB cross-linking and morphological techniques. For the biochemical experiments the antigen, dinitrophenylated bovine serum albumin (BSA), was labeled with radioiodinated tyramine cellobiose that cannot cross biological membranes and therefore traps labeled degradation products at the site of formation. The endocytic pathway followed by immune complexes was compared with that followed by scavenger receptor ligands, such as formaldehyde treated BSA and dinitrophenylated BSA, and the mannose receptor ligand ovalbumin. Both Kupffer cells and liver endothelial cells took up and degraded the immune complexes, but there was a clear delay in the degradation of immune complexes as compared to degradation of ligands taken up via scavenger receptors. The kinetics of the endocytosis of scavenger receptor ligand was unaffected by simultaneous uptake of immune complexes. Experiments using both biochemical and morphological techniques indicated that the delayed degradation was due to a late arrival of the immune complexes at the lysosomes, which partly was explained by retroendocytosis of immune complexes. Electron microscopy studies revealed that the immune complexes were retained in the early endosomes that remained accessible to other endocytic markers such as ovalbumin. In addition, the immune complexes were seen in multivesicular compartments apparently devoid of other endocytic markers. Finally, the immune complexes were degraded in the same lysosomes as the ligands of scavenger receptors. Thus, immune complexes seem to follow an endocytic pathway that is kinetically or maybe morphologically different from that followed by scavenger and mannose receptor ligands.

Optimization purity of isolated primary liver endothelial cells (LSEC) using adenoviral gene transfer

2014 ◽  
Vol 52 (01) ◽  
Author(s):  
V Sterzer ◽  
M Alsamman ◽  
R Weiskirchen ◽  
C Trautwein ◽  
D Scholten
Keyword(s):  
Endothelial Cells ◽  
Gene Transfer ◽  
Adenoviral Gene Transfer ◽  
Liver Endothelial Cells
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