scholarly journals Abstract 4081: Podoplanin expression in Kupffer cells and platelet deposition on the hepatic sinusoidal cells in the liver of transgenic mice with a hepatocyte-specific human BRAFV600E mutation

2018 ◽  
Author(s):  
Hiroki Tanaka ◽  
Kie Horioka ◽  
Masahiro Yamamoto ◽  
Asari Masaru ◽  
Katsuhiro Okuda ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Kupffer Cells ◽  
Brafv600e Mutation ◽  
Sinusoidal Cells ◽  
Platelet Deposition ◽  
Podoplanin Expression

scholarly journals Glucagon receptors in endothelial and Kupffer cells of mouse liver.

1988 ◽  
Vol 36 (9) ◽  
pp. 1081-1089 ◽  
Author(s):  
J Watanabe ◽  
K Kanai ◽  
S Kanamura
Keyword(s):  
Endothelial Cells ◽  
Plasma Membrane ◽  
Kupffer Cells ◽  
Mouse Liver ◽  
Intracellular Transport ◽  
Coated Pits ◽  
Sinusoidal Cells ◽  
Nonparenchymal Cells ◽  
Glucagon Receptors

To determine whether hepatic sinusoidal cells contain glucagon receptors and, if so, to study the significance of the receptors in the cells, binding of [125I]-glucagon to nonparenchymal cells (mainly endothelial cells and Kupffer cells) isolated from mouse liver was examined by quantitative autoradiography and biochemical methods. Furthermore, the pathway of intracellular transport of colloidal gold-labeled glucagon (AuG) was examined in vivo. Autoradiographic and biochemical results demonstrated many glucagon receptors in both endothelial cells and Kupffer cells, and more receptors being present in endothelial cells than in Kupffer cells. In vivo, endothelial cells internalized AuG particles into coated vesicles via coated pits and transported the particles to endosomes, lysosomes, and abluminal plasma membrane. Therefore, receptor-mediated transcytosis of AuG occurs in endothelial cells. The number of particles present on the abluminal plasma membrane was constant if the amount of injected AuG increased. Therefore, the magnitude of receptor-mediated transcytosis of AuG appears to be regulated by endothelial cells. Kupffer cells internalized the ligand into cytoplasmic tubular structures via plasma membrane invaginations and transported the ligand exclusively to endosomes and lysosomes, suggesting that the ligand is degraded by Kupffer cells.

scholarly journals Analytical study of microsomes and isolated subcellular membranes from rat liver. IX. Nicotinamide adenine dinucleotide glycohydrolase: a plasma membrane enzyme prominently found in Kupffer cells.

1985 ◽  
Vol 100 (1) ◽  
pp. 189-197 ◽  
Author(s):  
A Amar-Costesec ◽  
M Prado-Figueroa ◽  
H Beaufay ◽  
J F Nagelkerke ◽  
T J van Berkel
Keyword(s):  
Plasma Membrane ◽  
Density Gradient ◽  
Rat Liver ◽  
Kupffer Cells ◽  
Nicotinamide Adenine Dinucleotide ◽  
Specific Activity ◽  
Subcellular Fractionation ◽  
Sinusoidal Cells ◽  
Nad Glycohydrolase ◽  
Sinusoidal Cell

The distribution of nicotinamide adenine dinucleotide (NAD) glycohydrolase in rat liver was investigated by subcellular fractionation and by isolation of hepatocytes and sinusoidal cells. The behavior of NAD glycohydrolase in subcellular fractionation was peculiar because, although the enzyme was mainly microsomal, plasma membrane preparations contained distinctly more NAD glycohydrolase than could be accounted for by their content in elements derived from the endoplasmic reticulum or the Golgi complex identified by glucose-6-phosphatase and galactosyltransferase, respectively. When microsomal and plasmalemmal preparations were brought to equilibrium in a linear-density gradient, NAD glycohydrolase differed from these enzymes and behaved like 5'-nucleotidase and alkaline phosphodiesterase I. NAD glycohydrolase was markedly displaced towards higher densities after treatment with digitonin. This behavior in density-gradient centrifugation strongly suggests that NAD glycohydrolase is an exclusive enzyme of the plasma membrane. NAD glycohydrolase differed clearly from other plasmalemmal enzymes when the liver was fractionated into hepatocytes and sinusoidal cells; its specific activity was considerably greater in sinusoidal cell than in hepatocyte preparations. Further subfractionation of sinusoidal cell preparations into endothelial and Kupffer cells by counterflow elutriation showed that NAD glycohydrolase is more active in Kupffer cells. We estimate that the specific activity of NAD glycohydrolase activity is at least 65-fold higher at the periphery of Kupffer cells than at the periphery of hepatocytes. As the enzyme shows not structure-linked latency and is an exclusive constituent of the plasma membranes, we conclude that it is an ectoenzyme that cannot lead to a rapid turnover of the cytosolic pyridine nucleotides.

scholarly journals Different immunolocalizations of cathepsins B, H, and L in the liver.

1985 ◽  
Vol 33 (11) ◽  
pp. 1173-1175 ◽  
Author(s):  
K Ii ◽  
K Hizawa ◽  
E Kominami ◽  
Y Bando ◽  
N Katunuma
Keyword(s):  
Horseradish Peroxidase ◽  
Kupffer Cells ◽  
Cathepsin B ◽  
Cathepsin L ◽  
Sinusoidal Cells ◽  
Dense Bodies ◽  
Cathepsin H ◽  
Normal Rat ◽  
Endogenous Proteins ◽  
First Time

Different localizations of cathepsin B, H, and L in normal rat liver were revealed immunohistochemically with anticathepsin Fab'-horseradish peroxidase conjugates. Staining of cathepsin B was strong in the periportal sinusoids, possibly in Kupffer cells; and weaker in panlobular hepatocytes. Staining of cathepsin H was strong in panlobular hepatocytes, especially in the periphery of the cytoplasm, possibly representing the peribiliary dense bodies; and weaker in periportal sinusoidal cells, possibly Kupffer cells. Staining of cathepsin L was strongest in centrilobular hepatocytes and weaker in periportal sinusoidal cells, possibly Kupffer cells. These findings, revealed for the first time in the present study, show that the histologic and intracellular localizations of the three cathepsins are different, suggesting that they have different roles in degradation of exogenous and endogenous proteins.

Erythrophagocytosis in the Liver in Hemolytic Anemias

1968 ◽  
Vol 26 ◽  
pp. 184-185
Author(s):  
O. T. Minick ◽  
E. Orfei ◽  
F. Volini ◽  
G. Kent
Keyword(s):  
Acid Phosphatase ◽  
Oxidative Damage ◽  
Phosphatase Activity ◽  
Kupffer Cells ◽  
Acid Phosphatase Activity ◽  
Common Type ◽  
Red Cell ◽  
Cell Fragments ◽  
Reticulo Endothelial System ◽  
Important Site

Hemolytic anemias were produced in rats by administering phenylhydrazine or anti-erythrocytic (rooster) serum, the latter having agglutinin and hemolysin titers exceeding 1:1000.Following administration of phenylhydrazine, the erythrocytes undergo oxidative damage and are removed from the circulation by the cells of the reticulo-endothelial system, predominantly by the spleen. With increasing dosage or if animals are splenectomized, the Kupffer cells become an important site of sequestration and are greatly hypertrophied. Whole red cells are the most common type engulfed; they are broken down in digestive vacuoles, as shown by the presence of acid phosphatase activity (Fig. 1). Heinz body material and membranes persist longer than native hemoglobin. With larger doses of phenylhydrazine, erythrocytes undergo intravascular fragmentation, and the particles phagocytized are now mainly red cell fragments of varying sizes (Fig. 2).

Sinusoidal Cells in Bone Marrow Take Up BSA-Au Conjugates in the Presence of an Artificial Blood Substitute

1985 ◽  
Vol 43 ◽  
pp. 700-701
Author(s):  
J.S. Geoffroy ◽  
R.P. Becker
Keyword(s):  
Bone Marrow ◽  
Los Angeles ◽  
Iliac Artery ◽  
Blood Substitute ◽  
Sprague Dawley ◽  
Coated Pits ◽  
Sinusoidal Cells ◽  
Artificial Blood ◽  
Left Common Iliac Artery

The pattern of BSA-Au uptake in vivo by endothelial cells of the venous sinuses (sinusoidal cells) of rat bone marrow has been described previously. BSA-Au conjugates are taken up exclusively in coated pits and vesicles, enter and pass through an “endosomal” compartment comprised of smooth-membraned tubules and vacuoles and cup-like bodies, and subsequently reside in multivesicular and dense bodies. The process is very rapid, with BSA-Au reaching secondary lysosmes one minute after presentation. (Figure 1)In further investigations of this process an isolated limb perfusion method using an artificial blood substitute, Oxypherol-ET (O-ET; Alpha Therapeutics, Los Angeles, CA) was developed. Under nembutal anesthesia, male Sprague-Dawley rats were laparotomized. The left common iliac artery and vein were ligated and the right iliac artery was cannulated via the aorta with a small vein catheter. Pump tubing, preprimed with oxygenated 0-ET at 37°C, was connected to the cannula.

An ultrastructural study on the shark liver

1990 ◽  
Vol 48 (3) ◽  
pp. 512-513
Author(s):  
Masako Yamada ◽  
Yutaka Tanuma
Keyword(s):  
Portal Vein ◽  
Kupffer Cells ◽  
Ultrastructural Study ◽  
Lipid Droplets ◽  
Microscopic Level ◽  
The Other ◽  
Fish Stock ◽  
Structural Studies ◽  
Light Microscopic Level ◽  
Perfusion Fixation

Although many fine structural studies on the vertebrate liver have been reported on mammals, avians, reptiles, amphibians, teleosts and cyclostomes, there are no studies on elasmobranchii liver except one by T. Ito etal. (1962) who studied it on light microscopic level. The purpose of the present study was to as certain the ultrastructural details and cytochemical characteristics of normal elasmobranchii liver and was to compare with the other higher vertebrate ones.Seventeen Scyliorhinus torazame, one kind of elasmobranchii, were obtained from the fish stock of the Ueno Zoo aquarium, Ueno, Tokyo. The sharks weighing about 300-600g were anesthetized with MS-222 (Sigma), and the livers were fixed by perfusion fixation via the portal vein according to the procedure of Y. Saito et al. (1980) for 10 min. Then the liver tissues were immersed in the same fixative for 2 hours and postfixed with 1% OsO4-solution in 0.1 Mc acodylate buffer for one hour. In order to make sure a phagocytic activity of Kupffer cells, latex particles (0.8 μm in diameter, 0.05mg/100 g b.w.) were injected through the portal vein for one min before fixation. For preservation of lipid droplets in the cytoplasm, a series of these procedure were performed under ice cold temperature until the end of dehydration.

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