scholarly journals Cytochemical localization of beta-NADPase in rat hepatocytes and Kupffer cells. Comparison with thiamine pyrophosphatase (TPPase).

1984 ◽  
Vol 32 (5) ◽  
pp. 541-546 ◽  
Author(s):  
S Angermüller ◽  
H D Fahimi
Keyword(s):  
Golgi Apparatus ◽  
Kupffer Cells ◽  
Intracellular Localization ◽  
Rat Hepatocytes ◽  
The Other ◽  
Cytochemical Localization ◽  
Liver Parenchymal ◽  
Thiamine Pyrophosphatase ◽  
The Difference ◽  
Parenchymal Cells

The intracellular localization of beta-NADPase in rat hepatocytes and Kupffer cells has been studied and compared with the pattern of TPPase in these cells. The reaction product for beta-NADPase is present in some but not all hepatocytes in two cisternae on the trans aspect of the Golgi apparatus. It is absent from the trans-most lamella and the GERL of hepatocytes. TPPase, on the other hand, is limited to the first Golgi cisterna on the trans aspect with sprinkles of reaction product in the second lamella. Considering that TPPase is a marker of the trans Golgi lamella and hepatocyte Golgi stacks contain usually 2-4 lamellae, our observations suggest that beta-NADPase is localized in the trans as well as in the intermediate Golgi lamellae of liver parenchymal cells. In Kupffer cells, the reaction product for both beta-NADPase and TPPase was found in some but not in all cells. The enzyme beta-NADPase was localized in the rigid lamella and the tubulovacuolar system of GERL. This pattern differed significantly from that for TPPase, which was found in 2-3 cisternae at the trans aspect of the Golgi complex in Kupffer cells. These observations demonstrate the difference in the localization of beta-NADPase in hepatocytes and Kupffer cells. Such differences should be taken into consideration in studies of Golgi fractions, when phosphatase reactions are used as specific markers of Golgi components.

scholarly journals Regulation of vesicular pH in liver macrophages and parenchymal cells by ammonia and anisotonicity as assessed by fluorescein isothiocyanate-dextran fluorescence

1996 ◽  
Vol 315 (2) ◽  
pp. 385-392 ◽  
Author(s):  
Rainer SCHREIBER ◽  
Fan ZHANG ◽  
Dieter HÄUSSINGER
Keyword(s):  
Kupffer Cells ◽  
Ph Value ◽  
Fluorescein Isothiocyanate ◽  
Rat Hepatocytes ◽  
Cell Swelling ◽  
Membrane Flow ◽  
Liver Parenchymal ◽  
Concanamycin A ◽  
Acidic Compartment ◽  
Parenchymal Cells

Short-term-cultivated rat hepatocytes and Kupffer cells were allowed to endocytose fluorescein isothiocyanate (FITC)-coupled dextran, in order to study the effects of aniso-osmotic exposure and NH4Cl on apparent vesicular pH (pHves) by single-cell fluorescence. Following a 2 h loading period with FITC–dextran in normo-osmotic (305 mosmol/l) medium, the apparent pHves was 6.01±0.05 (n = 39) in parenchymal cells and 4.94±0.04 (n = 76) in Kupffer cells. Under these conditions pHves in parenchymal cells, but not in Kupffer cells, was sensitive to changes in ambient osmolarity. Inhibition of vacuolar H+-ATPase by concanamycin A did not affect the osmosensitivity of pHves in parenchymal cells. However, the effects of anisotonicity on pHves were largely abolished in the presence of 4,4´-di-isothiocyanato-stilbene-2,2´-disulphonic acid (DIDS) or when extracellular chloride was substituted for gluconate. In neither Kupffer cells, nor liver parenchymal cells did hypo-osmotic cell swelling cause an increase in intracellular Ca2+. With regard to vesicular acidification, the following differences were noted between parenchymal and Kupffer cells. (1) In Kupffer cells endocytosed FITC–dextran reached a strongly acidic compartment with a pH value of approx. 5 within 5 min, whereas it took 4–5 h in parenchymal cells. Modification of pHves by hypo-osmolarity in Kupffer cells was only observed in a short-lived ‘early’ compartment with a pH value of approx. 6. (2) In contrast to pHves in parenchymal cells, pHves in Kupffer cells was very sensitive towards alkalinization by NH4Cl: addition of NH4Cl at 1 or 10 mM increased apparent pHves by 0.80 or 1.46 in Kupffer cells, but only by 0.18 or 0.56 in parenchymal cells. The low ammonia sensitivity of pHves in parenchymal cells was observed not only in the less acidic (pH approx. 6) endocytotic compartment which is reached by FITC–dextran within 2 h, but also in the stronger acidic compartment (pH approx. 5) which is reached after 4–5 h. (3) NH4Cl had no effect on the osmosensitivity of pHves in parenchymal cells, whereas in Kupffer cells pHves became sensitive to anisotonicity when NH4Cl was present. Osmosensitivity of pHves in Kupffer cells under these conditions, however, was not affected by genistein, DIDS or colchicine, whereas these compounds abolished the osmosensitivity of pHves in parenchymal cells. It is suggested that regulation of pHves by cell volume in liver parenchymal cells involves changes of vesicular chloride conductance. In addition, there are marked differences between Kupffer and parenchymal cells with respect to vesicular ammonia permeability and the kinetics of endocytotic membrane flow and acidification.

The Application of Quantitative Stereology to the Study of Adenohypophyseal Cells

1976 ◽  
Vol 34 ◽  
pp. 124-125
Author(s):  
Max C. Poole ◽  
V.B. Mahesh ◽  
Allen Costoff
Keyword(s):  
Anterior Pituitary ◽  
Cell Types ◽  
The Other ◽  
Vaginal Smears ◽  
Prolactin Cells ◽  
Estrous Cycles ◽  
Liver Parenchymal ◽  
Quantitative Stereology ◽  
Parenchymal Cells ◽  
Different Cell Types

Quantitative stereology of liver parenchymal cells has previously been reported (1,2), but there have been few studies of morphometry applied to a heterogenous tissue (3). Due to the presence of several different cell types, it is difficult to study the synthesis and secretion of hormones in cells of the anterior pituitary by conventional biochemical means. In this study prolactin cells were analyzed using morphometry during different times of the rat estrous cycle, and were correlated with changing levels of prolactin in the serum and pituitary gland.Vaginal smears of 60 day old Holtzman rats were monitored through three estrous cycles, and only four day cycling rats were used. Groups of six animals were decapitated at 4 P.M., 6 P.M., 10 P.M. and 12 midnight of proestrus and one half of the pituitary was processed for electron microscopy and the other half for assay.

scholarly journals Low-density-lipoprotein receptors in different rabbit liver cells

1989 ◽  
Vol 261 (2) ◽  
pp. 587-593 ◽  
Author(s):  
M S Nenseter ◽  
O Myklebost ◽  
R Blomhoff ◽  
C A Drevon ◽  
A Nilsson ◽  
...  
Keyword(s):  
Kupffer Cells ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Binding Activity ◽  
Rabbit Liver ◽  
Low Density ◽  
Apo B ◽  
Liver Parenchymal ◽  
Ldl Binding ◽  
Parenchymal Cells

Receptor-dependent uptake mechanisms for low-density lipoprotein (LDL) were studied in rabbit liver parenchymal and non-parenchymal cells. Hybridization studies with a cDNA probe revealed that mRNA for the apo (apolipoprotein) B,E receptor was present in endothelial and Kupffer cells as well as in parenchymal cells. By ligand-blotting experiments we showed that apo B,E-receptor protein was present in both parenchymal and non-parenchymal cells. Studies of binding of homologous LDL in cultured rabbit parenchymal cells suggested that about 63% of the specific LDL binding was mediated via the apo B,E receptor. Approx. 47% of the specific LDL binding was dependent on Ca2+, suggesting that specific Ca2+-dependent as well as Ca2+-independent LDL-binding sites exist in liver parenchymal cells. Methylated LDL bound to the parenchymal cells in a saturable manner. Taken together, our results showed that apo B,E receptors are present in rabbit liver endothelial and Kupffer cells as well as in the parenchymal cells, and that an additional saturable binding activity for LDL may exist on rabbit liver parenchymal cells. This binding activity was not inhibited by EGTA or reductive methylation of lysine residues in apo B. LDL degradation in parenchymal cells was mainly mediated via the apo B,E receptor.

scholarly journals Peroxidase-positive endothelial cells in sinusoids of the mouse liver.

1978 ◽  
Vol 26 (5) ◽  
pp. 409-411 ◽  
Author(s):  
G Stöhr ◽  
W Deimann ◽  
H D Fahimi
Keyword(s):  
Endothelial Cells ◽  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Nuclear Envelope ◽  
Kupffer Cells ◽  
Peroxidase Activity ◽  
Mouse Liver ◽  
Negative Reaction ◽  
Cytochemical Localization ◽  
Endogenous Peroxidase

The cytochemical localization of endogenous peroxidase activity in sinus lining cells of mouse liver has been investigated. Kupffer cells, as identified by their exclusive ability to phagocytize large (0.8 micron) latex particles, exhibited strong peroxidase activity in nuclear envelope and endoplasmic reticulum. In addition, weak to moderate peroxidase activity was found in 57% of all endothelial cells. The enzyme in endothelial cells was also localized in nuclear envelope and endoplasmic reticulum, with a negative reaction in the Golgi apparatus. These observations indicate that peroxidase staining, as a marker for identification of Kupffer cells in mouse liver, is only of limited value and should be used in conjunction with other methods (e.g., latex phagocytosis).

Nuclear receptor atlas of female mouse liver parenchymal, endothelial, and Kupffer cells

2013 ◽  
Vol 45 (7) ◽  
pp. 268-275 ◽  
Author(s):  
Zhaosha Li ◽  
J. Kar Kruijt ◽  
Ronald J. van der Sluis ◽  
Theo J. C. Van Berkel ◽  
Menno Hoekstra
Keyword(s):  
Expression Pattern ◽  
Nuclear Receptors ◽  
Nuclear Receptor ◽  
Kupffer Cells ◽  
Virgin Female ◽  
Orphan Receptor ◽  
Orphan Nuclear Receptors ◽  
Liver Parenchymal ◽  
Hepatic Expression ◽  
Parenchymal Cells

The liver consists of different cell types that together synchronize crucial roles in liver homeostasis. Since nuclear receptors constitute an important class of drug targets that are involved in a wide variety of physiological processes, we have composed the hepatic cell type-specific expression profile of nuclear receptors to uncover the pharmacological potential of liver-enriched nuclear receptors. Parenchymal liver cells (hepatocytes) and liver endothelial and Kupffer cells were isolated from virgin female C57BL/6 wild-type mice using collagenase perfusion and counterflow centrifugal elutriation. The hepatic expression pattern of 49 nuclear receptors was generated by real-time quantitative PCR using the NUclear Receptor Signaling Atlas (NURSA) program resources. Thirty-six nuclear receptors were expressed in total liver. FXR-α, EAR2, LXR-α, HNF4-α, and CAR were the most abundantly expressed nuclear receptors in liver parenchymal cells. In contrast, NUR77, COUP-TFII, LXR-α/β, FXR-α, and EAR2 were the most highly expressed nuclear receptors in endothelial and Kupffer cells. Interestingly, members of orphan receptor COUP-TF family showed a distinct expression pattern. EAR2 was highly and exclusively expressed in parenchymal cells, while COUP-TFII was moderately and exclusively expressed in endothelial and Kupffer cells. Of interest, the orphan receptor TR4 showed a similar expression pattern as the established lipid sensor PPAR-γ. In conclusion, our study provides the most complete quantitative assessment of the nuclear receptor distribution in liver reported to date. Our gene expression catalog suggests that orphan nuclear receptors such as COUP-TFII, EAR2, and TR4 may be of significant importance as novel targets for pharmaceutical interventions in liver.

scholarly journals Receptor-mediated endocytosis of retinol-binding protein by liver parenchymal cells: interference by radioactive iodination

1993 ◽  
Vol 291 (1) ◽  
pp. 187-191 ◽  
Author(s):  
L Malaba ◽  
G M Kindberg ◽  
K R Norum ◽  
T Berg ◽  
R Blomhoff
Keyword(s):  
Binding Protein ◽  
The Other ◽  
Retinol Binding Protein ◽  
Lag Phase ◽  
Steady Increase ◽  
Release Process ◽  
Liver Parenchymal ◽  
Cell Association ◽  
Higher Temperature ◽  
Parenchymal Cells

Retinol-binding protein (RBP) was iodinated directly by radio-iodine substitution on the tyrosyl residues by the sodium hypochlorite (NaOCl) or the Enzymobead (EB) methods, or indirectly by linkage of 125I-tyramine-cellobiose (TC) or 125I-N-succinimidyl-3-(4- hydroxyphenyl)propionic acid ester (SHPP) adduct on to free amino residues of RBP. Binding, uptake and degradation of iodinated RBP were studied in isolated rat and rabbit liver parenchymal cells. The amount of ligand bound to cells at 4 degrees C was dependent on the type of labelling, in that the 125I-TC ligand was bound to a lesser extent than NaClO-labelled 125I-RBP, EB-labelled 125I-RBP and 125I-SHPP-RBP. At 37 degrees C, the 125I-SHPP-RBP and the EB-labelled 125I-RBP became cell-associated more rapidly than the other two ligands. The higher cell association at 37 degrees C than at 4 degrees C suggests that internalization of the ligand occurred at the higher temperature. The degradation of the ligands was also different. The EB-labelled 125I-RBP, the 125I-TC-RBP and the 125I-SHPP-RBP showed an apparent lag phase before a steady increase in acid-soluble radioactivity was observed. Much less of EB-labelled 125I-RBP and 125I-TC-RBP were degraded (about 6%) than of the other two ligands (about 16%) after 120 min. About 50% of the acid-soluble radioactivity in these experiments could be accounted for by degradation in the medium, suggesting that about half of the degradation observed was intracellular. The present study therefore shows that the different labelling techniques yield varying estimates of the cellular handling of RBP. In addition, a rapid release of RBP was observed in experiments where cells were pulsed with radioactive RBP at 4 degrees C, washed and incubated further at 37 degrees C. Between 50% and 70% was released after 5 min of incubation. By increasing the temperature during the pulse to 37 degrees C, or by lowering the temperature during the chase to 4 degrees C, much less RBP was released from the cells. These data suggest that the release process represents recycling of internalized ligand from an early endosome.

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

Lipoproteins in Golgi Apparatus and GERL of Rat Hepatocytes: A CytoChemical Study

1977 ◽  
Vol 35 ◽  
pp. 432-433
Author(s):  
P.M. Novikoff ◽  
A. Yam
Keyword(s):  
Golgi Apparatus ◽  
Orotic Acid ◽  
Rat Hepatocytes ◽  
Cell Types ◽  
Low Density Lipoproteins ◽  
Low Density ◽  
Very Low Density Lipoproteins ◽  
Hepatocyte Ultrastructure ◽  
Cytochemical Study ◽  
Thiamine Pyrophosphatase

Our laboratory has recently reported that the marked fatty liver induced in rats by feeding a purine-free diet with 1% orotic acid (OA) can be reversed by addition of ethyl chlorophenoxyiso- butyrate (clofibrate or CPIB) to the OA diet (1). Hepatocyte ultrastructure returns to normal, as do the triacylglycerol levels in liver and serum. During reversal, GERL becomes prominent, distended with particles interpreted as lipoproteins undergoing degradation.This communication reports cytochemical observations on such hepatocytes. Thiamine pyrophosphatase (TPPase) activity in hepatocytes, as in various cell types (2), is localized to the inner (trans) element of the Golgi apparatus (Figure 1). GERL, in contrast, shows no TPPase activity but displays acid phosphatase (AcPase) activity (Figure 2). Particles resembling very low density lipoproteins (VLDL) are found in both GERL and elements of the Golgi apparatus. The presence of both AcPase activity and VLDL-like particles strengthens our earlier suggestion that lipoproteins may undergo transformations in GERL.

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