Different Elimination of Circulating IgA Immune Complexes in Rat and Guinea Pig

Johansson, Anders

doi:10.1159/000236603

Cited by 4 publications

(3 citation statements)

References 30 publications

(48 reference statements)

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“…The ICs were characterized by ultracentrifugation in a continuous sucrose gradient as described previously [29]. Fractions of 0.5 ml were collected by upward displacement of the gradient, fraction number 1 representing the top contents of the tube.…”

Section: Methodsmentioning

confidence: 99%

“…The procedure for liver cell preparation has been described in detail elsewhere [29]. Briefly, the rats were anesthetized by intraperitoneal injections of pentobarbital (0.05 mg/g body weight).…”

Section: Methodsmentioning

confidence: 99%

“…in HEPES II buffer. After a total perfusion time of 20 min, single liver cells in suspension were isolated by filtration through nylon gauze, differential centrifugation and centrifugal elutriation [29]. This procedure yielded fractions of essential pure hepatocytes, pure SECs and a fraction containing both KCs and SECs.…”

Section: Methodsmentioning

confidence: 99%

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IgG Immune Complex Binding to and Activation of Liver Cells

Johansson

Sundqvist

2000

Int Arch Allergy Immunol

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Background/Aims: The aim was to study IgG immune complex (IC) binding to isolated hepatocytes, Kupffer cells (KCs) and sinusoidal endothelial cells (SECs). Further, we wished to analyze the capacity of IgG ICs to induce release of reactive oxygen metabolites by the IC-binding liver cells. Methods: ICs were formed between ¹²⁵I-tyramine-cellobiose-labelled dinitrophenyl-conjugated human serum albumin (¹²⁵I-TC-DNP₁₀HSA) and polyclonal rabbit IgG antibodies. Binding of ICs to different rat liver cells in suspension was studied at 4°C. Production of reactive oxygen metabolites was measured by luminol-enhanced chemiluminescence at 37°C. Results: IgG mediated binding of ¹²⁵I-TC-DNP₁₀HSA to both KCs and SECs, but not to hepatocytes. The binding showed saturation kinetics and was blocked by an excess of unlabelled IgG-ICs. IgG-ICs activated KCs, but not SECs, to a chemiluminescence response. Conclusions: Both KCs and SECs bind IgG-ICs in vitro, probably via Fc receptor interaction. IgG-ICs activate KCs to produce reactive oxygen metabolites. The binding of IgG-ICs to isolated hepatocytes is small.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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IgG Immune Complex Binding to and Activation of Liver Cells

Johansson

Sundqvist

2000

Int Arch Allergy Immunol

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Liver Cell Uptake and Degradation of Soluble Immunoglobulin G Immune Complexes In Vivo And In Vitro In Rats

Johansson

Løvdal

et al. 1996

Hepatology

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complement system also plays a crucial role in immune comImmune complexes were formed between dinitropheplex (IC) handling. Thus, binding and activation of complenylated human serum albumin (DNP-HSA) and polyment increases IC solubility, reduces the risk of extrahepatic clonal rabbit immunoglobulin G (IgG) anti-DNP antiboddeposition, and mediates binding to complement-receptor ies at antibody excess. The antigen was labelled with bearing cells. [10][11][12][13][14] In primates, complement-containing ICs isotope ( 125 I-tyramine-cellobiose) or fluorochrome, (6-bind to complement-receptor on erythrocytes, which deliver [fluorescein-5-(and-6)-carboxamido] hexanoic-acid, sucthe ICs to the reticuloendothelial system. 14,15 Complement cinimidyl ester). The radiolabelled antigen, native or deficiencies increase the risk of IC deposition outside of the antibody complexed, was given intravenously to rats.reticuloendothelial system, which has been proposed to be of Radioactivity was measured in various organs at 1 hour central importance for several inflammatory disease manifesfollowing injection. The liver was the main site for retations. 16 moval of the antigen as well as of the immune complexes.FcR-mediated elimination of circulating IgG-ICs has generWithin the liver, immune complexes were mainly associally been assumed to be mediated by Kupffer cells. I as a sensitive antigen label, with the advantage of retake in vitro was shown also by confocal fluorescence maining at the site of degradation. 30 We employed fluoresmicroscopy in Kupffer cells and in liver endothelial cells.cence labelling to visualize cell g-associated IgG-ICs by Also in vitro, only minor uptake was found in the hepatomeans of confocal fluorescence microscopy. cytes. We conclude that both liver endothelial cells andThe study was performed to elucidate the contribution of

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Hepatic cellular distribution and degradation of iron oxide nanoparticles following single intravenous injection in rats: implications for magnetic resonance imaging

Briley‐Saebo

Bjørnerud

Grant³

et al. 2004

Cell and Tissue Research

213

193

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The purpose of this study was to determine the cellular distribution and degradation in rat liver following intravenous injection of superparamagnetic iron oxide nanoparticles used for magnetic resonance imaging (NC100150 Injection). Relaxometric and spectrophotometric methods were used to determine the concentration of the iron oxide nanoparticles and their degradation products in isolated rat liver parenchymal, endothelial and Kupffer cell fractions. An isolated cell phantom was also constructed to quantify the effect of the degradation products on the loss of MR signal in terms of decreased transverse relaxation times, T2*. The results of this study show that iron oxide nanoparticles found in the NC100150 Injection were taken up and distributed equally in both liver endothelial and Kupffer cells following a single 5 mg Fe/kg body wt. bolus injection in rats. Whereas endothelial and Kupffer cells exhibited similar rates of uptake and degradation, liver parenchymal cells did not take up the NC100150 Injection iron oxide particles. Light-microscopy methods did, however, indicate an increased iron load, presumably as ferritin/hemosiderin, within the hepatocytes 24 h post injection. The study also confirmed that compartmentalisation of ferritin/hemosiderin may cause a significant decrease in the MRI signal intensity of the liver. In conclusion, the combined results of this study imply that the prolonged presence of breakdown product in the liver may cause a prolonged imaging effect (in terms of signal loss) for a time period that significantly exceeds the half-life of NC100150 Injection iron oxide nanoparticles in liver.

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Different Elimination of Circulating IgA Immune Complexes in Rat and Guinea Pig

Cited by 4 publications

References 30 publications

IgG Immune Complex Binding to and Activation of Liver Cells

IgG Immune Complex Binding to and Activation of Liver Cells

Liver Cell Uptake and Degradation of Soluble Immunoglobulin G Immune Complexes In Vivo And In Vitro In Rats

Hepatic cellular distribution and degradation of iron oxide nanoparticles following single intravenous injection in rats: implications for magnetic resonance imaging

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