scholarly journals Studies on the Uptake Mechanism of Liposomes by Perfused Rat Liver. II. An Indispensable Factor for Liver Uptake in Serum

1987 ◽  
Vol 35 (3) ◽  
pp. 1189-1195 ◽  
Author(s):  
HIROSHI KIWADA ◽  
TAKAAKI MIYAJIMA ◽  
YUREKO KATO
Keyword(s):  
Rat Liver ◽  
Perfused Rat Liver ◽  
Uptake Mechanism ◽  
Liver Uptake

Metabolic Fate of Plasma Diamine Oxidase: Evidence of Isolated and Perfused Rat Liver Uptake

Digestion ◽  
1986 ◽  
Vol 34 (4) ◽  
pp. 243-250 ◽  
Author(s):  
Luciano D’Agostino ◽  
Carolina Ciacci ◽  
Gaetano Capuano ◽  
Bruno Daniele ◽  
Giuseppe D’Argenio ◽  
...  
Keyword(s):  
Rat Liver ◽  
Diamine Oxidase ◽  
Perfused Rat Liver ◽  
Metabolic Fate ◽  
Liver Uptake

Hepatic lipase-mediated hydrolysis versus liver uptake of HDL phospholipids and triacylglycerols by the perfused rat liver

1991 ◽  
Vol 1082 (2) ◽  
pp. 185-194 ◽  
Author(s):  
Pedro Marques-Vidal ◽  
Christine Azéma ◽  
Xavier Collet ◽  
Hugues Chap ◽  
Bertrand P. Perret
Keyword(s):  
Rat Liver ◽  
Hepatic Lipase ◽  
Perfused Rat Liver ◽  
Liver Uptake

Hepatic uptake and disposition of human polymeric IgA1 in perfused rat liver: evidence for incomplete biliary excretion and intrahepatic degradation

1985 ◽  
Vol 248 (4) ◽  
pp. G450-G455
Author(s):  
M. H. Finck ◽  
J. Reichen ◽  
J. M. Vierling ◽  
T. M. Kloppel ◽  
W. R. Brown
Keyword(s):  
Rat Liver ◽  
Biliary Excretion ◽  
Immunoglobulin A ◽  
Hepatic Metabolism ◽  
Hepatic Uptake ◽  
Secretory Component ◽  
Secretory Iga ◽  
Perfused Rat Liver ◽  
Liver Uptake ◽  
Single Pass

The hepatic uptake of polymeric immunoglobulin A (IgA) is mediated by secretory component; the resulting secretory IgA is excreted intact into bile. To define the hepatic metabolism of polymeric IgA, we quantitated the uptake and transport of human polymeric IgA1 after a single pass through the perfused rat liver. Uptake of polymeric IgA1 was compared with that of asialoorosomucoid, a glycoprotein whose uptake is mediated by the asialoglycoprotein receptor. Single-pass hepatic uptake of 125I-polymeric IgA1 and of 125I-asialoorosomucoid averaged 18.0 +/- 3.1% (SE) and 71.8 +/- 2.8%, respectively. The uptake of 125I-polymeric IgA1 was inhibited by excess unlabeled polymeric IgA1 but not by asialoorosomucoid. Only 13.0 +/- 1.6% of the 125I-polymeric IgA1 extracted by the liver was excreted into bile, whereas three-fourths was released into the hepatic venous effluent in degraded form. Thus, both the uptake and biliary excretion of polymeric IgA1 by the rat liver are inefficient processes. Polymeric IgA1 follows two distinct pathways after uptake by the liver: a small proportion is excreted intact into bile, while the majority is degraded and released back into the circulation.

Liver Blood Flow as a Major Determinant of the Clearance of Recombinant Human Tissue-Type Plasminogen Activator

1992 ◽  
Vol 67 (01) ◽  
pp. 083-087 ◽  
Author(s):  
A de Boer ◽  
C Kluft ◽  
J M Kroon ◽  
F J Kasper ◽  
H C Schoemaker ◽  
...  
Keyword(s):  
Blood Flow ◽  
Rat Liver ◽  
Healthy Subjects ◽  
Liver Blood Flow ◽  
Major Determinant ◽  
Tissue Type ◽  
Perfused Rat Liver ◽  
Liver Model ◽  
Type Plasminogen Activator ◽  
Proportional Change

SummaryThe influence of changes in liver blood flow on the clearance of rt-PA was studied both in healthy subjects and in a perfused rat liver model. Liver blood flow in healthy subjects was documented indirectly by the clearance of indocyanine green (ICG). Exercise reduced liver blood flow on average by 57% with a 95% confidence interval (95% Cl) ranging from 51% to 62% (n = 5) and increased plasma levels of rt-PA activity (after an i. v. infusion of 18 mg of rt-PA over 120 min) by 119% (95% Cl, 58% - 203%) and rt-PA antigen by 91% (95% Cl, 30% - 140%). In the perfused rat liver model it was shown that halving or doubling of the physiological flow rate of a perfusate, containing rt-PA caused a proportional change in the clearance of rt-PA, while the extraction of rt-PA by the liver remained similar. In conclusion, liver blood flow is a major determinant of the clearance of rt-PA. This may have important implications for dosage of rt-PA in patients with myocardial infarction.

Uptake, Internalization and Degradation of the Novel Plasminogen Activator Reteplase (BM 06.022) in the Rat

1995 ◽  
Vol 74 (06) ◽  
pp. 1501-1510 ◽  
Author(s):  
J Kuiper ◽  
H van de Bilt ◽  
U Martin ◽  
Th J C van Berkel
Keyword(s):  
Plasminogen Activator ◽  
Liver Cells ◽  
The Novel ◽  
Uptake Mechanism ◽  
Liver Uptake ◽  
Lysosomal Compartment ◽  
Β Phase ◽  
Α Phase ◽  
Parenchymal Liver

SummaryThe catabolism of the novel plasminogen activator reteplase (BM 06.022) was described. For this purpose BM 06.022 was radiolabelled with l25I or with the accumulating label l25I-tyramine cellobiose (l25I-TC).BM 06.022 was injected at a pharmacological dose of 380 μg/kg b.w. and it was cleared from the plasma in a biphasic manner with a half-life of about 1 min in the α-phase and t1/2of 20-28 min in the β-phase. 28% and 72% of the injected dose was cleared in the α-phase and β-phase, respectively. Initially liver, kidneys, skin, bones, lungs, spleen, and muscles contributed mainly to the plasma clearance. Only liver and the kidneys, however, were responsible for the uptake and subsequent degradation of BM 06.022 and contributed for 75% to the catabolism of BM 06.022. BM 06.022 was degraded in the lysosomal compartment of both organs. Parenchymal liver cells were responsible for 70% of the liver uptake of BM 06.022. BM 06.022 associated rapidly to isolated rat parenchymal liver cells and was subsequently degraded in the lysosomal compartment of these cells. BM 06.022 bound with low-affinity to the parenchymal liver cells (550 nM) and the binding of BM 06.022 could be displaced by t-PA (IC50 5.6 nM), indicating that the low-density lipoprotein receptor-related protein (LRP) could be involved in the binding of BM 06.022. GST-RAP, which is an inhibitor of LRP, could in vivo significantly inhibit the uptake of BM 06.022 in the liver.It is concluded that BM 06.022 is metabolized primarily in the liver and the kidneys. These organs take up and degrade BM 06.022 in the lysosomes. The uptake mechanism of BM 06.022 in the kidneys is unknown, while LRP is responsible for a low-affinity binding and uptake of BM 06.022 in parenchymal liver cells.

A Comparison of Plasminogen Activators Derived from Rat Plasma, Primary Rat Hepatocytes and Isolated Perfused Rat Liver

1982 ◽  
Vol 47 (02) ◽  
pp. 166-172 ◽  
Author(s):  
Yoav Sharoni ◽  
Maria C Topal ◽  
Patricia R Tuttle ◽  
Henry Berger
Keyword(s):  
Rat Liver ◽  
Isoelectric Point ◽  
Rat Hepatocytes ◽  
Cell Types ◽  
Plasminogen Activators ◽  
Rat Plasma ◽  
Isolated Perfused Rat Liver ◽  
Perfused Rat Liver ◽  
Molecular Weights ◽  
Physiological Relevance

SummaryOf the two cell types it was possible to culture from the dissociated rat liver, hepatocytes and Kupffer cells, only the former were fibrinolytically active. Rat hepatocytes during the first 24 hr in culture secreted two plasminogen activators with molecular weights identical to those found in rat plasma, an 80,000-dalton form (PA-80) and a 45,000-dalton form (PA-45). Partially purified preparations of plasminogen activators from both sources were subjected to isoelectric focusing (IEF) to compare characteristics further. There were three distinct peaks of PA-45 in each preparation with isoelectric points of 7.1, 7.2 and 7.4; all electrophoretic forms had the same low affinity to fibrin. PA-80 from both sources displayed similar IEF profiles with forms ranging from pH values of 7 to 8, all with the same high affinity to fibrin. The major form of PA-80 in the plasma preparation had an isoelectric point of 7.9 whereas that in the hepatocyte preparation had an isoelectric point of 7.6. The isolated perfused rat liver was also shown to produce both PA-80 and PA-45 emphasizing the physiological relevance of the findings with hepatocytes. It is concluded that in the rat hepatocytes contribute to the plasma profile with regard to the plasminogen activator content.

Troxerutin protects the isolated perfused rat liver from a possible lipid peroxidation by coumarin

Phytomedicine ◽  
2005 ◽  
Vol 12 (1-2) ◽  
pp. 52-61 ◽  
Author(s):  
B.S. Adam ◽  
R. Pentz ◽  
C.P. Siegers ◽  
O. Strubelt ◽  
M. Tegtmeier
Keyword(s):  
Lipid Peroxidation ◽  
Rat Liver ◽  
Isolated Perfused Rat Liver ◽  
Perfused Rat Liver
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