A single endotoxin aggression causes dose-dependent reversible activation of rat liver ito cells without their transdifferentiation into myofibroblasts

2000 ◽  
Vol 130 (4) ◽  
pp. 997-1000
Author(s):  
I. M. Salakhov ◽  
A. S. Sozinov ◽  
S. R. Abdulkhakov ◽  
A. P. Kiyasov ◽  
N. L. Lysova ◽  
...  
Keyword(s):  
Rat Liver ◽  
Ito Cells ◽  
Dose Dependent ◽  
Endotoxin Aggression

Hepatic uptake of intact glutathione S-conjugate, inhibition by organic anions, and sinusoidal catabolism

1993 ◽  
Vol 265 (3) ◽  
pp. G547-G554
Author(s):  
C. A. Hinchman ◽  
A. T. Truong ◽  
N. Ballatori
Keyword(s):  
Guinea Pig ◽  
Rat Liver ◽  
Marked Decrease ◽  
Hepatic Uptake ◽  
Half Time ◽  
High Concentrations ◽  
Rat Livers ◽  
Dose Dependent ◽  
Uptake And Metabolism ◽  
Guinea Pig Liver

To identify potential mechanisms for hepatic removal of circulating glutathione (GSH) conjugates, uptake and metabolism of S-2,4-dinitrophenylglutathione (DNP-SG) were examined in isolated perfused livers from rat and guinea pig. Guinea pig livers perfused with 5 mumol of DNP-SG in a recirculating system (50 microM initial concn) rapidly cleared the conjugate from the perfusate (half time 3.7 min), whereas clearance was considerably slower in rat liver (half time 35 min). Disappearance of DNP-SG from the perfusate was accompanied by a simultaneous appearance of DNP-SG and its metabolites in bile. Addition of acivicin, an inhibitor of gamma-glutamyltransferase (gamma-GT), to the perfusate resulted in a marked decrease in DNP-SG clearance by guinea pig liver but had no effect in rat liver, suggesting that in the guinea pig this process is largely dependent on sinusoidal gamma-GT activity. However, even in the presence of acivicin, rat and guinea pig livers removed nearly one-half of the administered DNP-SG from the recirculating perfusate over 30 min. High concentrations of DNP-SG were found in bile (up to 3.7 mM), indicating that the liver is capable of transporting the intact conjugate from the circulation. When rat livers were perfused with higher concentrations of DNP-SG (100 and 250 microM), biliary excretion of DNP-SG increased dose dependently, with concentrations in bile reaching 10 mM at the higher dose. This was accompanied by a dose-dependent choleresis.(ABSTRACT TRUNCATED AT 250 WORDS)

ANALYSIS OF MT2A AND MT3 GENE EXPRESSION IN RAT'S LIVER AND KIDNEY IN RESPONSE TO CADMIUM CHLORIDE POISONING

2021 ◽  
pp. 38-42
Author(s):  
M. M. Ziatdinova ◽  
T. G. Yakupova ◽  
Ya. V. Valova ◽  
G. F. Mukhammadieva ◽  
D. O. Karimov ◽  
...  
Keyword(s):  
Gene Expression ◽  
Rat Liver ◽  
Cadmium Chloride ◽  
Transcriptional Activity ◽  
Female Rats ◽  
Expression Level ◽  
Cadmium Poisoning ◽  
Liver And Kidney ◽  
Dose Dependent ◽  
Higher Doses

The aim of this study was to investigate the expression of metallothionein genes in the liver and kidneys of rats with acute cadmium poisoning.Simulation of poisoning with cadmium chloride was carried out on white outbred female rats, divided into 4 groups depending on the dose of the injected toxicant. RNA samples isolated from rat liver and kidneys were used as research materials.The multiplicity of expression of the MT3 gene in the kidneys increased at the lowest dose of CdCl2 , which was used in this experiment (0.029 mg / kg); with increasing dosage, the expression level decreased, but not lower than the control values. Analysis of the expression of the same gene in the liver showed a tendency towards a decrease in the content of transcripts with increasing dose. The frequency of expression of the MT2A gene at higher doses of CdCl2 increased both in the liver and in the kidneys.In the present work, statistically significant dose-dependent changes in the expression multiplicity of metallothionein genes were detected 24 hours after CdCl2 administration. The revealed differences in the level of transcriptional activity of metallothionein genes require further investigation, since there are probably differences in the level of gene expression at earlier and later periods of toxicant action.

INACTIVATION AND DEGRADATION OF PORCINE CALCITONIN BY RAT LIVER, AND RELATIVE STABILITY OF SALMON CALCITONIN

1970 ◽  
Vol 48 (2) ◽  
pp. 181-188 ◽  
Author(s):  
M. de LUISE ◽  
T. J. MARTIN ◽  
R. A. MELICK
Keyword(s):  
Biological Activity ◽  
Rat Liver ◽  
Salmon Calcitonin ◽  
Trichloroacetic Acid ◽  
Maximal Activity ◽  
Active Principle ◽  
Rat Tissues ◽  
Prolonged Action ◽  
High Potency ◽  
Dose Dependent

SUMMARY Slices and homogenates of a number of rat tissues inactivated porcine calcitonin labelled with 125I; the most active tissue was the liver. Maximal activity was found in rat liver supernatant. The reaction was pH- and dose-dependent, the active principle was non-diffusible, inhibited by p-chloromercuribenzoate and EDTA, and destroyed by heat. Biological activity of calcitonin was lost parallel with the breakdown of the labelled calcitonin (as measured by loss of trichloroacetic acid precipitability). Salmon ultimobranchial calcitonin was much less susceptible to inactivation by rat liver supernatant than the porcine hormone, which may explain the high potency and prolonged action of the salmon hormone in the rat.

Synthesis and secretion of undulin by rat liver fat storing (ITO-) cells

1991 ◽  
Vol 13 ◽  
pp. S39
Author(s):  
T. Knittel ◽  
M. Odenthal ◽  
S. Schwögler ◽  
D. Schuppan ◽  
K-H.Meyer zum Büschenfelde ◽  
...  
Keyword(s):  
Rat Liver ◽  
Liver Fat ◽  
Ito Cells

Rat liver tolerance for partial resection and intraoperative radiation therapy: Regeneration is radiation dose dependent

1990 ◽  
Vol 45 (3) ◽  
pp. 196-200 ◽  
Author(s):  
Maurizio Bossola ◽  
Hollis W. Merrick ◽  
Ahmed Eltaki ◽  
Rocco Bellantone ◽  
Andrew J. Milligan ◽  
...  
Keyword(s):  
Radiation Therapy ◽  
Radiation Dose ◽  
Rat Liver ◽  
Partial Resection ◽  
Intraoperative Radiation Therapy ◽  
Intraoperative Radiation ◽  
Dose Dependent

scholarly journals Nucleoside uptake in rat liver parenchymal cells

1996 ◽  
Vol 317 (3) ◽  
pp. 835-842 ◽  
Author(s):  
Joan MERCADER ◽  
Mireia GOMEZ-ANGELATS ◽  
Belén del SANTO ◽  
Javier CASADO ◽  
Antonio F. FELIPE ◽  
...  
Keyword(s):  
Rat Liver ◽  
Nucleoside Transport ◽  
Transport Systems ◽  
Dependent Manner ◽  
Transport Activity ◽  
Liver Parenchymal ◽  
Uridine Uptake ◽  
High Concentrations ◽  
Parenchymal Cells ◽  
Dose Dependent

Rat liver parenchymal cells express Na+-dependent and Na+-independent nucleoside transport activity. The Na+-dependent component shows kinetic properties and substrate specificity similar to those reported for plasma membrane vesicles [Ruiz-Montasell, Casado, Felipe and Pastor-Anglada (1992) J. Membr. Biol. 128, 227–233]. This transport activity shows apparent Km values for uridine in the range 8–13 μM and a Vmax of 246 pmol of uridine per 3 min per 106 cells. Most nucleosides, including the analogue formycin B, cis-inhibit Na+-dependent uridine transport, although thymidine and cytidine are poor inhibitors. Inosine and adenosine inhibit Na+-dependent uridine uptake in a dose-dependent manner, reaching total inhibition. Guanosine also inhibits Na+-dependent uridine uptake, although there is some residual transport activity (35% of the control values) that is resistant to high concentrations of guanosine but may be inhibited by low concentrations of adenosine. The transport activity that is inhibited by high concentrations of thymidine is similar to the guanosine-resistant fraction. These observations are consistent with the presence of at least two Na+-dependent transport systems. Na+-dependent uridine uptake is sensitive to N-ethylmaleimide treatment, but Na+-independent transport is not. Nitrobenzylthioinosine (NBTI) stimulates Na+-dependent uridine uptake. The NBTI effect involves a change in Vmax, it is rapid, dose-dependent, does not need preincubation and can be abolished by depleting the Na+ transmembrane electrochemical gradient. Na+-independent uridine transport seems to be insensitive to NBTI. Under the same experimental conditions, NBTI effectively blocks most of the Na+-independent uridine uptake in hepatoma cells. Thus the stimulatory effect of NBTI on the concentrative nucleoside transporter of liver parenchymal cells cannot be explained by inhibition of nucleoside efflux.

scholarly journals Effect of micromolar concentrations of manganese ions on calcium-ion cycling in rat liver mitochondria

1983 ◽  
Vol 212 (3) ◽  
pp. 773-782 ◽  
Author(s):  
B P Hughes ◽  
J H Exton
Keyword(s):  
Rat Liver ◽  
Calcium Ion ◽  
Incubation Medium ◽  
Liver Mitochondria ◽  
Ruthenium Red ◽  
Rat Liver Mitochondria ◽  
Manganese Ions ◽  
Dose Dependent Decrease ◽  
Incubation Temperatures ◽  
Dose Dependent

The effects of micromolar concentrations of Mn2+ on the rat liver mitochondrial Ca2+ cycle were investigated. It was found that the addition of Mn2+ to mitochondria which were cycling 45Ca2+ led to a rapid dose dependent decrease in the concentration of extramitochondrial 45Ca2+ of about 1 nmol/mg of protein. The effect was complete within 30 s, was half maximal with 10 microM Mn2+ and was observed in the presence of 3 mM Mg2+ and 1 mM ATP. It occurred over a broad range of incubation temperatures, pH and mitochondrial Ca2+ loads. It was not observed when either Mg2+ or phosphate was absent from the incubation medium, or in the presence of Ruthenium Red. These findings indicate that micromolar concentrations of Mn2+ stimulate the uptake of Ca2+ by rat liver mitochondria, and provide evidence for an interaction between Mg2+ and Mn2+ in the control of mitochondrial Ca2+ cycling.

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