scholarly journals Re-activation by glutamate or aspartate of amino-oxyacetate-inhibited aspartate aminotransferase in vitro and in isolated hepatocytes

1981 ◽  
Vol 198 (1) ◽  
pp. 219-223 ◽  
Author(s):  
Neal W. Cornell ◽  
Kathryn E. Crow ◽  
Richard P. Whitefoot
Keyword(s):  
Amino Acids ◽  
Aspartate Aminotransferase ◽  
Rat Hepatocytes ◽  
Isolated Hepatocytes ◽  
Isolated Rat Hepatocytes ◽  
Whole Cells ◽  
Cell Extracts ◽  
Isolated Rat

Experiments with isolated rat hepatocytes and with cell extracts indicate, in contrast with previous reports, that pyruvate does not block or reverse the inhibition of aspartate aminotransferase (EC 2.6.1.1) by amino-oxyacetate. That inhibition, however, is partially overcome by glutamate or aspartate either in cell extracts or in whole cells incubated with substrate combinations that cause accumulation of those amino acids.

scholarly journals Inhibition by cycloserine of mitochondrial and cytosolic aspartate aminotransferase in isolated rat hepatocytes

1981 ◽  
Vol 194 (3) ◽  
pp. 1027-1030 ◽  
Author(s):  
A M Janski ◽  
N W Cornell
Keyword(s):  
Aspartate Aminotransferase ◽  
Rat Hepatocytes ◽  
Isolated Hepatocytes ◽  
Isolated Rat Hepatocytes ◽  
Isolated Mitochondria ◽  
Isolated Rat

Isolated hepatocytes were incubated with L-cycloserine and then treated with digitonin so that mitochondrial and cytosolic fractions were obtained in 5 s. Mitochondrial and total cellular aspartate aminotransferases (EC 2.6.1.1) were inactivated in parallel. The enzyme was also inhibited in isolated mitochondria incubated with L-cycloserine. These results, in contrast with previous reports, indicate that cycloserine reacts equally with mitochondrial and cytosolic aspartate aminotransferases.

The Hep G2 Cell Line as a Possible Alternative to Isolated Hepatocytes in Cytotoxicity Studies

1988 ◽  
Vol 16 (1) ◽  
pp. 16-22
Author(s):  
Marina Marinovich ◽  
Jose L. Lorenzo ◽  
Liliana M. Flaminio ◽  
Agnese Granata ◽  
Corrado L. Galli
Keyword(s):  
Cell Line ◽  
Rat Hepatocytes ◽  
Prostaglandin E ◽  
Human Hepatoma ◽  
Hep G2 ◽  
Hep G2 Cells ◽  
Isolated Rat Hepatocytes ◽  
G2 Cells ◽  
Isolated Rat

The hepatotoxicity of carbon tetrachloride (CC14) was evaluated in vitro in freshly isolated rat hepatocytes and in the human hepatoma cell line, Hep G2. Toxicity was assessed by the leakage of cytosolic enzymes (lactate dehydrogenase and aspartate aminotransferase) and cell viability (trypan blue exclusion). The established human cells were less sensitive to CCl4-induced injury; higher doses of the toxic agent and longer incubation times were necessary to elicit cell damage. Micromolar concentrations of prostaglandin E2 significantly decreased enzyme leakage in both Hep G2 cells and rat hepatocytes challenged with CC14; a stable derivative of prostacyclin (ZK 36374) was ineffective. These results suggest that human hepatoma Hep G2 cells may represent a valid alternative to isolated rat hepatocytes for an initial approach to the in vitro evaluation of cell toxicity.

Acellular liver matrix improves the survival and functions of isolated rat hepatocytes cultured in vitro.

2004 ◽  
Author(s):  
Patrizia Burra ◽  
Silvia Tomat ◽  
Maria Teresa Conconi ◽  
Carlo Macchi ◽  
Francesco P Russo ◽  
...  
Keyword(s):  
Rat Hepatocytes ◽  
Isolated Rat Hepatocytes ◽  
Isolated Rat

scholarly journals Comparative metabolism of the antiviral dimer 3'-azido-3'-deoxythymidine-P-2',3'-dideoxyinosine and the monomers zidovudine and didanosine by rat, monkey, and human hepatocytes.

1997 ◽  
Vol 41 (11) ◽  
pp. 2502-2510 ◽  
Author(s):  
X R Pan-Zhou ◽  
E Cretton-Scott ◽  
X J Zhou ◽  
M Y Xie ◽  
R Rahmani ◽  
...  
Keyword(s):  
High Performance ◽  
Rat Hepatocytes ◽  
Human Hepatocytes ◽  
Metabolic Fate ◽  
Extracellular Medium ◽  
Isolated Rat Hepatocytes ◽  
Cell Extracts ◽  
Comparative Metabolism ◽  
Isolated Rat

AZT-P-ddI is an antiviral heterodimer composed of one molecule of 3'-azido-3'-deoxythymidine (AZT) and one molecule of 2',3'-dideoxyinosine (ddI) linked through their 5' positions by a phosphate bond. The metabolic fate of the dimer was studied with isolated rat, monkey, and human hepatocytes and was compared with that of its component monomers AZT and ddI. Upon incubation of double-labeled [14C]AZT-P-[3H]ddI in freshly isolated rat hepatocytes in suspension at a final concentration of 10 microM, the dimer was taken up intact by cells and then rapidly cleaved to AZT, AZT monophosphate, ddI, and ddI monophosphate. AZT and ddI so formed were then subject to their respective catabolisms. High-performance liquid chromatography analyses of the extracellular medium and cell extracts revealed the presence of unchanged dimer, AZT, 3'-azido-3'-deoxy-5'-beta-D-glucopyranosylthymidine (GAZT), 3'-amino-3'-deoxythymidine (AMT), ddI, and a previously unrecognized derivative of the dideoxyribose moiety of ddI, designated ddI-M. Trace extracellular but substantial intracellular levels of the glucuronide derivative of AMT (3'-amino-3'-deoxy-5'-beta-D-glucopyranosylthymidine [GAMT]) were also detected. Moreover, the extent of the formation of AMT, GAZT, and ddI-M from the dimer was markedly lower than that with AZT and ddI alone by the hepatocytes. With hepatocytes in primary culture obtained from rat, monkey, and human, large interspecies variations in the metabolism of AZT-P-ddI were observed. While GAZT and ddI-M, metabolites of AZT and ddI, respectively, as well as AZT 5'-monophosphate (MP) and ddI-MP were detected in the extracellular media of all species, AMT and GAMT were produced only by rat and monkey hepatocytes. No such metabolites were formed by human hepatocytes. The metabolic fate of the dimer by human hepatocytes was consistent with in vivo data recently obtained from human immunodeficiency virus-infected patients.

Preparation of microgram quantities of BaP-DNA adducts using isolated rat hepatocytes in vitro

1989 ◽  
Vol 10 (4) ◽  
pp. 789-791 ◽  
Author(s):  
David A. Dankovic ◽  
David L. Springer ◽  
David B. Mann ◽  
Linda G. Smith ◽  
Berta L. Thomas ◽  
...  
Keyword(s):  
Dna Adducts ◽  
Rat Hepatocytes ◽  
Isolated Rat Hepatocytes ◽  
Isolated Rat

scholarly journals EFFECT OF MURRAYA KOENIGII LEAVES EXTRACT ON GLUCONEOGENESIS AND GLYCOGENOLYSIS IN ISOLATED RAT HEPATOCYTES CULTURE

2018 ◽  
Vol 11 (11) ◽  
pp. 264
Author(s):  
Rohan S Phatak ◽  
Chitra C Khanwelkar ◽  
Kailas D Datkhile ◽  
Pratik P Durgawale
Keyword(s):  
Glycogen Content ◽  
Ex Vivo ◽  
Rat Hepatocytes ◽  
Diabetic Rats ◽  
Murraya Koenigii ◽  
Isolated Rat Hepatocytes ◽  
Genes Expression ◽  
Different Doses ◽  
Isolated Rat

Objectives: The present study was aimed to investigate the in vitro activity of Murraya koenigii extracts through various carbohydrate metabolic pathways in the isolated rat hepatocyte models.Methods: Different doses of metformin, aqueous and methanol extracts of M. koenigii leaves were evaluated in the MTT, glucose, and glycogen content assays in the cultured in vitro rat hepatocytes.Results: The study showed that there was a significant increase in activity with respect to the increased concentration of extracts. Slight effect was observed in the isolated rat hepatocytes culture, M. koenigii leaves extract may exert cytoprotective and hypoglycemic action.Conclusion: It may be needed to determine the effect of ex vivo rat hepatocytes isolated from diabetic rats. Effects of the plant or isolated compounds on the genes expression of signaling pathways should be investigated in further studies.

Signalling pathways and combinatory effects of insulin and amino acids in isolated rat hepatocytes

2002 ◽  
Vol 269 (15) ◽  
pp. 3742-3750 ◽  
Author(s):  
Ulrike Krause ◽  
Luc Bertrand ◽  
Liliane Maisin ◽  
Maria Rosa ◽  
Louis Hue
Keyword(s):  
Amino Acids ◽  
Rat Hepatocytes ◽  
Signalling Pathways ◽  
Isolated Rat Hepatocytes ◽  
Isolated Rat

Propranolol metabolism by isolated hepatocytes from normal and cirrhotic rat livers: the effect of albumin

1990 ◽  
Vol 68 (6) ◽  
pp. 657-662 ◽  
Author(s):  
Louise Gariepy ◽  
Daphna Fenyves ◽  
Jean-Luc Petit ◽  
Ginette Raymond ◽  
Jean-Pierre Villeneuve
Keyword(s):  
Free Fraction ◽  
Rat Hepatocytes ◽  
Isolated Hepatocytes ◽  
Hepatic Uptake ◽  
Albumin Concentration ◽  
Isolated Rat Hepatocytes ◽  
Subsequent Elimination ◽  
Rat Livers ◽  
Mediated Catalysis ◽  
Isolated Rat

Several recent reports have shown that the hepatic uptake and subsequent elimination of some substrates is faster in the presence of albumin than in its absence, as if some of the substrate bound to albumin was also available for uptake. In the present study, we examined the effect of albumin on the clearance of propranolol by isolated rat hepatocyte suspensions. The clearance of total drug decreased progressively as albumin concentration increased. There was also a progressive decrease in the free fraction of propranolol and the net result was an increase in the clearance of unbound drug (+50% at 40 g/L albumin). This increase was not due to an oncotic pressure effect of albumin, nor to the presence of fatty acids bound to albumin. The clearance of propranolol by isolated hepatocytes from cirrhotic rats was decreased compared with controls (−50%), and albumin also increased propranolol free clearance, albeit to a lesser extent than in control animals. Our results indicate that albumin facilitates the elimination of propranolol by hepatocytes, possibly because of surface-mediated catalysis of the albumin–propranolol complexes.Key words: propranolol clearance, albumin, isolated rat hepatocytes, cirrhosis.

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