Effect of α-fetoprotein and albumin on the uptake of polyunsaturated fatty acids by rat hepatoma cells and fetal rat hepatocytes

1991 ◽  
Vol 1086 (1) ◽  
pp. 81-88 ◽  
Author(s):  
María Iturralde ◽  
M. Angeles Alava ◽  
Blanca González ◽  
Alberto Anel ◽  
Andrés Pin˜eiro
Keyword(s):  
Fatty Acids ◽  
Polyunsaturated Fatty Acids ◽  
Rat Hepatocytes ◽  
Hepatoma Cells ◽  
Fetal Rat ◽  
Rat Hepatoma ◽  
Rat Hepatoma Cells

Effects of fatty acids on apolipoprotein B secretion by McArdle RH-7777 rat hepatoma cells

1997 ◽  
Vol 1347 (1) ◽  
pp. 51-61 ◽  
Author(s):  
Janet D Sparks ◽  
Heidi L Collins ◽  
Ivan Sabio ◽  
Mark P Sowden ◽  
Harold C Smith ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Apolipoprotein B ◽  
Hepatoma Cells ◽  
Rat Hepatoma ◽  
Rat Hepatoma Cells

scholarly journals Membrane potential of rat hepatoma cells in culture: Influence of factors affecting amino acid transport

1995 ◽  
Vol 15 (4) ◽  
pp. 173-184 ◽  
Author(s):  
M. F. Mouat ◽  
A. C. Cantrell ◽  
K. L. Manchester
Keyword(s):  
Membrane Potential ◽  
Amino Acid ◽  
Amino Acid Transport ◽  
Rat Hepatocytes ◽  
Hepatoma Cells ◽  
Acid Transport ◽  
Factors Affecting ◽  
Cells In Culture ◽  
Rat Hepatoma ◽  
Rat Hepatoma Cells

The effect has been studied of various media, hormones and of amino acids on the membrane potential of rat hepatoma cells in culture measured by microelectrode impalement. Cells in Eagle's minimal essential medium plus 5% serum had a value which varied daily from about 5–8 mV, inside negative. The membrane potential of rat hepatocytes was measured to be 8.7 ± 0.2mV, inside negative. The membrane potential of the hepatoma cells was decreased by insulin and increased by glucagon. Membrane potential was unaffected by change of medium to Hanks' or Earle's balanced salt solutions or deprivation of serum. It was, however, reduced in cells in phosphate-buffered saline and by reduction of pH. The former effect was shown to be due to the higher [Na+] of phosphat-buffered saline as opposed to the other media. Addition of alanine, glycine, serine, proline and methylaminoisobutyrate all reduced membrane potential by 2–3 mV. Smaller decreases were seen with methionine, leucine and phenylalanine, but none with glutamine, threonine, BCH (2-aminonorborane-2-carboxylic acid) and D-alanine. The results are compared with the effects of similar conditions on aminoisobutyrate uptake. Whilst there was a correlation under some conditions there was not under others. It is concluded that for the hepatoma cells factors additional to the membrane potential must exert some influence on the capacity for amino acid transport.

scholarly journals Fatty Acids Induce L-CPT I Gene Expression through a PPARα-Independent Mechanism in Rat Hepatoma Cells

2005 ◽  
Vol 135 (10) ◽  
pp. 2313-2319 ◽  
Author(s):  
Cédric Le May ◽  
Michèle Caüzac ◽  
Claire Diradourian ◽  
Dominique Perdereau ◽  
Jean Girard ◽  
...  
Keyword(s):  
Gene Expression ◽  
Fatty Acids ◽  
Hepatoma Cells ◽  
Independent Mechanism ◽  
Cpt I ◽  
Rat Hepatoma ◽  
I Gene ◽  
Rat Hepatoma Cells

scholarly journals Dexamethasone increases the synthesis and secretion of a partially active fibronectin in rat hepatoma cells.

1982 ◽  
Vol 95 (1) ◽  
pp. 29-40 ◽  
Author(s):  
H Baumann ◽  
D Eldredge
Keyword(s):  
Rat Hepatocytes ◽  
Cell Interaction ◽  
Hepatoma Cells ◽  
Cell Protein ◽  
Adhesion Properties ◽  
Culture Cells ◽  
Unique System ◽  
Fetal Rat ◽  
Functional Defect ◽  
Rat Hepatoma

After treatment with dexamethasone, rat hepatoma-tissue culture cells show a markedly enhanced adhesion to the substratum and increased cell-to-cell interaction. In addition, there is a profound change in the production of secretory glycoproteins. Although the relative synthesis and secretion of a gelatin-binding, fibronectinlike glycoprotein is increased threefold, we do not think this protein is responsible for the improved adhesion properties of the cells because the hepatoma cells do not bind normal fibronectin and because the HTC-produced fibronectin is neither bound by fibroblasts nor has it any affinity for ganglioside-containing phospholipid vesicles. Therefore, these hepatoma cells represent a unique system for studying the regulation of fibronectin synthesis by glucocorticoids. Furthermore, analyses of primary fetal rat hepatocytes have shown that these cells, unlike normal adult hepatocytes, synthesize and secrete fibronectin, which is structurally related to the HTC-cell protein. The comparison of this protein with fibronectin from normal cells will allow a structural characterization of the functional defect in the fibronectin synthesized by transformed cells.

scholarly journals Rat hepatoma cells express novel transport systems for glutamine and glutamate in addition to those present in normal rat hepatocytes

1998 ◽  
Vol 330 (1) ◽  
pp. 255-260 ◽  
Author(s):  
D. John MGIVAN
Keyword(s):  
Cell Line ◽  
Transport System ◽  
Hepatoma Cell ◽  
Rat Hepatocytes ◽  
Hepatoma Cells ◽  
Transport Systems ◽  
Hepatoma Cell Line ◽  
High Affinity ◽  
Rat Hepatoma ◽  
Rat Hepatoma Cells

The rat hepatoma cell line H4-II-E was found to express much higher activities of Na+-dependent glutamine and aspartate transport than those observed in normal cultured hepatocytes, in agreement with previous work of others on human hepatocytes. Na+-dependent glutamine transport in rat hepatoma cells could be resolved into two components. One was pH-dependent, tolerated Li+ for Na+ substitution and was inhibited only by asparagine and histidine; characteristics similar to those of transport System N in hepatocytes. The other transport system had a similar Km for glutamine but was pH independent, did not accept Li+ ions and was completely inhibited by excess concentrations of lysine, histidine, leucine, serine and cysteine, but not by methyl-aminoisobutyrate or phenylalanine. This pattern of inhibition is distinct from that of any transporter occurring in normal hepatocytes and may indicate the presence of a new transporter isoform. Similar results were obtained with the cell line HTC. Na+-dependent aspartate transport in H4 hepatoma cells was mediated by a high-affinity system (Km 5 μM) and was inhibited by D-aspartate and L-glutamate but not by D-glutamate - properties characteristic of the high-affinity glutamate transporter EAAC1. C-terminal antibodies to the EAAC1 protein recognized a single band of 58 kDa in hepatocyte membranes, but an additional strong band of 60 kDa was present in H4 hepatoma cells. These results provide further evidence for the view that tumour cells may express additional isoforms of amino acid transport systems which are not present in non-transformed cells.

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