scholarly journals Fish oil fatty acids impair VLDL assembly and/or secretion by cultured rat hepatocytes.

1990 ◽  
Vol 31 (11) ◽  
pp. 2079-2086
Author(s):  
CA Lang ◽  
RA Davis
Keyword(s):  
Fatty Acids ◽  
Fish Oil ◽  
Rat Hepatocytes ◽  
Cultured Rat Hepatocytes ◽  
Vldl Assembly

High Peroxidative Susceptibility of Fish Oil Polyunsaturated Fatty Acid in Cultured Rat Hepatocytes

1994 ◽  
Vol 126 (1) ◽  
pp. 124-128 ◽  
Author(s):  
N. Sugihara ◽  
Y. Tsuruta ◽  
Y. Date ◽  
K. Furuno ◽  
K. Kohashi
Keyword(s):  
Fatty Acid ◽  
Fish Oil ◽  
Polyunsaturated Fatty Acid ◽  
Rat Hepatocytes ◽  
Cultured Rat Hepatocytes

scholarly journals Albumin stimulates the release of lysophosphatidylcholine from cultured rat hepatocytes

1988 ◽  
Vol 253 (3) ◽  
pp. 693-701 ◽  
Author(s):  
D J Baisted ◽  
B S Robinson ◽  
D E Vance
Keyword(s):  
Fatty Acids ◽  
Fatty Acid Composition ◽  
Unsaturated Fatty Acids ◽  
Rat Hepatocytes ◽  
Water Soluble ◽  
Measurable Effect ◽  
Rat Hepatocyte ◽  
Low Concentrations ◽  
Cultured Rat Hepatocytes ◽  
Secreted Enzymes

The effect of albumin on the release of [3H]lysophosphatidylcholine from cultured rat hepatocytes prelabelled with [Me-3H]choline was studied. In the absence of serum and albumin from the medium, the cells released essentially no [3H]lysophosphatidylcholine. Albumin stimulated this process dramatically, and it reached a plateau at 2 mg/ml. After an initial lag of 30 min, the release of [3H]lysophosphatidylcholine was linear for at least 4 h. At low concentrations, albumin slightly stimulated [3H]phosphatidylcholine release. The albumin had no measurable effect on the metabolism of cellular [3H]phosphatidylcholine, [3H]lysophosphatidylcholine or [3H]glycerophosphocholine. In addition, albumin did not alter the release of 3H-labelled water-soluble compounds, including [3H]glycerophosphocholine, into the medium. The possibility that the [3H]lysophosphatidylcholine was arising from catabolism of [3H]phosphatidylcholine in the medium by secreted enzymes was excluded. The effect on [3H]lysophosphatidylcholine secretion was also observed when the cells were incubated with alpha-cyclodextrin, a cyclic polysaccharide that has the ability to bind lysophosphatidylcholine. The albumin-released lysophosphatidylcholine was enriched in unsaturated fatty acids. Alteration of the fatty acid composition of cellular phosphatidylcholine gave rise to parallel changes in phosphatidylcholine and lysophosphatidylcholine in the medium. It is concluded that phosphatidylcholine is constantly being degraded in the rat hepatocyte to lysophosphatidylcholine which is released into the medium only when a suitable acceptor is present.

scholarly journals Evidence for dissociation of gluconeogenesis stimulated by non-esterified fatty acids and changes in fructose 2,6-bisphosphate in cultured rat hepatocytes

1992 ◽  
Vol 288 (1) ◽  
pp. 145-148 ◽  
Author(s):  
J N Clore ◽  
J S Stillman ◽  
S T Helm ◽  
W G Blackard
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Glucose Production ◽  
Rat Hepatocytes ◽  
Inhibitory Effect ◽  
Fed State ◽  
Palmitate Oxidation ◽  
Lower Glucose ◽  
The Media ◽  
Cultured Rat Hepatocytes

In order to examine the role of fructose 2,6-bisphosphate (Fru-2,6-P2) in non-esterified-fatty-acid-stimulated gluconeogenesis, Fru-2,6-P2 levels were measured in cultured rat hepatocytes under conditions mimicking the fasted state. After addition of either 1.5 mM-palmitate or 10 nM-glucagon, [U-14C]lactate incorporation into glucose increased 2-fold, but only glucagon suppressed Fru-2,6-P2. Prevention of palmitate oxidation with a carnitine palmitoyltransferase-I inhibitor (2-bromopalmitate) diminished glucose production and Fru-2,6-P2 levels. Addition of exogenous glucose to the media increased Fru-2,6-P2 in a dose-related manner, which was further augmented by addition of palmitate. When Fru-2,6-P2 levels were examined in cells cultured under conditions mimicking the fed state (significantly higher basal Fru-2,6-P2 levels and lower glucose production), palmitate oxidation was associated with a significant fall in Fru-2,6-P2. In conclusion, the present studies have demonstrated a dissociation between fatty-acid-stimulated gluconeogenesis and changes in Fru-2,6-P2 in cultured rat hepatocytes. Further experiments suggest that the accumulation of intracellular hexose 6-phosphate as a result of fatty-acid-stimulated gluconeogenesis masks a putative inhibitory effect of fatty acids on Fru-2,6-P2 concentrations.

scholarly journals Comparison of albumin-mediated release of lysophosphatidylcholine and lysophosphatidylethanolamine from cultured rat hepatocytes

1989 ◽  
Vol 264 (1) ◽  
pp. 125-131 ◽  
Author(s):  
B S Robinson ◽  
D J Baisted ◽  
D E Vance
Keyword(s):  
Fatty Acids ◽  
Culture Medium ◽  
Unsaturated Fatty Acids ◽  
Rat Hepatocytes ◽  
Fatty Acyl ◽  
Detectable Change ◽  
Cultured Rat Hepatocytes

We have investigated the albumin-stimulated release from cultured rat hepatocytes of lysophosphatidylcholine derived from methylation of phosphatidylethanolamine and of lysophosphatidylethanolamine. In the absence [corrected] of albumin, neither lysophosphatidylethanolamine nor lysophosphatidylcholine was released into the culture medium. Albumin stimulated the accumulation of both phospholipids in the medium. After 2 h, 14.1 nmol of lysophosphatidylcholine and 2.0 nmol of lysophosphatidylethanolamine per 3 x 10(6) cells had accumulated in the medium. The rate of release of [3H]ethanolamine-labelled lysophosphatidylethanolamine was rapid in the first 2 h and then was decreased, whereas there was a 1 h lag in the release of [3H]ethanolamine-labelled lysophosphatidylcholine. This apparent lag probably reflected the time necessary for the synthesis of phosphatidylcholine from phosphatidylethanolamine in the cells. Albumin caused a decrease in labelled cellular lysophosphatidylethanolamine and lysophosphatidylcholine which only partially accounted for the accumulation of the labelled phospholipids in the medium. Albumin also stimulated the release of labelled phosphatidylethanolamine (almost 3-fold) and phosphatidylcholine (2-fold) into the medium. There was no detectable change in the labelling of the cellular pools of these phospholipids, most likely owing to the large amounts in the cells compared with the medium. The labelled lysophospholipids did not arise from catabolism of the parent phospholipid in the medium. Analysis of the fatty acids of the secreted lysophospholipids showed a preferential release of unsaturated fatty acyl species of lysophosphatidylcholine, whereas lysophosphatidylethanolamine contained similar amounts of saturated and unsaturated fatty acids.

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