scholarly journals Hormonal regulation of concentrative nucleoside transport in liver parenchymal cells

1996 ◽  
Vol 313 (3) ◽  
pp. 915-920 ◽  
Author(s):  
Mireia GOMEZ-ANGELATS ◽  
Belén del SANTO ◽  
Joan MERCADER ◽  
Andreu FERRER-MARTINEZ ◽  
Antonio FELIPE ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Cyclic Amp ◽  
Hormonal Regulation ◽  
Nucleoside Transporter ◽  
Dibutyryl Cyclic Amp ◽  
Liver Parenchymal ◽  
Uridine Uptake ◽  
Concentrative Nucleoside Transporter ◽  
Hormonal Modulation ◽  
Parenchymal Cells

Na+-dependent uridine uptake is stimulated in isolated rat liver parenchymal cells by glucagon. This effect is transient, reaches maximum levels of stimulation 10 min after hormone addition, and is dose-dependent. Glucagon action can be mimicked by agents that are able to hyperpolarize the plasma membrane (e.g. monensin) and by dibutyryl cyclic AMP. The effects triggered by glucagon, monensin and dibutyryl cyclic AMP are not additive, suggesting a common mechanism of action. 8-(4-Chlorophenylthio)adenosine 3´:5´-cyclic monophosphate (PCT), a cyclic AMP analogue but also a nucleoside analogue, markedly stimulates Na+-dependent uridine uptake in an additive manner to that triggered by monensin, similarly to the effect described for nitrobenzylthioinosine. Considering the roles reported for nucleosides in liver metabolism, the use of PCT as a cyclic AMP analogue should be precluded. Insulin is also able to up-regulate Na+-dependent uridine uptake by a mechanism which involves a stable induction of this transport activity at the plasma-membrane level. This is consistent with a mechanism involving synthesis and insertion of more carriers into the plasma membrane. It is concluded that the recently characterized hepatic concentrative nucleoside transporter is under short-term hormonal regulation by glucagon, through mechanisms which involve membrane hyperpolarization, and under long-term control by insulin. This is the first report showing hormonal modulation of the hepatic concentrative nucleoside transporter.

scholarly journals Regulation of coenzyme A biosynthesis by glucagon and glucocorticoid in adult rat liver parenchymal cells

1980 ◽  
Vol 188 (1) ◽  
pp. 175-184 ◽  
Author(s):  
Colleen M. Smith ◽  
C. Richard Savage
Keyword(s):  
Cyclic Amp ◽  
Rat Liver ◽  
Maximum Effect ◽  
Maximal Effect ◽  
Dibutyryl Cyclic Amp ◽  
Liver Parenchymal ◽  
Adult Rat ◽  
Intracellular Mechanism ◽  
Inhibitor Of Protein Synthesis ◽  
Parenchymal Cells

We studied the effects of glucagon, dibutyryl cyclic AMP and dexamethasone on the rate of [14C]pantothenate conversion to CoA in adult rat liver parenchymal cells in primary culture. The presence of 30nm-glucagon increased the rate by about 1.5-fold relative to control cultures (range 1.4–2.3) and 2.4-fold relative to cultures containing 1–3m-i.u. of insulin/ml. The half-maximal effect was obtained at 3nm-glucagon. Dibutyryl cyclic AMP plus theophylline also enhanced the rate by about 1.5-fold. Dexamethasone acted synergistically with glucagon; glucagon at 0.3nm had no effect when added alone, but resulted in a 1.7-fold enhancement when added in the presence of dexamethasone (maximum effect at 50nm). The 1.4-fold enhancement caused by the addition of saturating glucagon concentrations was increased to a 3-fold overall enhancement by the addition of dexamethasone. However, dexamethasone added alone over the range 5nm to 5μm had no effect on the rate of [14C]pantothenate conversion to CoA. The stimulatory effect of dibutyryl cyclic AMP plus theophylline was also enhanced by the addition of dexamethasone. Changes in intracellular pantothenate concentration or radioactivity could not account for the stimulatory effects of glucagon, dibutyryl cyclic AMP or dexamethasone. Addition of 18μm-cycloheximide, an inhibitor of protein synthesis, decreased the rate of incorporation of [14C]pantothenate into CoA and the enhancement of this rate by glucagon and dibutyryl cyclic AMP plus theophylline in a reversible manner. These results demonstrate an influence of glucagon, dibutyryl cyclic AMP and glucocorticoids on the intracellular mechanism regulating total CoA concentrations in the liver.

Link between high-affinity adenosine concentrative nucleoside transporter-2 (CNT2) and energy metabolism in intestinal and liver parenchymal cells

2010 ◽  
Vol 225 (2) ◽  
pp. 620-630 ◽  
Author(s):  
Isabel Huber-Ruano ◽  
Itziar Pinilla-Macua ◽  
Gonzalo Torres ◽  
F. Javier Casado ◽  
Marçal Pastor-Anglada
Keyword(s):  
Energy Metabolism ◽  
Nucleoside Transporter ◽  
Liver Parenchymal ◽  
High Affinity ◽  
Concentrative Nucleoside Transporter ◽  
Parenchymal Cells

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.

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