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 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.

TGF-β transcriptionally activates the gene encoding the high-affinity adenosine transporter CNT2 in rat liver parenchymal cells

2006 ◽  
Vol 63 (21) ◽  
pp. 2527-2537 ◽  
Author(s):  
R. Valdés ◽  
S. Fernández-Veledo ◽  
I. Aymerich ◽  
F. J. Casado ◽  
M. Pastor-Anglada
Keyword(s):  
Rat Liver ◽  
Gene Encoding ◽  
Liver Parenchymal ◽  
High Affinity ◽  
Parenchymal Cells

The concentrative nucleoside transporter family (SLC28): new roles beyond salvage?

2005 ◽  
Vol 33 (1) ◽  
pp. 216-219 ◽  
Author(s):  
I. Aymerich ◽  
S. Duflot ◽  
S. Fernández-Veledo ◽  
E. Guillén-Gómez ◽  
I. Huber-Ruano ◽  
...  
Keyword(s):  
Cell Cycle Progression ◽  
Cell Physiology ◽  
Nucleoside Transporter ◽  
Cycle Progression ◽  
Suitable Candidate ◽  
Concentrative Nucleoside Transporter ◽  
Transporter Family ◽  
Nucleoside Salvage ◽  
Parenchymal Cells ◽  
Regulatory Properties

The concentrative nucleoside transporter (CNT) family (SLC28) has three members: SLC28A1 (CNT1), SLC28A2 (CNT2) and SLC28A3 (CNT3). The CNT1 and CNT2 transporters are co-expressed in liver parenchymal cells and macrophages, two suitable models in which to study cell cycle progression. Despite initial observations suggesting that these transporter proteins might contribute to nucleoside salvage during proliferation, their subcellular localization and regulatory properties suggest alternative roles in cell physiology. In particular, CNT2 is a suitable candidate for modulation of purinergic responses, since it is under the control of the adenosine 1 receptor. Increasing evidence also suggests a role for CNT2 in energy metabolism, since its activation relies on the opening of ATP-sensitive K+ channels. Animal and cell models genetically modified to alter nucleoside transporter expression levels may help to elucidate the particular roles of CNT proteins in cell physiology.

scholarly journals Induction of amino acid transport in primary cultures of adult rat liver parenchymal cells by insulin.

1976 ◽  
Vol 251 (10) ◽  
pp. 3014-3020 ◽  
Author(s):  
R F Kletzien ◽  
M W Pariza ◽  
J E Becker ◽  
V R Potter ◽  
F R Butcher
Keyword(s):  
Amino Acid ◽  
Rat Liver ◽  
Amino Acid Transport ◽  
Primary Cultures ◽  
Acid Transport ◽  
Liver Parenchymal ◽  
Adult Rat ◽  
Parenchymal Cells
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