Uptake and release of [3H]formycin B via sodium-dependent nucleoside transporters in mouse leukemic L1210/MA27.1 cells.
Identifieur interne : 003A62 ( Main/Exploration ); précédent : 003A61; suivant : 003A63Uptake and release of [3H]formycin B via sodium-dependent nucleoside transporters in mouse leukemic L1210/MA27.1 cells.
Auteurs : S L Borgland [Canada] ; F E ParkinsonSource :
- The Journal of pharmacology and experimental therapeutics [ 0022-3565 ] ; 1997.
English descriptors
- KwdEn :
- Adenosine Triphosphate (analysis), Animals, Antibiotics, Antineoplastic (pharmacokinetics), Carrier Proteins (physiology), Formycins (pharmacokinetics), Leukemia L1210 (metabolism), Membrane Proteins (physiology), Mice, Nucleoside Transport Proteins, Sodium (physiology), Sodium-Potassium-Exchanging ATPase (physiology), Tumor Cells, Cultured.
- MESH :
- chemical , analysis : Adenosine Triphosphate.
- chemical , pharmacokinetics : Antibiotics, Antineoplastic, Formycins.
- chemical , physiology : Carrier Proteins, Membrane Proteins, Sodium, Sodium-Potassium-Exchanging ATPase.
- metabolism : Leukemia L1210.
- Animals, Mice, Nucleoside Transport Proteins, Tumor Cells, Cultured.
Abstract
At least seven functionally distinct nucleoside transport processes exist; however, mouse leukemic L1210/MA27.1 cells possess only one subtype, a Na+-dependent transporter termed N1/cif. The capacity of this transporter subtype to release nucleosides from L1210/MA27.1 cells was investigated with the poorly metabolized inosine analog [3H]formycin B. Uptake of [3H]formycin B into these cells was inhibited by replacement of Na+ in the buffer with choline, or by blocking Na+/K+ ATPase with 2 mM ouabain, inhibiting glycolysis with 5 mM iodoacetic acid or inhibiting nucleoside transport with 1 mM phloridzin. Sodium stimulated uptake with an EC50 value of 12 mM. To measure release of [3H]formycin B, cells were loaded with [3H]formycin B (10 microM) then washed and resuspended in buffer. Replacement of Na+ in the buffer with choline enhanced [3H]formycin B release by 20 to 47%, and significant stimulation of release was observed with Na+ concentrations of 30 mM or less. Resuspending loaded cells into Na+ buffer containing 2 mM ouabain or 10 microM monensin, a Na+ ionophore, significantly enhanced [3H]formycin B release during 20 min by 39% or 29%, respectively. Release of [3H]formycin B into choline buffer was inhibited 26.5% by 10 mM phloridzin and 39.6% by 10 mM propentofylline, compounds known to inhibit various transporters including Na+-dependent nucleoside transporters. Release was also inhibited significantly by 100 microM concentrations of dilazep, dipyridamole and nitrobenzylthioinosine, inhibitors with selectivity for Na+-independent nucleoside transporters. In the absence of Na+, the permeants adenosine and uridine enhanced [3H]formycin B release by up to 40.9% and 21.4%, respectively. These data indicate that in the absence of an inwardly directed Na+ gradient, Na+-dependent nucleoside transporters can function in the release of nucleosides.
PubMed: 9103516
Affiliations:
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Le document en format XML
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Uptake and release of [3H]formycin B via sodium-dependent nucleoside transporters in mouse leukemic L1210/MA27.1 cells.</title>
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<series><title level="j">The Journal of pharmacology and experimental therapeutics</title>
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<term>Carrier Proteins (physiology)</term>
<term>Formycins (pharmacokinetics)</term>
<term>Leukemia L1210 (metabolism)</term>
<term>Membrane Proteins (physiology)</term>
<term>Mice</term>
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<term>Sodium-Potassium-Exchanging ATPase (physiology)</term>
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<term>Sodium</term>
<term>Sodium-Potassium-Exchanging ATPase</term>
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<front><div type="abstract" xml:lang="en">At least seven functionally distinct nucleoside transport processes exist; however, mouse leukemic L1210/MA27.1 cells possess only one subtype, a Na+-dependent transporter termed N1/cif. The capacity of this transporter subtype to release nucleosides from L1210/MA27.1 cells was investigated with the poorly metabolized inosine analog [3H]formycin B. Uptake of [3H]formycin B into these cells was inhibited by replacement of Na+ in the buffer with choline, or by blocking Na+/K+ ATPase with 2 mM ouabain, inhibiting glycolysis with 5 mM iodoacetic acid or inhibiting nucleoside transport with 1 mM phloridzin. Sodium stimulated uptake with an EC50 value of 12 mM. To measure release of [3H]formycin B, cells were loaded with [3H]formycin B (10 microM) then washed and resuspended in buffer. Replacement of Na+ in the buffer with choline enhanced [3H]formycin B release by 20 to 47%, and significant stimulation of release was observed with Na+ concentrations of 30 mM or less. Resuspending loaded cells into Na+ buffer containing 2 mM ouabain or 10 microM monensin, a Na+ ionophore, significantly enhanced [3H]formycin B release during 20 min by 39% or 29%, respectively. Release of [3H]formycin B into choline buffer was inhibited 26.5% by 10 mM phloridzin and 39.6% by 10 mM propentofylline, compounds known to inhibit various transporters including Na+-dependent nucleoside transporters. Release was also inhibited significantly by 100 microM concentrations of dilazep, dipyridamole and nitrobenzylthioinosine, inhibitors with selectivity for Na+-independent nucleoside transporters. In the absence of Na+, the permeants adenosine and uridine enhanced [3H]formycin B release by up to 40.9% and 21.4%, respectively. These data indicate that in the absence of an inwardly directed Na+ gradient, Na+-dependent nucleoside transporters can function in the release of nucleosides.</div>
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<tree><noCountry><name sortKey="Parkinson, F E" sort="Parkinson, F E" uniqKey="Parkinson F" first="F E" last="Parkinson">F E Parkinson</name>
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<country name="Canada"><region name="Manitoba"><name sortKey="Borgland, S L" sort="Borgland, S L" uniqKey="Borgland S" first="S L" last="Borgland">S L Borgland</name>
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