scholarly journals Glycine transport into plasma-membrane vesicles derived from rat brain synaptosomes

1981 ◽  
Vol 198 (3) ◽  
pp. 535-541 ◽  
Author(s):  
F Mayor ◽  
J G Marvizón ◽  
M C Aragón ◽  
C Gimenez ◽  
F Valdivieso
Keyword(s):  
Rat Brain ◽  
Membrane Vesicles ◽  
Uptake System ◽  
Plasma Membrane Vesicles ◽  
Glycine Uptake ◽  
High Affinity ◽  
Carbonyl Cyanide ◽  
Brain Synaptosomes ◽  
Glycine Transport ◽  
Sole Energy

1. Transport of glycine has been demonstrated in membrane vesicles isolated from rat brain, using artificially imposed ion gradients as the sole energy source. 2. The uptake of glycine is strictly dependent on the presence of Na+ and Cl- in the medium, and the process can be driven either by an Na+ gradient (out greater than in) or by a C1- gradient (out greater than in) when the other essential ion is present. 3. The uptake of glycine is stimulated by a membrane potential (interior negative), as demonstrated by the effects of the ionophores valinomycin and carbonyl cyanide m-chlorophenylhydrazone and anions of different permeabilities. 4. The kinetic analysis shows that glycine is accumulated by two systems with different affinities. 5. The presence of ouabain, an inhibitor (Na+ + K+)-activated ATPase, does not affect glycine transport. 6. The existence of a high-affinity, Na+-dependent glycine-uptake system in membrane vesicles derived from rat brain suggests that this amino acid may have a transmitter role in some areas of the rat brain.

L-Aspartate Transport into Plasma Membrane Vesicles Derived from Rat Brain Synaptosomes

1981 ◽  
Vol 37 (6) ◽  
pp. 1401-1406 ◽  
Author(s):  
J. G. Marvizón ◽  
F. Mayor ◽  
M. C. Aragón ◽  
C. Giménez ◽  
F. Valdivieso
Keyword(s):  
Plasma Membrane ◽  
Rat Brain ◽  
Membrane Vesicles ◽  
Plasma Membrane Vesicles ◽  
Rat Brain Synaptosomes ◽  
Brain Synaptosomes

?-Alanine transport into plasma membrane vesicles derived from rat brain synaptosomes

1984 ◽  
Vol 9 (5) ◽  
pp. 695-707 ◽  
Author(s):  
Francisco Zafra ◽  
M. Carmen Aragon ◽  
Fernando Valdivieso ◽  
Cecilio Gimenez
Keyword(s):  
Plasma Membrane ◽  
Rat Brain ◽  
Membrane Vesicles ◽  
Plasma Membrane Vesicles ◽  
Rat Brain Synaptosomes ◽  
Alanine Transport ◽  
Brain Synaptosomes

Na+-glycine cotransport in canalicular liver plasma membrane vesicles

1988 ◽  
Vol 255 (2) ◽  
pp. G253-G259 ◽  
Author(s):  
R. H. Moseley ◽  
N. Ballatori ◽  
S. M. Murphy
Keyword(s):  
Plasma Membrane ◽  
Amino Acid ◽  
Driving Forces ◽  
High Capacity ◽  
Membrane Vesicles ◽  
Transport Systems ◽  
Plasma Membrane Vesicles ◽  
Glycine Uptake ◽  
Liver Plasma Membrane ◽  
Glycine Transport

By use of purified rat canalicular liver plasma membrane (cLPM) vesicles, the present study determined the driving forces for glycine transport across this membrane domain. Initial rates of [3H]glycine uptake (10 microM) in cLPM vesicles were stimulated by an inwardly directed Na+ gradient but not by a K+ gradient. Na+ gradient-dependent uptake of glycine demonstrated cation specificity for Na+, dependence on extravesicular Cl-, stimulation by an intravesicular-negative membrane potential, and inhibition by dissipation of the Na+ gradient with gramicidin D. Na+ gradient-dependent glycine cotransport also demonstrated greater sensitivity to inhibition by sarcosine than 2-(methylamino)-isobutyric acid. Accelerated exchange diffusion of [3H]glycine was demonstrated in the presence of Na+ when cLPM vesicles were preloaded with glycine but not with L-alanine or L-proline. Substrate velocity analysis of net Na+-dependent [3H]glycine uptake over the range of amino acid concentrations from 5 microM to 5 mM demonstrated two saturable transport systems, one of high capacity (2.2 +/- 0.2 nmol.mg protein-1.15 s-1) and low affinity (11.2 +/- 1.7 mM) and one of low capacity (51 +/- 14 pmol.mg protein.15 s-1) and comparatively high affinity (66 +/- 12 microM). These results indicate that, in addition to previously described neutral and anionic amino acid transport systems, Na+ gradient-dependent glycine transport mechanisms are present on the canalicular domain of the liver plasma membrane. These canalicular reabsorptive mechanisms may serve to reclaim some of the glycine generated within the canalicular lumen from the intrabiliary hydrolysis of glutathione.

Na(+)-dependent and Na(+)-independent systems of choline transport by plasma membrane vesicles of A549 cell line

1994 ◽  
Vol 267 (5) ◽  
pp. C1279-C1287 ◽  
Author(s):  
A. Kleinzeller ◽  
C. Dodia ◽  
A. Chander ◽  
A. B. Fisher
Keyword(s):  
A549 Cells ◽  
Membrane Vesicles ◽  
Choline Uptake ◽  
Plasma Membrane Vesicles ◽  
Choline Transport ◽  
High Affinity ◽  
A Value ◽  
Carbonyl Cyanide ◽  
Rate Limiting ◽  
A549 Lung

Membrane vesicles of A549 lung cells accumulate choline by two pathways: the Na(+)-independent uphill uptake of choline [Michaelis-Menten constant (Km) approximately 44 microM; steady-state gradient approximately 45 at 5 microM external choline] is dependent on a transmembrane H+ gradient, is relatively insensitive to hemicholinium-3, is amiloride sensitive, and is abolished by valinomycin plus carbonyl cyanide p-trifluoromethoxyphenylhydrazone (FCCP). The Na(+)-dependent active choline uptake (Km approximately 4 microM, inhibitor constant for hemicholinium-3 approximately 0.1 microM), is specific for Na+, is amiloride and FCCP sensitive, and is electrogenic: the overshoot using K(+)-loaded vesicles and NaCl gradient was increased by valinomycin. The time of the overshoot peak, T was approximately 90 s in a NaSCN medium (or in presence of other lipid-soluble anions), a value close to that for alpha-aminoisobutyrate as substrate (T = approximately 1.5 min). T was lengthened in NaCl medium to approximately 10 min, and the overshoot was abolished by impermeant anions. External Cl- is not required for the choline uptake: valinomycin produced an overshoot in the presence of only impermeant anions, with T approximately 90 s. Most of the above properties are shared by the high-affinity Na(+)-dependent choline transport in synaptosomes. The characteristics of the Na(+)-dependent choline uptake by membrane vesicles of A549 cells are consistent with an electrogenic choline(+)-Na+ cotransport, with the rate-limiting anion (e.g., Cl-) influx balancing the positive charges transferred into the vesicles. The data are also consistent with an involvement of an amiloride-sensitive choline+/H+ antiport (or choline(+)-OH- symport) in the low- and high-affinity choline uptake pathways.

A High-Affinity, Na+-Dependent Uptake System for ?-Hydroxybutyrate in Membrane Vesicles Prepared from Rat Brain

1982 ◽  
Vol 38 (6) ◽  
pp. 1570-1575 ◽  
Author(s):  
J. Benavides ◽  
J. F. Rumigny ◽  
J. J. Bourguignon ◽  
C. G. Wermuth ◽  
P. Mandel ◽  
...  
Keyword(s):  
Rat Brain ◽  
Membrane Vesicles ◽  
Uptake System ◽  
High Affinity

Ontogenetic studies on tryptophan transport into plasma membrane vesicles derived from rat brain synaptosomes: Effect of thyroid hormones

1985 ◽  
Vol 10 (5) ◽  
pp. 579-589 ◽  
Author(s):  
Elisa Herrero ◽  
M. Carmen Aragon ◽  
Javier Diez-Guerra ◽  
Fernando Valdivieso ◽  
Cecilio Gimenez
Keyword(s):  
Plasma Membrane ◽  
Thyroid Hormones ◽  
Rat Brain ◽  
Membrane Vesicles ◽  
Plasma Membrane Vesicles ◽  
Rat Brain Synaptosomes ◽  
Brain Synaptosomes ◽  
Tryptophan Transport
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