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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1977-5-20
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pubmed:abstractText |
Selectively permeable membrane vesicles isolated from Simian virus 40-transformed mouse fibroblasts catalyzed Na+ gradient-coupled active transport of several neutral amino acids dissociated from intracellular metabolism. Na+-stimulated alanine transport activity accompanied plasma membrane material during centrifugation in discontinuous dextran 110 gradients. Carrier-mediated transport into the vesicle was demonstrated. When Na+ was equilibrated across the membrane, countertransport stimulation of L-[3H]alanine uptake occurred in the presence of accumulated unlabeled L-alanine, 2-aminoisobutyric acid, or L-methionine. Competitive interactions among neutral amino acids, pH profiles, and apparent Km values for Na+ gradient-stimulated transport into vesicles were similar to those previously described for amino acid uptake in Ehrlich ascites cells, which suggests that the transport activity assayed in vesicles is a component of the corresponding cellular uptake process. Both the initial rate and quasi-steady state of uptake were stimulated as a function of a Na+ gradient (external Na+ greater than internal Na+) applied artificially across the membrane and were independent of endogenous (Na+ + K+)-ATPase activity. Stimulation by Na+ was decreased when the Na+ gradient was dissipated by monensin, gramicidin D or Na+ preincubation. Na+ decreased the apparent Km for alanine, 2-aminoisobutyric acid, and glutamine transport. Na+ gradient-stimulated amino acid transport was electrogenic, stimulated by conditions expected to generate an interior-negative membrane potential, such as the presence of the permeant anions NO3- and SCN-. Na+-stimulated L-alanine transport was also stimulated by an electrogenic potassium diffusion potential (K+ internal greater than K+ external) catalyzed by valinomycin; this stimulation was blocked by nigericin. These observations provide support for a mechanism of active neutral amino acid transport via the "A system" of the plasma membrane in which both a Na+ gradient and membrane potential contribute to the total driving force.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Cations, Monovalent,
http://linkedlifedata.com/resource/pubmed/chemical/Gramicidin,
http://linkedlifedata.com/resource/pubmed/chemical/Ouabain,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium,
http://linkedlifedata.com/resource/pubmed/chemical/Valinomycin
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
252
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1990-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:66232-Amino Acids,
pubmed-meshheading:66232-Biological Transport, Active,
pubmed-meshheading:66232-Cations, Monovalent,
pubmed-meshheading:66232-Cell Line,
pubmed-meshheading:66232-Cell Membrane,
pubmed-meshheading:66232-Cell Transformation, Neoplastic,
pubmed-meshheading:66232-Endoplasmic Reticulum,
pubmed-meshheading:66232-Fibroblasts,
pubmed-meshheading:66232-Gramicidin,
pubmed-meshheading:66232-Hydrogen-Ion Concentration,
pubmed-meshheading:66232-Kinetics,
pubmed-meshheading:66232-Ouabain,
pubmed-meshheading:66232-Potassium,
pubmed-meshheading:66232-Simian virus 40,
pubmed-meshheading:66232-Sodium,
pubmed-meshheading:66232-Temperature,
pubmed-meshheading:66232-Valinomycin
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pubmed:year |
1977
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pubmed:articleTitle |
Active amino acid transport in plasma membrane vesicles from Simian virus 40-transformed mouse fibroblasts. Characteristics of electrochemical Na+ gradient-stimulated uptake.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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