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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1998-6-4
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pubmed:abstractText |
The properties are discussed of system y+L, a broad scope amino acid transporter which was first identified in human erythrocytes. System y+L exhibits two distinctive properties: (a) it can bind and translocate cationic and neutral amino acids, and (b) its specificity varies depending on the ionic composition of the medium. In Na+ medium, the half-saturation constant for L-lysine influx was 9.5 +/- 0.67 microM and the inhibition constant (Ki) for L-leucine was 10.7 +/- 0.72 microM. L-Leucine is the neutral amino acid that binds more powerfully, whereas smaller analogues, such as L-alanine and L-serine interact less strongly (the corresponding inhibition constants were Ki,Ala, 0.62 +/- 0.11 mM; Ki,Ser, 0.49 +/- 0.08 mM). In the presence of K+, the carrier functions as a cationic amino acid specific carrier, but Li+ is able to substitute for Na+ facilitating neutral amino acid binding. The effect of the inorganic cations is restricted to the recognition of neutral amino acids; translocation occurs at similar rates in the presence of Na+, K+ and Li+. The only structural feature that appears to impair translocation is bulkiness and substrates with half-saturation constants differing by more than 100-fold translocate at the same rate. This suggests that translocation is largely independent of the forces of interaction between the substrate and the carrier site. System y+L activity has been observed in Xenopus laevis oocytes injected with the cRNA for the heavy chain of the 4F2 human surface antigen. 4F2hc is an integral membrane protein with a single putative membrane-spanning domain and it remains to be clarified whether it is part of the transporter or an activator protein.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0958-0670
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
83
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
211-20
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9568481-Amino Acid Transport Systems,
pubmed-meshheading:9568481-Amino Acids,
pubmed-meshheading:9568481-Animals,
pubmed-meshheading:9568481-Biological Transport,
pubmed-meshheading:9568481-Carrier Proteins,
pubmed-meshheading:9568481-Cations, Monovalent,
pubmed-meshheading:9568481-Erythrocytes,
pubmed-meshheading:9568481-Humans,
pubmed-meshheading:9568481-Membrane Potentials,
pubmed-meshheading:9568481-Protein Binding,
pubmed-meshheading:9568481-Xenopus laevis
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pubmed:year |
1998
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pubmed:articleTitle |
System y+L: the broad scope and cation modulated amino acid transporter.
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pubmed:affiliation |
Programa de Fisiología y Biofísica, Facultad de Medicina, Universidad de Chile, Santiagó, Chile. rdeves@bitmed.med.uchile.cl
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pubmed:publicationType |
Journal Article,
In Vitro,
Review,
Research Support, Non-U.S. Gov't
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