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Kwon, Hyug Moo
Immunometabolism and Cancer Lab
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  • TonEBP, Obesity, Cancer, Chronic inflammatory diseases, Brain disorder, Kidney disorder, Genomic instability

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Functional characterization of the betaine/gamma-aminobutyric acid transporter BGT-1 expressed in Xenopus oocytes

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dc.contributor.author Matskevitch, I ko
dc.contributor.author Wagner, CA ko
dc.contributor.author Stegen, C ko
dc.contributor.author Broer, S ko
dc.contributor.author Noll, B ko
dc.contributor.author Risler, T ko
dc.contributor.author Kwon, HM ko
dc.contributor.author Handler, JS ko
dc.contributor.author Waldegger, S ko
dc.contributor.author Busch, AE ko
dc.contributor.author Lang, F ko
dc.date.available 2014-05-23T04:21:56Z -
dc.date.created 2014-05-23 ko
dc.date.issued 1999-06 ko
dc.identifier.citation JOURNAL OF BIOLOGICAL CHEMISTRY, v.274, no.24, pp.16709 - 16716 ko
dc.identifier.issn 0021-9258 ko
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/4739 -
dc.description.abstract Betaine is an osmolyte accumulated in cells during osmotic cell shrinkage. The canine transporter mediating cellular accumulation of the osmolyte betaine and the neurotransmitter γ-aminobutyric acid (BGT-1) was expressed in Xenopus oocytes and analyzed by two-electrode voltage clamp and tracer flux studies. Exposure of oocytes expressing BGT-1 to betaine or γ- aminobutyric acid (GABA) depolarized the cell membrane in the current clamp mode and induced an inward current under voltage clamp conditions. At 1 mM substrate the induced currents decreased in the following order: betaine = GABA > diaminobutyric acid = β-alanine > proline = quinidine > dimethylglycine > glycine > sarcosine. Both the V(max) and K(m) of GABA- and betaine-induced currents were voltage-dependent, and GABA- and betaine- induced currents and radioactive tracer uptake were strictly Na+-dependent but only partially dependent on the presence of Cl-. The apparent affinity of GABA decreased with decreasing Na+ concentrations. The K(m) of Na+ also depended on the GABA and Cl-concentration. A decrease of the Cl- concentration reduced the apparent affinity for Na+ and GABA, and a decrease of the Na+ concentration reduced the apparent affinity for Cl- and GABA. A comparison of 22Na+-, 36Cl-, and 14C-labeled GABA and 14C-labeled betaine fluxes and GABA- and betaine-induced currents yielded a coupling ratio of Na+/Cl-/organic substrate of 3:1:1 or 3:2:1. Based on the data, a transport model of ordered binding is proposed in which GABA binds first, Na+ second, and Cl- third. In conclusion, BGT-1 displays significant functional differences from the other members of the GABA transporter family. ko
dc.description.statementofresponsibility close -
dc.language 영어 ko
dc.publisher AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC ko
dc.title Functional characterization of the betaine/gamma-aminobutyric acid transporter BGT-1 expressed in Xenopus oocytes ko
dc.type ARTICLE ko
dc.identifier.scopusid 2-s2.0-0033546413 ko
dc.identifier.wosid 000080780400009 ko
dc.type.rims ART ko
dc.description.wostc 47 *
dc.description.scopustc 46 *
dc.date.tcdate 2014-10-18 *
dc.date.scptcdate 2014-07-12 *
dc.identifier.doi 10.1074/jbc.274.24.16709 ko
dc.identifier.url http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0033546413 ko
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