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DC Field | Value | Language |
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dc.citation.endPage | 16716 | - |
dc.citation.number | 24 | - |
dc.citation.startPage | 16709 | - |
dc.citation.title | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.citation.volume | 274 | - |
dc.contributor.author | Matskevitch, I | - |
dc.contributor.author | Wagner, CA | - |
dc.contributor.author | Stegen, C | - |
dc.contributor.author | Broer, S | - |
dc.contributor.author | Noll, B | - |
dc.contributor.author | Risler, T | - |
dc.contributor.author | Kwon, HM | - |
dc.contributor.author | Handler, JS | - |
dc.contributor.author | Waldegger, S | - |
dc.contributor.author | Busch, AE | - |
dc.contributor.author | Lang, F | - |
dc.date.accessioned | 2023-12-22T12:11:22Z | - |
dc.date.available | 2023-12-22T12:11:22Z | - |
dc.date.created | 2014-05-23 | - |
dc.date.issued | 1999-06 | - |
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. | - |
dc.identifier.bibliographicCitation | JOURNAL OF BIOLOGICAL CHEMISTRY, v.274, no.24, pp.16709 - 16716 | - |
dc.identifier.doi | 10.1074/jbc.274.24.16709 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.scopusid | 2-s2.0-0033546413 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/4739 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0033546413 | - |
dc.identifier.wosid | 000080780400009 | - |
dc.language | 영어 | - |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | - |
dc.title | Functional characterization of the betaine/gamma-aminobutyric acid transporter BGT-1 expressed in Xenopus oocytes | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
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