Influence of rBAT-Mediated Amino Acid Transport on Cytosolic pH
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Moschen, I; Setiawan, Iwan; Palacin, Manuel; Broer, Stefan; Albers, Alexandra; Lang, Florian
Description
rBAT, together with its subunit b0,+ AT mediates the hetero- and homoexchange of neutral and dibasic amino acids. Since the heteroexchange of dibasic amino acids against neutral amino acids is coupled to net transport of positive charge, this transport is electrogenic. Extracellular addition of histidine could create an inward or an outward current depending on extracellular pH (pHe) and cell membrane potential. It has been concluded that histidine may be transported in both its protonated and...[Show more]
dc.contributor.author | Moschen, I | |
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dc.contributor.author | Setiawan, Iwan | |
dc.contributor.author | Palacin, Manuel | |
dc.contributor.author | Broer, Stefan | |
dc.contributor.author | Albers, Alexandra | |
dc.contributor.author | Lang, Florian | |
dc.date.accessioned | 2015-12-07T22:44:57Z | |
dc.date.available | 2015-12-07T22:44:57Z | |
dc.identifier.issn | 0028-2766 | |
dc.identifier.uri | http://hdl.handle.net/1885/25419 | |
dc.description.abstract | rBAT, together with its subunit b0,+ AT mediates the hetero- and homoexchange of neutral and dibasic amino acids. Since the heteroexchange of dibasic amino acids against neutral amino acids is coupled to net transport of positive charge, this transport is electrogenic. Extracellular addition of histidine could create an inward or an outward current depending on extracellular pH (pHe) and cell membrane potential. It has been concluded that histidine may be transported in both its protonated and its neutral form. In this study measurements of cytosolic pH (pHi) were performed to test this hypothesis. As a result, addition of protonated histidine at acidic pHe to Xenopus oocytes expressing rBAT creates an inward current which is paralleled by cytosolic acidification. Both can be reduced by increase of pHe. At alkaline pHe and simultaneous depolarization of the cell membrane the effect of histidine on pHi is virtually abolished. The neutral amino acid leucine does not alter cytosolic pH at neither pH 6.0 nor at pH 8.0. In conclusion, histidine can be transported in either its neutral or its protonated form. Transport of the protonated form is facilitated by extracellular acidification and hyperpolarization of the cell membrane. | |
dc.publisher | S Karger AG | |
dc.source | Nephron Journals, The | |
dc.subject | Keywords: amino acid; histidine; leucine; protein; protein rbat; unclassified drug; carrier protein; ion channel; membrane protein; mitochondrial protein; mitochondrial uncoupling protein; recombinant protein; acidification; acidity; alkalinity; amino acid transpor Amino acid transport; Cystinuria; Histidine; Proximal tubule; rBAT; Xenopus oocytes | |
dc.title | Influence of rBAT-Mediated Amino Acid Transport on Cytosolic pH | |
dc.type | Journal article | |
local.description.notes | Imported from ARIES | |
local.identifier.citationvolume | 91 | |
dc.date.issued | 2002 | |
local.identifier.absfor | 060110 - Receptors and Membrane Biology | |
local.identifier.ariespublication | u4325460xPUB38 | |
local.type.status | Published Version | |
local.contributor.affiliation | Moschen, I, University of Tubingen | |
local.contributor.affiliation | Setiawan, Iwan, University of Tubingen | |
local.contributor.affiliation | Palacin, Manuel, Universidad de Barcelona | |
local.contributor.affiliation | Broer, Stefan, College of Medicine, Biology and Environment, ANU | |
local.contributor.affiliation | Albers, Alexandra, University of Tubingen | |
local.contributor.affiliation | Lang, Florian, University of Tubingen | |
local.bibliographicCitation.startpage | 631 | |
local.bibliographicCitation.lastpage | 636 | |
local.identifier.doi | 10.1159/000065024 | |
dc.date.updated | 2015-12-07T11:30:32Z | |
local.identifier.scopusID | 2-s2.0-0035995354 | |
Collections | ANU Research Publications |
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