title: Electrogenic L-histidine transport in neutral and basic amino acid transporter (NBAT)-expressing Xenopus laevis oocytes. Evidence for two functionally distinct transport mechanisms induced by NBAT expression.
abstract: We have investigated the neutral and basic amino acid transporter (NBAT)-induced transport of L-histidine in Xenopus laevis oocytes. Transport of L-histidine (pH 7.5) was electrogenic and Na+-dependent with a 14-fold increase in L-histidine- (1 mM) evoked current (I(His) = -14.7 +/- 1.5 nA) in NBAT-expressing oocytes compared with native (water-injected or uninjected) oocytes (-1.0 +/- 0.2 nA); the Na+-dependent histidine transport showed a stoichiometry of 1:1 (histidine:sodium). I(His) was stereospecific at pH 7.5 and saturable in both NaCl and tetramethylammonium chloride media. L-Histidine (1 mM) at pH 8.5, at which histidine is uncharged, evoked an Na+-independent outward current (11 +/- 1.2 nA) in NBAT-expressing oocytes. The total inward 0.1 mM I(His) increased from -9 +/- 0.8 nA at pH 7.5 to -19 +/- 2.6 nA at pH 6.5, at which histidine is predominantly cationic. The increase in I(His) from pH 7.5 to 6.5 was found to be almost entirely due to the Na+-independent component. At pH 7.5, L-histidine weakly inhibited the Na+-independent L-arginine uptake; however, this inhibition was much stronger (>90%) at pH 6.5. L-Histidine transport, at pH 7.5, is stimulated by NBAT expression, but unlike L-phenylalanine or L-arginine transport, L-histidine transport is Na+-dependent and stereoselective. The induction of Na+-dependent L-histidine transport in NBAT-expressing oocytes provides new evidence that NBAT stimulates functionally distinct amino acid transporters including Na+-dependent L-histidine and Na+-independent L-arginine and L-phenylalanine transporters. The parallel induction of two different mechanisms argues that NBAT is not an amino acid transporter itself but, instead, is a transport-activating protein for a range of amino acid translocases.
authors.affiliation: Department of Anatomy and Physiology, University of Dundee, Scotland, United Kingdom. aahmed@dundee.ac.uk
authors.forename: A
authors.initials: A
authors.lastname: Ahmed
authors.forename: P C
authors.initials: PC
authors.lastname: Yao
authors.forename: A M
authors.initials: AM
authors.lastname: Brant
authors.forename: G J
authors.initials: GJ
authors.lastname: Peter
authors.forename: A A
authors.initials: AA
authors.lastname: Harper
mesh_terms: D026923:Amino Acid Transport Systems, Basic; D026921:Amino Acid Transport Systems, Neutral; D000596:Amino Acids / Q000502:physiology*; D000818:Animals; D001120:Arginine / Q000378:metabolism; D001692:Biological Transport; D002352:Carrier Proteins / Q000502:physiology*; D004553:Electric Conductivity; D006639:Histidine / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008564:Membrane Potentials; D009865:Oocytes; D018408:Patch-Clamp Techniques; D011994:Recombinant Proteins; D012964:Sodium / Q000502:physiology; D013237:Stereoisomerism; D014982:Xenopus laevis
chemical_list: D026923:Amino Acid Transport Systems, Basic; D026921:Amino Acid Transport Systems, Neutral; D000596:Amino Acids; D002352:Carrier Proteins; D011994:Recombinant Proteins; D006639:Histidine; D001120:Arginine; D012964:Sodium