title: Activation of a novel organic solute transporter in mammalian red blood cells.
abstract: 1. Suspending human red blood cells in isotonic sucrose (low ionic strength, LIS) medium induces a significant increase in membrane transport of glutamine, glutamate, lactate, histidine, taurine, glycine, serine, choline and carnitine but not sorbitol or sucrose. 2. Progressive lowering of ionic strength by sucrose or NaCl replacement gave a similar activation profile for taurine influx as found earlier for residual K+(86Rb+) flux. 3. The induced taurine transport could be measured as enhanced influx and efflux. Influx was linear with external concentration up to 10 mM, largely insensitive to alteration in cell volume, and did not vary with red blood cell age. 4. Unlike previous results for residual K+ transport, altering transmembrane potential with gluconate or glucuronate media led to an increase in taurine influx similar to that observed in LIS media. Varying medium pH confirmed the effect was not due to alteration in pH. 5. The LIS-induced flux was sensitive to a variety of 'classical' anion transport inhibitors in the order of potency DNDS, DIDS, NPPB, DIOA, niflumic acid, furosemide (frusemide), glibenclamide, nitrendipine and bumetanide. 6. The taurine flux showed a temperature dependence similar to that of the LIS-induced residual K+ flux. High hydrostatic pressure (40 MPa), however, inhibited taurine flux but stimulated residual K+ influx in LIS media. 7. A significant enhanced taurine flux could be demonstrated in red blood cells of other species, including horse, cattle, pig and high and low potassium type sheep. 8. It is concluded that lowering ionic strength activates a transport pathway for organic molecules sharing some similarities with background Cl- channels and LIS-induced residual K+ fluxes. In the latter context, however, there are certain significant differences (effect of transmembrane potential; volume; pressure sensitivity; species distribution) which may be important, and the unequivocal identity of the two transport processes remains to be confirmed.
authors.affiliation: University Laboratory of Physiology, University of Oxford, UK.
authors.forename: S J
authors.initials: SJ
authors.lastname: Culliford
authors.forename: I
authors.initials: I
authors.lastname: Bernhardt
authors.forename: J C
authors.initials: JC
authors.lastname: Ellory
mesh_terms: D000818:Animals; D027321:Anion Transport Proteins; D000963:Antimetabolites / Q000494:pharmacology; D001711:Biotransformation / Q000187:drug effects / Q000502:physiology; D002352:Carrier Proteins / Q000378:metabolism*; D002417:Cattle; D003470:Culture Media; D004912:Erythrocytes / Q000187:drug effects / Q000378:metabolism*; D006736:Horses; D006801:Humans; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D008564:Membrane Potentials / Q000502:physiology; D009994:Osmolar Concentration; D011188:Potassium / Q000097:blood; D011312:Pressure; D012756:Sheep; D012964:Sodium / Q000097:blood; D013045:Species Specificity; D013552:Swine; D013654:Taurine / Q000097:blood; D013696:Temperature
chemical_list: D027321:Anion Transport Proteins; D000963:Antimetabolites; D002352:Carrier Proteins; D003470:Culture Media; D013654:Taurine; D012964:Sodium; D011188:Potassium