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. The kidney efficiently salvages creatine from the urine;  however, the mechanism(s) that mediates renal creatine reabsorption has not  been investigated. This study characterizes the creatine transport mechanism  in brush-border membrane vesicles isolated from the rat renal cortex. An  osmolality plot revealed that creatine is transported into an osmotically  active space and that it is also bound to the membranes. An inwardly directed  NaCl gradient stimulated creatine uptake and the time course of uptake  exhibited an overshoot phenomenon, which indicates the presence of an active  process for creatine in these membranes. The uptake of creatine showed an  absolute requirement for both Na +  and Cl - . The NaCl  gradient—dependent creatine uptake was stimulated by a  valinomycin-induced, inside-negative, K + -diffusion potential, which  suggests that the uptake process is electrogenic. Stoichiometric analyses  indicated a probable couple ratio of 2 Na + :1 Cl - :1  creatine molecule. The kinetic study showed that creatine is transported by a  high-affinity system ( K  m  of 15 μM). Creatine uptake was  inhibited by a 100-fold excess of various compounds with the following potency  order: cold creatine = guanidinopropionic acid &gt; nipecotic acid &gt;  γ-aminobutyric acid (GABA) = β-alanine = betaine, whereas  carnitine, glycine, taurine, and choline were without effect. This pattern of  inhibition differs from that observed for GABA uptake (unlabeled GABA = GPA  &gt; β-alanine &gt; nipecotic acid ≫ creatine). The conclusion drawn  was that the apical membrane of the renal cortical tubules contains an active,  high-affinity, electrogenic, 2 Na + /1 Cl - /creatine  cotransporter.

Creatine Transport in Brush-Border Membrane Vesicles Isolated from Rat Kidney Cortex