Figure 2
From: Impaired K+ binding to glial glutamate transporter EAAT1 in migraine
Internal potassium abolishes hEAAT1 anion currents in T387P hEAAT1. (a) Representative whole-cell patch clamp recordings from HEK293T cells expressing WT (left) or T387P (right) hEAAT1 internally dialyzed with K+-based solutions in the absence (top) and presence (bottom) of glutamate. Inset depicts the glutamate transport cycle16,17,19. (b and c) Current-voltage relationships for WT (b, circles), mutant (c, squares) hEAAT1, and untransfected HEK293T cells (b and c, small diamonds) under these experimental conditions (n = 9/12/8). (d) Statistical analysis of current amplitude differences from untransfected cells (small diamonds) and T387P hEAAT1 transfected HEK293T cells (squares) at a holding potential of −125 mV under uptake conditions. Bath solution (in mM): 140 NaNO3, 4 KCl, 2 CaCl2, 1 MgCl2, 5 HEPES, 5 TEA-Cl, pH 7.4; Pipette solution: 115 KNO3, 2 MgCl2, 5 EGTA, 5 L-glutamate, 10 HEPES, pH 7.4.
