Molecular characterization of taurine transport in bovine aortic endothelial cells.

Cultured bovine aortic endothelial (BAE) cells expressed a Na(+)/Cl(-)-dependent taurine uptake activity that saturated with an apparent K(0.5) of approximately 4.9 microM for taurine and was inhibited by beta-alanine, guanidinoethane sulfonate, and homotaurine. We isolated a taurine transporter clone from a BAE cell cDNA library that revealed >91% sequence identity at the amino acid level to the previously cloned high-affinity mammalian taurine transporters. The biochemical and pharmacological properties of the bovine taurine transporter cDNA expressed in Xenopus oocyte was similar to those of the high-affinity taurine transporter. Surprisingly, F(-) blocked taurine uptake in BAE cells with an IC(50) of approximately 17.5 mM. The endogenous taurine uptake was also inhibited by the protein kinase C activator phorbol 12-myristate 13-acetate, but not by its inactive analog, 4 alpha-phorbol 12,13-didecanoate. The endogenous uptake was stimulated, however, by hypertonic stress and the increase was due to an increase in the V(max) of taurine uptake. Our results provide the first description of a molecular mechanism that may be responsible for maintaining the intracellular taurine content in the endothelial cells.