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Expression of the type II membrane proteins of the rbAT/4F2hc family in Xenopus laevis oocytes results in the induction of amino acid transport activity. To elucidate the mechanism of action, amino acid transport was investigated in oocytes expressing the surface antigen 4F2hc. Leucine transport was mediated by a Na+-independent and a Na+-dependent transport mechanism. Both systems could be further discriminated by their stereochemical constraints. Isoleucine, with a branch at the beta-position, shared only the Na+-independent transport system with leucine. Both transport systems were sensitive to inhibition by arginine, but only the Na+-independent system was sensitive to inhibition by 2-aminobicyclo[2,2,1]heptane-2-carboxylic acid. When compared with known transport systems the two transport activities could be described as similar to, but not identical with, mammalian systems b0,+ and y+L. The Na+-independent b0,+-like transport system was found both in rbAT and 4F2hc expressing oocytes, indicating that both proteins act in a similar way.

Discrimination of two amino acid transport activities in 4F2 heavy chain- expressing Xenopus laevis oocytes