Schistosoma mansoni muscle fibers contract in response to L-glutamate in a dose-dependent manner (10(-6)-10(-3) M). L-aspartate and D-aspartate are likewise effective in eliciting contraction of the fibers. Mammalian glutamate receptor agonists produce little or no contraction at concentrations as high as 1 mM. In addition, common glutamate receptor antagonists do not inhibit the contraction induced by L-glutamate. However, amino acids known to be substrates for the high-affinity glutamate transporter elicit contraction of the muscle fibers. These results suggests that there is a high-affinity glutamate transporter on the muscle fibers which, because of its electrogenic nature, is causing depolarization and contraction. This is supported by the evidence that contraction induced by L-glutamate is dependent on extracellular Ca2+ and is blocked by nicardipine (10 microM). [3H]L-glutamate is taken up in a dose-dependent manner by the muscle fiber preparation. This uptake is also time- and temperature-dependent. Both the L-glutamate-induced contractile response and [3H]L-glutamate uptake are Na(+)-dependent and can be blocked by specific inhibitors of the high-affinity transporter. This experimental evidence supports the hypothesis that there is a Na(+)-dependent high-affinity glutamate transporter on the schistosome muscle membrane.