Characterization of glutamine synthetase transcript, protein, and enzyme activity in the human placenta.

This study characterizes the molecular mechanisms necessary for glutamine synthesis in the human placenta. RNA hybridization and protein immunoblotting were used to verify the presence of glutamine synthetase (GS) transcripts and protein, respectively. Additionally, the presence of GS was determined by immunohistochemistry. RNA hybridization demonstrated the presence of 1.8- and 2.8-kB transcripts and protein immunoblotting yielded a single 49-kDa band, characteristics of GS transcripts and protein, respectively. The mean (+/- s.d.) specific activity of placental GS, expressed as mumol gamma-glutamyl hydroxamic acid/mg protein/h was 1.80 +/- 0.59, which is comparable to other organs which are net glutamine producers. Immunohistochemical analysis indicated the presence of GS within the cytotrophoblast and mesenchyme layers of placental villi, but not in the syncytiotrophoblast. Although these results suggest that the human placenta is capable of synthesizing glutamine, the fate of glutamine produced by this organ remains speculative.