Ultracytochemical localizations of adenylate cyclase, guanylate cyclase and cyclic 3',5'-nucleotide phosphodiesterase activity on the trophoblast in the human placenta. Direct histochemical evidence.
Ultracytochemical localizations of cyclic nucleotide-metabolizing enzymes, namely adenylate cyclase (AC), guanylate cyclase (GC) and cyclic 3',5'-nucleotide phosphodiesterase (PDE), have been demonstrated in the human term placenta. AC activity was found positive on the basal plasma membrane of the syncytiotrophoblast and on the pinocytotic vesicle of the fetal capillary endothelial cell. GC activity was observed to be strong on the plasma membrane of the microvilli of the syncytiotrophoblast. The cAMP PDE activity was shown positive both on the basal plasma membrane and on the microvillous membrane, while cGMP PDE activity was exclusively confined to the microvilli of the syncytiotrophoblast. These observations suggest that the syncytiotrophoblast plays an important role in the cyclic nucleotide metabolism in the human term placenta and that there might be significant functional differences between its basal plasma membrane and its microvillous membrane.
D015105:3',5'-Cyclic-AMP Phosphodiesterases / Q000032:analysis*; D015106:3',5'-Cyclic-GMP Phosphodiesterases / Q000032:analysis*; D000262:Adenylyl Cyclases / Q000032:analysis*; D002462:Cell Membrane / Q000201:enzymology; D005260:Female; D006162:Guanylate Cyclase / Q000032:analysis*; D006651:Histocytochemistry; D006801:Humans; D008854:Microscopy, Electron; D010920:Placenta / Q000201:enzymology / Q000648:ultrastructure; D011247:Pregnancy; D014327:Trophoblasts / Q000201:enzymology* / Q000648:ultrastructure
D015105:3',5'-Cyclic-AMP Phosphodiesterases; D015106:3',5'-Cyclic-GMP Phosphodiesterases; D000262:Adenylyl Cyclases; D006162:Guanylate Cyclase