Ultrastructural localization of pregnancy-specific beta 1-glycoprotein (SP1) and cathepsin B in villi of early placenta of the macaque.

Pregnancy-specific beta 1-glycoprotein (SP1) is found in maternal serum very early in gestation in both human and non-human primates. As judged by light microscopic immunocytochemistry, the major source of SP1 is the syncytial trophoblast, but little is known of the subcellular localization of SP1 indicative of the cellular pathway involved in secretion of the hormone. To study subcellular distribution of SP1, we used electron microscopic immunocytochemistry carried out on macaque placental villi from early (3-4 weeks) gestation. Both light and electron microscopic results confirmed localization confined to syncytial trophoblast in the villi. Within syncytial trophoblast labeling was predominantly over small granules in the apical cytoplasm. The Golgi complex also showed labeling, and light labeling was associated with the endoplasmic reticulum. For comparison, we also localized cathepsin B, a lysosomal protease. By way of contrast this enzyme was localized primarily in large cytoplasmic granules. The results are consistent with a secretory pathway including synthesis in the ER, processing by the Golgi complex, and exocytotic release into maternal blood in the intervillous space.