Jacques‐Edmond Fléchon

Fibronectins (FN) and laminin (LN) distributions were studied in the pig embryo by indirect immunofluorescence using antiporcine FN and antimurine LN antibodies. Extracellular FN are first detected in the early blastocyst before endodermal cell migration. They appear between the cells and on the blastocoelic face of the inner cell mass; thus, they are located at the interface of the trophectoderm and extraembryonic endoderm. Mesodermal cells migrate in a tridimensional network of fibrillar FN. These glycoproteins are also in the extraembryonic membranes (chorion and yolk sac wall) contiguous to the FN-rich basement membranes of embryonic ectoderm and endoderm. Extracellular LN appears in the blastocyst when the endoderm is already established as a continuous cellular monolayer, and is located between the trophectoderm and the extraembryonic endoderm, which produces it. Laminin also accumulates at the basal surface of the embryonic ectoderm at the onset of gastrulation. In the extraembryonic membranes, LN appears at the interface of the endoderm and mesoderm and at the interface of the trophectoderm and mesoderm. It is produced and secreted by extraembryonic mesodermal cells. Analysis of the distribution of these glycoproteins suggests that FN allow the migration of endodermal and mesodermal cells by providing them with a suitable substrate. When these cells become immobilized, they synthesize LN, probably to stabilize their interactions with the underlying extracellular material and epithelia.

Ferritin-conjugated soybean trypsin inhibitor was used for the ultrastructural localization of acrosin in bull spermatozoa following acrosomal disruption. The ferritin label was observed in the anterior segment of the acrosome in disrupted cells only. Emptied acrosomes were labeled, mostly on the external surface of their outer membrane. Labeling was also found on the material bound to detached acrosomal caps. However, at no time could the ferritin label be found on the inner acrosomal membrane. It is concluded that acrosin activity is not present on the inner acrosomal membrane but is lost from the acrosomal matrix as the acrosomal reaction proceeds.