Expression of the 14 kDa and 16 kDa galactoside-binding lectins during differentiation of the chick yolk sac.

Abstract

The gastrulating chick embryo expresses two galactoside-binding lectins of 14 kDa and 16 kDa. These lectins are present in the area pellucida and area opaca, and in the latter are concentrated in the endoderm. Since the area opaca is the progenitor of the yolk sac, we studied the galactose-binding lectins during the development of this extraembryonic organ. In the yolk sac, lectin expression surges between 2 and 4 days, and thereafter remains constant throughout development. Using monoclonal antibodies (mAbs) specific to the 16 kDa yolk sac lectin, and a panel of polyclonal antibodies to the 14 kDa and 16 kDa lectins we studied lectin expression. The mAbs inhibit the hermagglutinating activity of extracts from chick yolk sac, embryonic pectoral muscle, and adult liver, but have no effect on the hemagglutinating activity of extracts from the adult intestine. Immunolocalization studies with the mAbs and polyclonal antibodies indicate that in the less differentiated endodermal cells of the area vitellina the 16 kDa lectin is present in discrete lectin-rich inclusions. In contrast, within the maturing endodermal epithelium of area vasculosa the 16 kDa lectin is present around the intracellular yolk platelets, and is associated with the cytoplasmic matrix. The 16 kDa lectin is also found at the apical cell surface of the yolk sac epithelium, in some regions closely associated with the plasma membrane. The 14 kDa lectin is distributed intracellularly surrounding the yolk platelets of the maturing yolk sac endoderm. The surge in expression of the 16 kDa lectin at the time of expansion of the area opaca suggests that it may be involved in the spreading of this area. Our findings also indicate that as the yolk sac endoderm differentiates into an epithelium intracellular lectin expression changes from predominantly organelle associated to cytoplasm associated. The association of both lectins with yolk suggest that the lectins may also be involved in the processing of intracellular and extracellular yolk proteins. These results, in con junction with previous findings indicating the presence of these lectins in the extracellular matrix (Didier et al., Histochemistry 100:485, 1993; Zalik et al., Intl J Dev Biol 38:55-68, 1994) indicate that these lectins play multiple roles in embryonic development.