N. Miosge et al., ULTRASTRUCTURAL-LOCALIZATION OF BINDING-SITES FOR THE LECTINS RCA-I, WGA, AND LTA IN THE PREIMPLANTATION MOUSE EMBRYO, The Journal of histochemistry and cytochemistry, 45(3), 1997, pp. 447-453
In biological tissues, specific carbohydrate moieties of the oligosacc
haride chains of glycoproteins can be localized by lectin binding. Suc
h carbohydrate moieties are among the factors that mediate cell-cell o
r cell-matrix interactions during pre- and postimplantation embryonic
development. Binding sites for the lectins RCA I, WGA, and LTA were lo
calized in preimplantation mouse embryos at the ultrastructural level
with the help of postembedding lectin gold cytochemistry. WGA and RCA
I binding sites, but no CTA binding sites, were present in the zona pe
llucida. WGA and RCA I binding sites were found at cell surfaces of mo
rulae and in cells of the inner cell mass of blastocysts, suggesting t
hat N-acetylglucosamine-, terminal beta-galactosyl-, and N-acetylgalac
tosamine-rich glycoproteins might be involved in cell-cell and cell-ma
trix interactions. WGA binding sites were found predominantly in elect
ron lucid vesicles of the blastomeres, whereas RCA I was detected in e
lectron dense vesicles of the compacted morula and later in the polar
trophoblast cells. This allows early identification of blastomere cell
s that later differentiate into the polar trophoblast.