Glycoconjugate unique to migrating primordial germ cells differs with genera

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Abstract
Previous cytochemical studies showing that rat primordial germ cells (PGCs) possess a unique surface glycoconjugate containing terminal α‐Nacetylgalactosamine were extended in this study to determine whether a similar distinctive glycoconjugate coats the surface of PGCs in the mouse. The results showed that mouse PGCs fail to react with peroxidase‐conjugated lectins specific for localizing glycoconjugate with terminal N‐acetylgalactosamine. All available lectin conjugates with affinity for other terminal sugars or internal sugar linkages also failed to stain mouse PGCs except for the conjugates that bind to α‐fucose. One fucose‐specific lectin conjugate stained only PGCs in the early mouse embryo but stained additional sites in more mature embryos and lost reactivity with PGCs after gestational day 14. Another fucose‐specific conjugate stained PGCs until day 15, but with less selectivity, and a third such conjugate bound to several sites, but not to PGCs. The results suggest that the developmental mechanisms mediating cellular interaction, migration, and differentiation may be similar in different genera, but the specific structure of the cell surface glycoconjugate involved in these mechanisms differs.