These mammalian ovarian glycolipids are complementary also to the anti-A/Tn cross-reactive -Gal NAc glycosylations.
The hexameric structure of this primitive invertebrate defense protein gives rise to speculation regarding an evolutionary relationship to the mammalian nonimmune, anti-A-reactive immunoglobulin M (Ig M) molecule.
In fact, A-allelic, phenotype-specific Gal NAc glycosylation of plasma proteins does not occur in human blood group O, affecting anti-Tn antibody levels, which may function as a growth regulator that contributes to a potential survival advantage of this group in the overall risk of developing cancer when compared with non-O blood groups.
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Hypothetically, this molecule obtains its complementarity from the first step of protein glycosylations, initiated by Gal NAc via reversible -glycan-depleted proteins, such as complementary Ig M revealing the structure of the volatilely expressed “lost” glycan carrier through germline Ser residues.