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Trans-species “A-like” and human blood group A-phenotype.pdf (368.81 kB)

Trans-species “A-like” and human blood group A-phenotype-specific GalNAc-glycosylations as they relate to the formation of natural anti-A isoagglutinin and Tn cross-reactive IgM.

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Version 71 2018-03-01, 06:55
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posted on 2018-03-01, 06:55 authored by Peter ArendPeter Arend
The multiple trans-species, genetically as-yet-undefined functions of serologically “A-like” O-GalNAc-Ser/Thr glycosylations, which dominate the early carbohydrate metabolism of all metazoan species, are different from the species-intrinsic and human phenotype-determining A-allelic enzyme proteins and/or functions only expressed after formation of the zygote. The productions of early O-glycans are subject to an extremely rapid turnover, and the volatilely expressed developmental “A-like”, mucin-type epitope GalNAcα1-O-Ser/Thr-R, also referred to as the Tn antigen is, when accumulated in non-developmental tissues, a marker of malignancy and is then called an “aberrant” glycosylated molecule. Historically, the “A-like” Tn antigen or “T nouvelle” was named upon its discovery reported in 1957 to emphasize its distinction from the functionally similar T (Thomsen-Friedenreich) antigen, reported in 1930. Early O-glycan expressions, which may be observed during germ cell development and embryonic stem cell differentiations, are characterized by extremely short half-lives, and their enzyme depletions most likely have caused the release of characteristic O-glycan-depleted, complementary plasma proteins, such as non-immune IgM that is not restricted to B cell secretion but also arises from epithelial cells.These enzyme depletions might reveal the structure of the volatilely expressed, “lost” O-glycans through germline-specific serine/threonine residues, whose terminal -OH group and acceptor of the first protein glycosylations is assumed to remain a functional, predetermined breaking point of the polyreactive, non-immune IgM molecule.

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