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• W3148540722 abstract "The murine and the human genome have global properties in common. So the murine antiA-specific complementary IgM and related human innate isoagglutinin represent developmental, 2-mercaptoethanol-sensitive, complement-binding glycoproteins, which do not arise from any measurable environmentally-induced or autoimmune response. The murine anti-A certainly originates from a cell surfaceor cell adhesion molecule, which in the course of germ cell development becomes devoid of O-GalNAc-transferase and is released into the circulation. In human sera the enzyme occurs exclusively in those of blood group Aand AB subjects, while in group O(H) an identically encoded protein lets expect an opposite function and appears in conjunction with a complementary anti-A reactive glycoprotein. Since O-glycosylations rule the carbohydrate metabolism in growth and reproduction processes, we propose that the ancestral histo-(blood)-group A molecule arises in the course of O-GalNAc-glycosylations of glycolipids and protein envelops at progenitor cell surfaces. Germ cell development postulates embryonic stem cell fidelity, which is characterised by persistent production of -linked O-GalNAc-glycans. They are determined by the A-allele within the human, “complete” histo (blood) group AB(O) structure that in early ontogeny is hypothesised to be synthesised independently from the final phenotype. The structure either passes “completely” through the germline, in transferase-secreting mature tissues becoming the “complete” phenotype AB, or disappears in exhaustive glycotransferase depletion from the differentiating cell surfaces and leaves behind the “incomplete” blood group O-phenotype, which has released a transferaseand O-glycan-depleted, complementary glycoprotein (IgM) into the circulation. The process implies, that in humans the different blood phenotypes evolve from a “complete” AB(O) molecular complex in a distinct enzymatic and/or complement cascade suggesting O-glycanase involvements. While the murine and human oocyte zona pellucida express identical O-glycans, the human phenotype O might be explainable by the kinetics of the murine ovarian O-GalNAc glycan synthesis and the complementary anti-A released in parallel. The maturing murine ovary may provide insight into encoding of the physiologically superior -linked GalNAc ancestral epitope that becomes essential in reproduction as well as in tissue renewal events. According to recent reports, O-GalNAc-transferase-determined blood group A suggests superiority in human female fertility and was called even “protective”. So the minor fertility of blood-group-O females may reside in a critical timing in developmental shifting of enzyme functions affecting the formation of GalNAc-determined hormone receptors on the way to maturation. Experiments that had inserted an oocyte genome into a somatic one to generate pluripotent stem cells, might elucidate a developmental dilemma by testing oocytes from different blood group AB donors donors. Perhaps they will unmask the molecular basis of an evolutionary trend, while stem cell generation itself capitalises on the enzymatically-advantaged, lineage-maintaining (histo) blood group A-allele, which guaranties ancestral functional completeness. © 2013 Elsevier GmbH. All rights reserved. Abbreviations: GalNAc, N-acetyl-d-galactosamine; D-Gal, galactose; IgM, immunoglobulin M; RBC, red blood cells; GalNACase, -N-acetyl-d-galactosaminidase. ∗ Correspondence to: Am Oberen Stotchen 14, D-57462 Olpe, Germany. Tel.: +49 2761 71963; fax: +49 2761 825156. E-mail address: parend@t-online.de 1 The cited experiments of the author were performed at. 0171-2985/$ – see front matter © 2013 Elsevier GmbH. All rights reserved. http://dx.doi.org/10.1016/j.imbio.2013.10.011 Author's personal copy 286 P. Arend / Immunobiology 219 (2014) 285–291" @default.
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• W3148540722 date "2014-01-01" @default.
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• W3148540722 title "Complementary innate (anti-A-specific) IgM emerging from ontogenic O-GalNAc-transferase depletion (Innate IgM complementarity residing in ancestral antigen completeness)" @default.
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