PubMed · 5775253
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C Salmon. 1969. [ABO blood groups and genetic functioning].. https://doi.org/10.1016/s0035-2977(69)80013-1
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Six patients received an allogeneic bone marrow transplant from HLA-identical ABO-mismatched donors. ABO genotype of erythroid burst-forming units (BFU-E) from peripheral blood was analyzed using polymerase chain reaction with sequence specific primers (PCR-SSP). After bone marrow transplantation (BMT), engraftment of donor cells by ABO genotypic analysis of BFU-E was compared with ABO phenotypic analysis of red blood cells (RBCs). During the early stage after BMT, ABO genotype of BFU-E in the recipients converted to that of the donors. In contrast, mixed ABO phenotype of RBCs persisted for about 3 months. In one patient, autologous hemopoietic cell recovery was detected by the ABO genotypic analysis before clinical manifestation. ABO genotypic analysis of BFU-E is relevant for enagraftment after ABO-mismatched BMT.
A linear synthesis of a fully protected H-type II blood group determinant pentasaccharide utilizing glycosyl phosphate and glycosyl trichloroacetimidate building blocks is reported. Envisioning an automated solid-phase synthesis of blood group determinants, the utility of glycosyl phosphates in the stepwise construction of complex oligosaccharides, such as the H-type II antigen, is demonstrated. Installation of the central glucosamine building block required the screening of a variety of nitrogen protecting groups to ensure good glucosamine donor reactivity and protecting group compatibility. The challenge to differentiate C2 of the terminal galactose in the presence of other hydroxyl and amine protecting groups prompted us to introduce the 2-(azidomethyl)benzoyl group as a novel mode of protection for carbohydrate synthesis. The compatibility of this group with traditionally employed protecting groups was examined, as well as its use as a C2 stereodirecting group in glycosylations. The application of the 2-(azidomethyl)benzoyl group along with a systematic evaluation of glycosyl donors allowed for the completion of the pentasaccharide and provides a synthetic strategy that is expected to be generally amenable to the solid support synthesis of blood group determinants.
This review article offers a survey of the biochemical and molecular biological basis of the ABO subgroups. In contrast to protein-based blood groups, the antigens of the ABO system are carbohydrate antigens. The determinant carbohydrate structures are synthesised stepwise by the action of glycosyltransferases which transfer single monosaccharide residues onto an appropriate precursor substance. The genes responsible for the formation of the antigens of the ABO system (viz. ABO, Hh, and Sese) each encode single glycosyltransferases. Sequence analyses have shown that mutations in the ABO gene affecting only two amino acids in the encoded glycosyltransferase decide whether A or B epitope is synthesised. In blood group O individuals several inactive alleles of the ABO locus have been detected, which encode inactive transferases. These mutilated enzymes are not able to synthesise a defined blood group specificity. Blood group O is therefore characterised by the presence of unchanged A and B precursor, i.e. H-substance. Similarly, inactive variants of the H gene are responsible for the rare 'Bombay' phenotype and inactive variants of the secretor gene (Se) are responsible for the non-secretor status. In both cases the mutant transferases are not able to synthesise H-substances.