ABO(H) System

Schenkel‐Brunner, Helmut

doi:10.1007/978-3-7091-3686-7_5

Cited by 5 publications

(2 citation statements)

References 370 publications

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“…The ABH antigens are not confined to red blood cells (RBCs) and are widely expressed in body fluids and other tissues 4 . ABH antigens are expressed in a cell type‐specific manner and undergo drastic changes during the development, differentiation, and maturation of cells in the epithelial and erythroid lineages 5 …”

Section: Introductionmentioning

confidence: 99%

Regulation of ABO blood group antigen expression by miR-331-3p and miR-1908-5p during hematopoietic stem cell differentiation

et al. 2020

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The ABO blood group system is the most important factor in clinical transfusion medicine and is implicated in a number of human diseases. ABO antigens are not confined to red blood cells (RBCs) and are widely expressed in a variety of human cells and tissues. To date, many alleles with variant ABO expression have been identified and in many cases traced to one of the >250 reported genetic variations in the respective glycosyltransferase. The role of microRNAs (miRNAs) in the regulation of blood group antigens during erythropoiesis has not been addressed, however. Here, we show that miR-331-3p and miR-1908-5p directly target the mRNA of glycosyltransferases A and B. Expression levels of miR-331-3p and miR-1908-5p inversely correlated with levels of blood group A antigen. In addition, we found that overexpression of these miRNAs in hematopoietic stem cells led to a significantly reduced number of blood group A antigens per RBC. Simultaneous targeting of the transcription factor (TF) SP1 by miR-331-3p further enhanced these effects. The targeting rendered SP1 incapable of binding to the ABO gene promoter, causing further downregulation of blood group A antigen expression by up to 70%. Taken together, expression changes in these miRNAs may account for rare cases of weak A/B phenotypes that genetic variations in the glycosyltransferase coding region cannot explain. These results also suggest an explanation for the disappearance of ABH antigens during carcinogenesis and point to new therapeutic targets in ABO mismatched organ transplantation.

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Section: Introductionmentioning

confidence: 99%

Regulation of ABO blood group antigen expression by miR-331-3p and miR-1908-5p during hematopoietic stem cell differentiation

et al. 2020

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“…This required incorporation of an intact erythrocyte into the polymer since the Rh (D) antigen can retain activity only while supported in the erythrocyte membrane. The ability to bind antibody by the Rhesus antigens depends on the presence of phospholipids because the lipids orientate the Rh protein allowing antibody binding [35].…”

Section: Introductionmentioning

confidence: 99%

Incorporation of Erythrocytes into Polypyrrole to Form the Basis of a Biosensor to Screen for Rhesus (D) Blood Groups and Rhesus (D) Antibodies

1999

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Antibodies to Rhesus (Rh) antigens are important indicators in screening for haemolytic disease of the new-born (HDN) and autoimmune haemolytic anaemia (AIHA). Identi®cation of the Rh antibodies formed by immune stimulation is also essential in order to maximize the in vivo survival time of transfused erythrocytes. Currently this is performed by agglutination based assays that are time consuming. A prototype of an immuno-biosensor for detecting antibodies recognizing the Rhesus blood group antigen, Rh (D), was constructed. Human erythrocytes were incorporated into a conducting polypyrrole, polyelectrolyte matrix. The process was followed by using oximetry and light microscopy to demonstrate the integrity of the erythrocytes in the polymerization solution and in the polymer matrix; cyclic voltammetry and resistometry for electrochemical characterization of the polymer and then agglutination, ELISA techniques and cyclic resistometry for analysis of the immuno response from antigenaantibody binding. Antigenaantibody binding could be detected qualitatively by using resistometry while cycling the polymer between 0X35 V and À0X7 V (vs. AgaAgCl). A characteristic cyclic change in resistance (a resistogram) was recorded. After addition of Anti-Rh (D) antibody (250 mgamL), the change in resistance during the resistogram decreased by 1.1 O (p`0X0008) in polymers containing Rh (D) positive erythrocytes, whereas polymers without erythrocytes showed no signi®cant change.

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Origin of an 84‐kDa Protein with ABH Blood‐Typing Antigen Activity in Human Seminal Plasma

SATO,

NAKAMURA,

YAMAZAKI

et al. 1999

Journal of Andrology

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In order to investigate the origin of an 84‐kDa protein with ABH blood‐typing antigen activity (p 84) and its concentration in human seminal plasma, a monoclonal antibody (mAb p 84) was produced. The protein was recognized in breast milk as well as in seminal plasma by an indirect, enzyme‐linked immunosorbent assay (ELISA) using this mAb. mAb p 84 identified 84‐kDa and 83‐kDa forms of the protein in seminal plasma and breast milk, respectively, on immunoblotting. The mean concentration of p 84 in seminal plasma was 949 μg/ml (n = 54 subjects). There was no significant difference in the concentration of p 84 between individuals who secreted (Se) or did not secrete (non‐se) the ABH antigen into their seminal plasma, nor were there any significant correlations between the concentration of p 84 and the total seminal protein concentration. An immunohistochemical study using mAb p 84 with light microscopic detection showed that p 84 was located in the cytoplasm of the inner layer of pseudostratified cuboidal epithelial cells of the seminal vesicles, but no immunoreactivity was found in the prostate. These data indicate that p 84 originates from a single tissue, the seminal vesicles, and suggest that p 84 is an ABH epitope‐bearing protein that has not previously been identified but possesses some immunological properties similar to those of lactotransferrin.

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ABO(H) System

Cited by 5 publications

References 370 publications

Regulation of ABO blood group antigen expression by miR-331-3p and miR-1908-5p during hematopoietic stem cell differentiation

Regulation of ABO blood group antigen expression by miR-331-3p and miR-1908-5p during hematopoietic stem cell differentiation

Incorporation of Erythrocytes into Polypyrrole to Form the Basis of a Biosensor to Screen for Rhesus (D) Blood Groups and Rhesus (D) Antibodies

Origin of an 84‐kDa Protein with ABH Blood‐Typing Antigen Activity in Human Seminal Plasma

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