Blood group A/B-defined glycosyltransferase and A/B blood group antigens in human normal and malignant endometrium in relation to morphology, age and oestrogen levels

1994 ◽  
Vol 1 (3) ◽  
pp. 153-163
Author(s):  
Vibeke Ravn ◽  
Ulla Mandel ◽  
Birgit Svenstrup ◽  
Erik Dabelsteen
1992 ◽  
Vol 176 (5) ◽  
pp. 1311-1317 ◽  
Author(s):  
J Carlson ◽  
M Wahlgren

Herein we describe an assay that was developed to quantitate the binding of normal red blood cells (RBC), labeled with carboxy fluorescein diacetate (C-FDA), to rosetting Plasmodium falciparum-infected RBC. The binding of RBC obtained from various animal species or humans to different strains or clones of rosetting P. falciparum-infected RBC was studied. A strain-specific preference of rosetting was observed for either blood group A/AB or B/AB RBC for all parasites tested. The higher affinity of rosette binding of blood group A, B, or AB vs. O RBC was reflected in larger rosettes when a given parasite was grown in RBC of the preferred blood group. The small size of the rosettes formed when P. falciparum was grown in blood group O RBC may be the in vitro correlate of the relative protection against cerebral malaria afforded by belonging to blood group O rather than to blood group A or B. Rosettes of a blood group A-preferring parasite could be completely disrupted by heparin only when grown in blood group O or B RBC, but not when grown in blood group A RBC. Similarly, the rosettes of a blood group B-preferring parasite could be more easily disrupted by heparin when grown in blood group O or A RBC than when grown in blood group B RBC. Several different saccharides inhibited rosetting of group O RBC, including two monosaccharides that are basic components of heparin. The rosetting of the same parasites grown in blood group A or B RBC was less sensitive to heparin and was specifically inhibited only by the terminal mono- and trisaccharides of the A and the B blood group antigens, the H disaccharide, and fucose. Our results suggest that rosetting is mediated by multiple lectin-like interactions, the usage of which rely on the parasite phenotype and whether the receptors are present on the host cell or not.


1965 ◽  
Vol 121 (6) ◽  
pp. 1039-1050 ◽  
Author(s):  
H. A. Thiede ◽  
J. W. Choate ◽  
H. H. Gardner ◽  
H. Santay

The chorionic villi of term placentas were examined for A and B blood group substance using the IF technique with heterologous and homologous antisera. No specific fluorescence was found in either the villous trophoblast or vessels of the chorionic villi. The implications of these findings in relation to the question of trophoblastic antigenicity are discussed.


1988 ◽  
Vol 256 (2) ◽  
pp. 661-664 ◽  
Author(s):  
M S Stoll ◽  
T Mizuochi ◽  
R A Childs ◽  
T Feizi

Conditions have been established for the rapid and efficient conjugation of reducing oligosaccharides (di- to deca-saccharides) to dipalmitoyl phosphatidylethanolamine. The resulting neoglycolipids derived from several naturally occurring oligosaccharides and a series of N-linked high-mannose-type oligosaccharides released by hydrazinolysis from RNAase B showed specific and potent reactivities, as appropriate, with monoclonal antibodies to blood group Lewis(b), blood group A or a stage-specific embryonic (SSEA-1) antigen, or the lectin concanavalin A.


1989 ◽  
Vol 37 (7) ◽  
pp. 1153-1155 ◽  
Author(s):  
T F Orntoft ◽  
K Nielsen

Intratumor heterogeneity is a major problem in immunodiagnosis and treatment of carcinomas. To elucidate the well-known heterogeneity in transitional-cell carcinomas of the ability to express blood group ABO isoantigens, a stereological estimate of the mean nuclear volume in areas expressing blood group antigens was compared to the estimate from areas of identical pathological grade at which antigen expression was deleted. Four microscopic fields were examined from antigen-positive and four from antigen-negative areas in sections from 21 blood group O and 20 blood group A individuals. The sections were stained before examination by an indirect peroxidase method using monoclonal anti-H and anti-A antibodies. The mean nuclear volume increased, as expected, with increasing pathological grade. In blood group O individuals the mean nuclear volume was 241.5 microns 3 in antigen-positive areas and 338.2 microns 3 in antigen-negative areas (2p less than 0.0005) of identical pathological grade. In group A individuals the mean nuclear volume was 217.1 microns 3 in positive areas and 351.1 microns 3 in corresponding negative areas (2p less than 0.0025). The variation in volume parameter was essentially caused by a true variation between tumors (greater than 82%). The results indicate a complex biological mechanism associated with the cellular ability to express blood group antigens.


2000 ◽  
Vol 68 (5) ◽  
pp. 2971-2975 ◽  
Author(s):  
Antonio Barragan ◽  
Peter G. Kremsner ◽  
Mats Wahlgren ◽  
Johan Carlson

ABSTRACT The malaria parasite Plasmodium falciparum utilizes molecules present on the surface of uninfected red blood cells (RBC) for rosette formation, and a dependency on ABO antigens has been previously shown. In this study, the antirosetting effect of immune sera was related to the blood group of the infected human host. Sera from malaria-immune blood group A (or B) individuals were less prone to disrupt rosettes from clinical isolates of blood group A (or B) patients than to disrupt rosettes from isolates of blood group O patients. All fresh clinical isolates and laboratory strains exhibited distinct ABO blood group preferences, indicating that utilization of blood group antigens is a general feature of P. falciparumrosetting. Soluble A antigen strongly inhibited rosette formation when the parasite was cultivated in A RBC, while inhibition by glycosaminoglycans decreased. Furthermore, a soluble A antigen conjugate bound to the cell surface of parasitized RBC. Selective enzymatic digestion of blood group A antigen from the uninfected RBC surfaces totally abolished the preference of the parasite to form rosettes with these RBC, but rosettes could still form. Altogether, present data suggest an important role for A and B antigens as coreceptors in P. falciparum rosetting.


Blood ◽  
1999 ◽  
Vol 93 (12) ◽  
pp. 4418-4424 ◽  
Author(s):  
Sergio H. Spalter ◽  
Srini V. Kaveri ◽  
Emmanuelle Bonnin ◽  
Jean-Claude Mani ◽  
Jean-Pierre Cartron ◽  
...  

Abstract It is widely accepted that the serum of healthy individuals contains natural antibodies only against those blood group A or B antigens that are not expressed on the individual’s red blood cells. The mechanisms involved in tolerance to autologous blood group antigens remain unclear. In the present study, we show that IgM and IgG antibodies reactive with autologous blood group antigens are present in the immunoglobulin fraction of normal human serum. Natural IgG anti-A antibodies purified by affinity chromatography from IgG of individuals of blood group A exhibited an affinity for A trisaccharide antigen in the micromolar range and agglutinated A red cells at sixfold higher concentrations than those required for agglutination with affinity-purified anti-A IgG of individuals of blood group B. Whereas autoantibodies reactive with self A and B antigens are readily detected in purified IgG and IgM fractions, their expression is restricted in whole serum as a result of complementary interactions between variable regions of antibodies. These observations suggest that tolerance to autologous ABO blood group antigens is dependent on peripheral control of antibody autoreactivity.


2017 ◽  
Vol 49 (9) ◽  
pp. 473-483 ◽  
Author(s):  
Anuhya Gampa ◽  
Phillip A. Engen ◽  
Rima Shobar ◽  
Ece A. Mutlu

FUT2 is a gene for a fucosyltransferase that encodes expression of ABO blood group antigens found on gastrointestinal mucosa and secretions. We hypothesized that the fecal microbiomes of healthy subjects, with blood group antigens A, B, and O, have differing compositions. We analyzed 33 fecal and blood specimens from healthy subjects for FUT2 genotype, and the fecal microbiome was determined by 454 pyrosequencing. Our data show that being a blood group secretor is associated with less diversity at higher orders of taxonomy; and the presence of blood group A antigens in the secretor subjects are associated with an expansion families of bacteria within the gut. Furthermore, our study confirms the previous findings that secretors and nonsecretors have differing bacterial taxa. This extends the previous findings by demonstrating that the impact of being a nonsecretor is higher than that of individual blood group antigens. Additionally, we demonstrate that both secretor status and blood group antigen expression especially affect the Lachnospiraceae family of bacteria within the gut microbiome, with lower abundances noted in nonsecretors and higher abundances in secretors of various blood groups. We further note specific differences in blood group A-secretors demonstrating that the genus Blautia is lower in the group A-secretors compared with the non-A-secretors and that this reduction is accompanied by higher abundances of members of the Rikenellaceae, Peptostreptococcaceae, Clostridiales, and Turicibacter. This study offers a first insight into the relationship between the fecal microbiome and blood group antigens in secretors.


1988 ◽  
Vol 36 (4) ◽  
pp. 337-348 ◽  
Author(s):  
M Nakajima ◽  
N Ito ◽  
K Nishi ◽  
Y Okamura ◽  
T Hirota

We investigated localization of blood group antigens and their related substances in human labial salivary and submandibular glands by application of a post-embedding cytochemical staining procedure using lectin- or glycoprotein-gold complexes. Surgical tissue was obtained from 10 patients. Blood group-specific lectins, such as Dolichos biflorus agglutinin or Helix pomatia agglutinin (group A-specific), Griffonia simplicifolia agglutinin-I B4 (group B-specific), and Ulex europaeus agglutinin I (group H-specific) could recognize A, B, and H antigens, respectively, only in mature secretory granules (mature SG), which were found preferentially in cells in the late phase of the maturation cycle. In immature secretory granules (immature SG), which were found in cells in the early or middle phase of the maturation cycle, no binding with these lectins was observed. The Golgi complexes and endoplasmic reticula also were not labeled with these lectins. In blood group O and B secretors, blood group antigens were uniformly distributed throughout all the mature SG examined. However, in blood group A secretors, the distribution was heterogeneous, i.e., in some granules only H antigen was demonstrated, whereas in others both A antigens and a small amount of H antigens were detected. Among the blood group-nonspecific lectins, wheat germ agglutinin (WGA) was found to bind more preferentially to immature SG than to mature SG. This was demonstrated irrespective of the blood group and secretor status of the tissue donor, except that in blood group A secretors WGA bound strongly to some mature SG which possessed A antigen. We discuss the significance of cellular and subcellular mosaic distribution of blood group antigens in connection with morphological differences of secretory granules and the maturation cycle of mucous cells.


Blood ◽  
2017 ◽  
Vol 130 (Suppl_1) ◽  
pp. 925-925
Author(s):  
Romy Kronstein-Wiedemann ◽  
Laura Schmidt ◽  
Jörn Lausen ◽  
Erhard Seifried ◽  
Torsten Tonn

Abstract Background: The ABO blood group system is unequivocally the most important in clinical transfusion medicine. Furthermore ABO is implicated in the development of a number of human diseases. The ABO antigens are not confined to RBCs but are widely expressed in a variety of human cells and tissues. Thus, ABO matching is critical not only in blood transfusion but also in cell, tissue and organ transplantation. The molecular genetic basis of the ABO system has been known since 1990. However, despite extensive investigations about regulation of ABO blood group receptor expression, the mechanism is not fully resolved. Previously we found that miRNAs plays a critical role in regulation of ABO blood group antigen. Numerous miRNAs which were up- or downregulated in RBCs of blood group O and of heterozygous genotypes as compared to homozygous genotype possess potential binding sites in the 3'UTR of several transcription factors, such as SP1 and RUNX1. Here we show that silencing of the transcription factor RUNX1 leads to downregulation of blood group A antigen. Methods: We performed knockdown experiments for RUNX1 by lentiviral gene transfer of shRNA in primary hematopoietic stem cells (HSCs) and analyzed blood group A-antigen expression using different method, including flow cytometry, western blot and qPCR. Result: Knockdown of RUNX1 in HSCs leads to a 10-20% reduction of blood group A positive erythroid cells and a 30-40% reduction of blood group A antigens per cell in differentiated RBCs. Furthermore, microarray analysis showed a significant increase of miR-215-5p and miR-192-5p in RBCs of blood group O as compared to homozygous genotype. RUNX1 is known to be a target gene for these miRNAs. Conclusion: Glycosyltransferase A and B expression is regulated by different miRNAs, via simultaneously targeting of the transcription factors SP1 and Runx1 and glycosyltransferase A and B mRNA. The knowledge of the role of microRNAs and the transcription factors SP1 and RUNX1 in the expression of blood group antigens may be extended to other blood groups (Rhesus, Kell, Duffy) and may open the door for therapeutic interventions in diseases where blood group receptors promote disease pathology. Disclosures No relevant conflicts of interest to declare.


Blood ◽  
1999 ◽  
Vol 93 (12) ◽  
pp. 4418-4424 ◽  
Author(s):  
Sergio H. Spalter ◽  
Srini V. Kaveri ◽  
Emmanuelle Bonnin ◽  
Jean-Claude Mani ◽  
Jean-Pierre Cartron ◽  
...  

It is widely accepted that the serum of healthy individuals contains natural antibodies only against those blood group A or B antigens that are not expressed on the individual’s red blood cells. The mechanisms involved in tolerance to autologous blood group antigens remain unclear. In the present study, we show that IgM and IgG antibodies reactive with autologous blood group antigens are present in the immunoglobulin fraction of normal human serum. Natural IgG anti-A antibodies purified by affinity chromatography from IgG of individuals of blood group A exhibited an affinity for A trisaccharide antigen in the micromolar range and agglutinated A red cells at sixfold higher concentrations than those required for agglutination with affinity-purified anti-A IgG of individuals of blood group B. Whereas autoantibodies reactive with self A and B antigens are readily detected in purified IgG and IgM fractions, their expression is restricted in whole serum as a result of complementary interactions between variable regions of antibodies. These observations suggest that tolerance to autologous ABO blood group antigens is dependent on peripheral control of antibody autoreactivity.


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