Blood group-A Research Articles

Anxiety and depression among various blood groups of undergraduate medical and physical therapy students

Objective: To access the frequency of depression and anxiety among the various blood groups of medical and physiotherapy students. Method: A cross-sectional study on 215 MBBS and DPT students was conducted at Aziz Fatimah Medical and Dental College (AFMDC) from November 2022-May 2023. Google Form containing sections for relevant information concerning participants and fourteen items- Hospital anxiety and depression Scale (HADS) questionnaire for evaluation of anxiety and depression, was administered among the MBBS and DPT students through social media. The data was analyzed using SPSS version 26. Mean ±SD was calculated for continuous variables like HADS score and age. Frequency and percentage were calculated for categorical variables such as blood groups, anxiety and depression. ANOVA was used to compare HADS score among various blood groups. P-value ≤0.05 was taken statistically significant. Result: Mild anxiety was found in A>O>B>AB, while severe anxiety was found in B>A>AB>O. Mild depression was found in A>B>O>AB, while severe depression was found in A>O>B>AB. However, on ANOVA, when comparing anxiety and depression scores with blood groups, they were found to be higher in blood Group-A. Rhesus factor positive blood groups have severe anxiety and mild depression while Rhesus factor negative blood groups have mild anxiety and severe depression. Conclusion: Severe anxiety was common in blood Group-B while severe depression was common in people with blood Group-A. While mild anxiety and mild depression was found in blood Group-A, however, sever anxiety was common in positive Rhesus factor blood types while severe depression was found in negative Rhesus factor blood types. doi: https://doi.org/10.12669/pjms.40.10.8984 How to cite this: Rubab-e-Hira, Ali M, Jawed S, Altaf B. Anxiety and depression among various blood groups of undergraduate medical and physical therapy students. Pak J Med Sci. 2024;40(10):2422-2427. doi: https://doi.org/10.12669/pjms.40.10.8984 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Effect of ABO blood group on the severity and clinico-pathological parameters of COVID-19.

The COVID-19 pandemic has highlighted the need to understand the factors affecting disease severity. Prior research has indicated the potential roles of the ABO blood group system in disease susceptibility and progression. Our objective was to investigate the association between ABO Blood groups and the severity of COVID-19 and clinicopathological parameters. An analytical cross-sectional study was conducted across three locations of Ziauddin University Hospital, including COVID-19 outpatient departments (OPDs), wards, and intensive care units (ICUs) from May 2020 to December 2020.The study utilized a non-probability convenient sampling technique with a sample size of 120 PCR-positive adult patients, as calculated by OpenEpi with a 95% confidence interval. Patients were excluded if they were under 14, intellectually impaired, post-chemotherapy or radiotherapy, or had a malignant condition. Disease severity was determined based on clinicopathological parameters and associated with blood group data using ANOVA and Chi-square tests in SPSS version 21. A significant association was found between the ABO blood groups and COVID-19 severity. Blood group-A was notably overrepresented in patients with severe COVID-19 and correlated with higher inflammatory markers and coagulation parameters. ABO blood group, particularly Blood Group-A significantly associates with the severity of COVID-19. This finding suggests the potential utility of ABO blood group typing as a predictive marker for disease severity, which could contribute to personalized patient management strategies. Further research is necessary to understand the mechanisms underlying this association.

Association of blood groups/Rh and diabetes mellitus in Karachi city, Pakistan.

The main purpose of this study was to find out a possible association between ABO blood groups or Rh and diabetes mellitus (DM) in the local population of eight (8) different towns of Karachi, Pakistan. For this purpose a survey was carried out in Karachi to have a practical observation of these towns during the period of 9 months from June 2019 to Feb. 2020. Out of eighteen (18) towns of Karachi, samples (N= 584) were collected from only eight (8) Towns of Karachi and gave a code-number to each town. Diabetic group sample was (n1=432) & pre-diabetes sample was (n2 =152). A standard Abbot Company Glucometer for Random Blood Sugar (RBS) and Fasting Blood Sugar (FBS) tests, standard blood anti sera were used for ABO/Rh blood type. Health assessment techniques were performed ethically by taking informed consent from all registered subjects. Finally data was analyzed by SPSS version 20.0. In our current study, the comparison of ABO blood groups frequencies between diabetic and pre-diabetic individuals were carried out. The percentage values of blood Group-B as given as: (32% in DM vs. 31% in pre-diabetics), followed by blood Group-O as: (18% in DM vs. 11% in pre-diabetics). Contrary to Group-"B" & "O", blood Group-A and Group-AB were distribution percentage higher pre-diabetic as compared to DM patients, as given as: Group-A (32% in pre-diabetics vs. 26% in DM) & Group-AB (26% in pre-diabetics vs. 24% in diabetic's patients). In addition, percentage distribution of Rh system was also calculated, in which Rh+ve Group was high and more common in DM patients as compared to pre-diabetics; numerically given as: Rh+ve Group (80% in DM vs. 72% in pre-diabetics). Different views and dimensions of the research topic were studied through literature support, some have found no any association and some established a positive association still some were not clear in making a solid conclusion. It is concluded that DM has a positive correlation with ABO blood groups, and people with Group-B have increased susceptibility to DM disease.

Prevalence of A2 and A2B Subgroups among Blood Groups A and AB in healthy donors.

To determine the frequency of A2 and A2B subgroups among blood groups A and AB in healthy donors. It was a Cross-Sectional study, conducted at the Department of Hematology & Transfusion Medicine, UCHS, The Children's Hospital Lahore and Sundas foundation Lahore from June 2022 to December 2022 including 13,120 healthy blood donors of both genders, after taking informed consent. Venous blood samples of donors were collected in EDTA vials (3ml) and serum gel vial for routine blood grouping which was done by standard tube method. Further testing of donors positive for an antigen (blood Group-A and AB) was performed using anti-A1 lectin by standard tube method as per manufacturer's instruction. The data was analyzed using SPSS version 23. Among 13120 blood donors, 12857 (97.9%) were male and 263 (2.0%) were female with mean age of 36.7 years ± 15.04 years. Majority of them (91.7%) were of Punjabi ethnicity. Donors having blood group phenotype A and AB were 3890 (29.6%). Among blood Group-A donors, A1 was found in 97.8% and A2 in 2.2% donors. While among Blood Group-AB, 96.7% donors belonged to A1B blood group and 3.2% belonged to A2B blood group. Blood group A2 and A2B do exist in blood donors of Punjabi ethnicity. The knowledge of presence of these blood groups' phenotypes in our population can provide a better base for transfusion staff to do troubleshooting in compatibility testing and to avoid any rare but hazardous transfusion outcome.

Serological and Molecular Characterization of Blood Group A2 in Pakistan

Objective: To determine the frequency of Blood Group A2 genotype among Group A Pakistani whole blood donors.
 Study Design: Cross-sectional study.
 Place and Duration of Study: Armed Forces Institute of Transfusion (AFIT), Rawalpindi Pakistan, from Jan 2019 to Jan 2020.
 Methodology: One thousand (1000) healthy and unrelated blood donors were selected. The blood samples were typed for ABO, and those of Blood Groups-A and AB were further subtyped with the help of anti-A1 lectin to categorize them as A1,non-A1, A1B and non-A1B Groups. Next, DNA of non-A1 samples was extracted, and a Polymerase Chain Reaction using sequence-specific primers (PCR-SSP) for type A2 was performed, followed by polyacrylamide gel electrophoresis (PAGE).
 Results: Among one thousand blood donors, 247(24.7%) were typed as Blood Group-A, 94(9.4%) as AB-Group, 339(33.9%) BGroup and 320(32%) O Group with variable strength of reaction with ABO antisera. A and AB Blood Groups were further subgrouped as A1 202(20.2%), A1B 77(7.7%), non-A1 45(4.5%) and non-A1B 17(1.7%). Anti-A1 antibodies were detected in 6(13.3%) of non-A1 samples. PCR of non-A1 samples showed 32(12.9%) to be genotypically A2, and the remaining 13(5.2%) were not A2 and were not further resolved.
 Conclusion: Blood Group A2 is not a rare Subgroup in our population. PCR-SSP is a more specific technique than anti-A1 lectin for establishing the Blood Group status of an individual.

Factors related to asymptomatic or severe COVID-19 infection

The factors that may contribute to a COVID-19 patient remaining in the asymptomatic stage, or to the infection evolving into the more serious stages are examined. In particular, we refer to the TMPRSS2 expression profile, balance of androgen and estrogen, blood group-A and/or B, nonsynonymous mutations in ORF3, and proteins NS7b and NS8 in SARS-CoV-2. Also, we review other factors related to the susceptibility and pathogenicity of SARS-CoV-2.

Diverse molecular recognition properties of blood group A binding monoclonal antibodies.

Information about specificity and affinity is critical for use of carbohydrate-binding antibodies. Herein, we evaluated eight monoclonal antibodies to the blood group A (BG-A) antigen. Antibodies 87-G, 9A, HE-10, HE-24, HE-193, HE-195, T36 and Z2A were profiled on a glycan microarray to assess specificity, relative affinity and the influence of glycan density on recognition. Our studies highlight several noteworthy recognition properties. First, most antibodies bound GalNAcα1-3Gal and the BG-A trisaccharide nearly as well as larger BG-A oligosaccharides. Second, several antibodies only bound the BG-A trisaccharide when displayed on certain glycan chains. These first two points indicate that the carrier glycan chains primarily influence selectivity, rather than binding strength. Third, binding of some antibodies was highly dependent on glycan density, illustrating the importance of glycan presentation for recognition. Fourth, some antibodies recognized the tumor-associated Tn antigen, and one antibody only bound the variant composed of a GalNAc-alpha-linked to a serine residue. Collectively, these results provide new insights into the recognition properties of anti-BG-A antibodies.

No evidence for a direct effect of von Willebrand factor's ABH blood group antigens on von Willebrand factor clearance

One of the major determinants of von Willebrand factor (VWF) plasma levels is ABO blood group status, and individuals with blood groupO have ~25% lower plasma levels. The exact mechanism behind this relationship remains unknown, although effects on clearance have been postulated. To determine whether clearance of VWF is directly dependent on the presence of ABH antigens on VWF. Three type3 von Willebrand disease (VWD) patients were infused with Haemate-P, and the relative loading of VWF with ABH antigens at different time points was measured. VWF-deficient mice were injected with purified plasma-derived human VWF obtained from donors with either blood groupA, blood groupB, or blood groupO. In mice, we found no difference in clearance rate between plasma-derived blood groupA, blood groupB and blood groupO VWF. Faster clearance of the blood groupO VWF present in Haemate-P infused in type3 VWD patients would have resulted in a relative increase in the loading of VWF with A and B antigens over time. However, we observed a two-fold decrease in the loading with A and B antigens in two out of three patients, and stable loading in the third patient. There is no direct effect of ABH antigens on VWF in VWF clearance. We demonstrate that, in a direct comparison within one individual, blood groupO VWF is not cleared faster than blood groupA or blood groupB VWF. Clearance differences between blood groupO and non-blood groupO individuals may therefore be related to the blood group status of the individual rather than the ABH antigen loading on VWF itself.

T-Cell Dependency of T-Independent (TI) Antigens: Antibody Response to Blood Group A-Antigen Requires CD4 T-Cells and CD40/CD40L Interaction

Introduction: Polysaccharides are considered TI antigens capable of eliciting antibody secretion without T-cell help. TNP-Ficoll is used as a model TI (type 2) antigen, but detailed mechanisms of B-cell responses remain unclear. We studied a T-cell role in the antibody response to polysaccharides, using a clinically relevant ABO antigen in its natural form. Methods: Mice (4-8 week-old) received three standardized immunizations (days 0- 7- 14) with human blood group-A erythrocyte membranes, TNP-Ficoll or sperm whale myoglobin (SPWM; protein); some groups received first injection in complete Freund's adjuvant then two boosts without adjuvant. For T-cell depletion studies, anti-CD4 (clone GK1.5) or isotype control were injected on day -1-0- +1. To further characterize direct and indirect interaction of CD40/CD40L, CD40L KO mice were injected with anti-CD40 (clone IC10) or isotype control in order to activate or block CD40 on B cells; CD40 KO mice were injected with mouse rCD40-Fc fusion protein to activate T-cells which in turn may activate B-cells through soluble factors. TLR contribution was studied in MyD88 KO. Anti-A antibodies were measured in plasma at day -1-14-21 by hemagglutination and ABO-ELISA, and TNP and SPWM antibodies by ELISA. Results: Natural anti-A antibodies were undetectable on day -1 in all groups, whereas anti-TNP antibody was present in young mice. A-erythrocytes elicited a substantial antibody response, which was abrogated by CD4 T-cell depletion (fig 1), including IgM (fig 2), whereas of SPWM antibodies, only IgG was absent with normal or low IgM and IgA. Antibodies to TNP-Ficoll were comparable in CD4-depleted vs. control mice. Similarly there were no differences in response to secondary A-antigen immunization when CD4 cells were depleted in pre-immunized mice. Anti-A antibodies were significantly reduced in CD40L KO, and further diminished with anti-CD40 antibody; no reduction was seen in MyD88 KO mice. Conclusions: This study clearly demonstrates that antibody response to A-antigen requires CD4 T-cells. Although polysaccharides may not stimulate MHC class II-dependent T-cell help, the presence of activated CD4 T-cells and their interaction with B-cells through CD40-CD40L (fig 2) is critical for B-cells to become antibody secreting cells. These findings have major implications for ABO-incompatible and xenotransplants.[Figure 1][Figure 2]

Glycan array analysis of the antigen repertoire targeted by tumor-binding antibodies

Immunization with whole cells has been used extensively to generate monoclonal antibodies, produce protective immune responses, and discover new disease antigens. While glycans are abundant on cell surfaces, anti-glycan immune responses have not been well-characterized. We used glycan microarrays to profile 49 tumor-binding monoclonal antibodies generated by immunizing mice with whole cancer cells. A substantial proportion (41%) of the tumor binding antibodies bound carbohydrate antigens. The antibodies primarily recognize a group of 5 glycan antigens: Sialyl Lewis A (SLeA), Lewis A (LeA), Lewis X (LeX), blood group A (BG-A), and blood group H on a type 2 chain (BG-H2). The results have important implications for monoclonal antibody production and cancer vaccine development.

Glycosylation changes in different developmental stages of Trichinella

AbstractThe in situ identification of carbohydrate structures in Trichinella spiralis intestinal larvae, adults and L1 muscular larvae was carried out by lectin histochemistry, with emphasis on the O-linked glycans. The absence of reactivity with two lectins-TML and MAL indicated that Trichinella spiralis does not synthesize sialic acid. Reactivity with HPA, VVL-B4, PNA and UEA-I staining suggested that T. spiralis synthesizes and expresses on its cuticle O-linked glycans analogous to Tn-antigen (GalNAc-α-Ser/Thr), T-antigen (Gal-β1,3-GalNAc-α-Ser/Thr) and also structures analogous to A-blood group antigens (GalNAc-α1,3-Gal-β1,3(4)-(Fuc-α1,2-)-R). Expression of the saccharidic moieties is stage-specific. Blood group-A and T-antigen structures were identified on the cuticle of the intestinal and muscular larvae. The Tn-antigen structure was missing in the intestinal larvae. Appropriate ligands for WGA were not identified in the adult individuals. The obtained results may contribute to a better understanding of the glycobiology of this parasitic nematode in relation to occupation of its intracellular niche. The presence of saccharidic structures analogous to some of those expressed on the intestinal epithelial cells may serve as a protective shield on the surface of the parasite.

The cell surface carbohydrate blood group A regulates the selective fasciculation of regenerating accessory olfactory axons

Cell surface carbohydrates are differentially expressed by discrete subpopulations of primary sensory axons in the mammalian main and accessory olfactory systems. It has been proposed that these carbohydrates provide a glycocode which mediates the sorting of these sensory axons as they project from the olfactory neuroepithelium to their central targets in the main and accessory olfactory bulbs during development. As the differential expression of cell surface carbohydrates on olfactory axons persists in the adult we have now investigated their role during regeneration. We have recently generated a line of transgenic mice, BGAT-Tg, that mis-express the blood group A (BGA) carbohydrate on all primary olfactory axons rather than just on accessory olfactory axons as in wild-type mice. Following unilateral bulbectomy, accessory and main olfactory axons regenerate and grow into the frontal cortex where they fill the cavity which remains after the olfactory bulb ablation. In wild-type mice, the regenerating BGA-expressing accessory olfactory axons selectively aggregated with each other in large bundles but clearly separated from the BGA-negative main olfactory axons. In contrast, in the BGAT-Tg transgenic mice in which all main and accessory axons express the BGA carbohydrate, the accessory olfactory axons failed to correctly separate from the main olfactory axons. Instead, these axons formed numerous small bundles interspersed with main olfactory axons. These data provide strong evidence that the restricted expression of BGA is in part responsible for the selective segregation of accessory olfactory axons.

Evidence of Immune Tolerance to Blood Group Antigens in a Case of ABO‐Incompatible Pediatric Liver Transplantation

In a 12-year-old patient with blood group O, who had received a partial liver graft 10 years ago from his father with blood group A, the levels of anti-A-specific antibodies (Abs) were persistently undetectable after the transplantation, while the levels of anti-B-specific Abs gradually increased and attained a plateau. Peripheral blood mononuclear cells (PBMCs) from this patient were engrafted into NOD/SCID mouse in order to investigate the immune response to donor-type blood group antigens. Even after sensitization with blood group-A erythrocytes, no anti-A Abs were detected in the serum samples of the mouse that received PBMCs from the blood group-O recipient of group-A liver allograft, however, immunoglobulins specific for antigens other than the A antigens were produced. Thus, we provide a possible evidence of immune tolerance to blood group antigens in this ABO-incompatible pediatric liver transplantation.

Modification of blood group A expression in human pancreatic tumor cell lines by inhibitors of N-glycan processing.

Pancreatic adenocarcinomas induced in Syrian hamsters by N-nitrosobis (2-oxopropyl)amine (BOP) treatment express blood group A (BGA) antigen, which was previously shown by this lab to be expressed on multiantennary asparagine (Asn)-linked glycans attached to membrane glycoproteins. To determine if a similar expression pattern was found in humans, three human pancreatic ductal adenocarcinoma cell lines (CD18, CD11, and Capan 1) from individuals of blood type A were analyzed and shown to express BGA antigen on membrane glycoproteins similar in molecular mass to those found in hamster tumor cells. The BGA antigen was located on Asn-linked oligosaccharides in all three human cell lines, as indicated by loss of activity after peptide:N-glycosidase F (PNGase F) treatment. Also, as shown previously in hamster pancreatic tumor cells, BGA expression at the surface of the human cell lines was blocked by growth of the cells in media containing deoxymannojirimycin (dMM), an inhibitor of mannosidase I. These results demonstrate that the BGA antigen is on Asn-linked glycans in human pancreatic adenocarcinoma cells and that these glycoproteins are processed similarly to the BGA glycoproteins in hamster pancreatic adenocarcinoma.

Glycan Structure of Blood Group-A Antigen in Hamster Normal Tissues and Pancreatic Cancers

Pancreatic cancers induced by N-nitrosobis(2-oxopropyl)amine in Syrian hamsters produce blood group A antigen. The glycan structure of the blood group A antigen-bearing glycoproteins purified from pancreatic cancer cells has been shown previously to be bound to Asn-linked complex oligosaccharides. Because blood group A antigen has usually been described as being on Ser/Thr-linked glycans, the distribution and glycan-protein linkage of the antigen were examined in normal hamster tissues in comparison with the findings on pancreatic cancer cells. The gastrointestinal tract, excluding the small intestine, expressed blood group A antigen. The liver, pancreas, and gallbladder did not show blood group A reactivity. Blood group A antigen in the proximal gastrointestinal tract was resistant to peptide N-glycosidase F digestion, which cleaves Asn-linked glycans from core proteins. Blood group A antigen was peptide N-glycosidase F sensitive in membrane preparations from pancreatic cancers. In the colon, this antigen was only partially removed by peptide- N-glycosidase F. These results demonstrate a difference in the structure of blood group A antigen-associated glycan between pancreatic cancers and normal hamster gastrointestinal tissues.

Relationship between blood group-A antigen expression and malignant potential in hamster pancreatic cancers.

The loss of expression of the ABH blood group antigens is suggested to be associated with more aggressive behavior of cancers. We have compared the growth behaviors of two hamster pancreatic cancer cell lines with different blood group-A expressions. PC-1.0 cells, which expressed blood group-A antigen poorly, showed a faster growth in vitro and in vivo when implanted into the pancreas of homologous animals, whereas PC-1.2 cells, all of which express the antigen, had a slower growth rate both in vitro and in vivo. PC-1.0 also tended to metastasize, whereas PC-1.2 cells grew primarily locally. The allografts of both PC-1.2 cells (PC-1.2AG) and PC-1.0 cells (PC-1.0AG) and the metastases of PC-1.0 cells expressed blood group A antigen in a similar rate. There was no significant difference in the number of A-antigen positive cells (A+) between the PC-1.2AG and PC-1.0AG, although the expression of A antigen in PC-1.0AG showed a greater heterogeneity. The combined immunohistochemistry and autoradiography did not show any significant differences in the labeling index of A+ or A- cells between the two allografts. Thus, the results indicate that blood group A antigen expression is unrelated to malignancy in this model. The faster growth rate of PC-1.0 cells may be due to their shorter cell cycle.

UDP-GalNAc:Fuc alpha 1-2Gal alpha 1-3GalNAc transferase activity in hamster pancreatic cancers and in normal hamster alimentary tissues.

Ductal adenocarcinomas induced by N-nitrosobis(2-oxopropyl)amine treatment in Syrian hamsters produce blood group-A antigen, which is not present in normal hamster pancreas. To understand the underlying mechanism of A antigen neoexpression in pancreatic cancer cells, we examined the activity of UDP-GalNAc:Fuc alpha 1-2Gal alpha 1-3GalNAc transferase (A-transferase), the enzyme responsible for blood group-A antigen production. The specific activity of A-transferase in the pancreatic cancers was approximately 8 nmol/mg protein/h in membrane preparations, 0.3 nmol/mg protein/h in whole cell extracts, and undetectable in normal hamster pancreas. Significant A-transferase activity was found in normal tissues expressing blood group-A antigen. Although both normal (gastric antrum, colon) and pancreatic cancer cells showed similar enzymatic characteristics (optimal pH, substrate affinity, optimal [Mn2+]), there was a difference in the requirement for divalent cations. The A-transferase in cancer cells showed a more stringent requirement for Mn2+. These results suggest that A-transferase is activated during nitrosamine-induced pancreatic carcinogenesis, which results in the neoexpression of blood group-A antigen. The difference in divalent cation requirements between A-transferase activities of cancer and normal cells may indicate that there are multiple A-transferases present in hamster tissues.

Specific biodetection of a murine spontaneous mammary carcinoma with labelled anti-human blood group-A monoclonal antibody

The expression of cell surface antigens of the spontaneous transplantable M3-murine tumour was studied by means of the monoclonal antibody (MAb) B2C114 which recognizes the human blood group-A carbohydrate antigen. Following radioiodination the MAb retained their immunoreactivity and demonstrated a significantly higher in vitro binding with isolated M3-tumour cells as compared with a control antibody. B2C114 revealed 10 6 antigenic sites per cell, with a constant affinity of 5.1 × 10 9/M. Biodistribution studies showed that B2C114 discriminated between malignant tumour and mouse normal tissues. Radioimmunodetection of Balb/c mice bearing s.c. M3-tumour showed that tumour was specifically defined without substraction 1 day after injection of the radiolabelled antibody.

Purification and analysis of glycoproteins bearing blood group-A determinants from hamster pancreatic ductal adenocarcinomas.

Although the hamster pancreas does not express A, B or H blood group antigens, all hamster pancreatic ductal adenocarcinomas induced by treatment with N-nitrosobis(2-oxopropyl)amine express blood group-A antigen. Thus, the acquisition of blood group-A antigen expression in this system is a cancer-associated alteration. We have purified three major blood group-A antigen bearing glycoproteins (gp120, gp135 and gp150) from hamster pancreatic cancer cell membrane preparations using affinity chromatography on DBA (Dolichos biflorus) agglutinin-agarose. When assayed by immunoblotting, gp120 and gp135 showed strong blood group-A reactivity, which was removed by treating membrane samples with peptide-N-glycosidase F. Blood group-A reactivity was unchanged by treatment of the membrane fractions with endoglycosidases F and H. In addition, these two glycoproteins bearing blood group-A antigen also bound L-PHA (Phaseolus vulgaris leucoagglutinin). These results demonstrate that gp120 and gp135 express blood group-A antigen on Asn-linked multi-antennary complex type glycan structures. The gp150 showed weak blood group-A expression. This is the first demonstration of the neoexpression of cancer-associated blood group-A determinants which reside on Asn-linked glycan structures.

177 - Experimental Immunotherapy of Xenografted Bladder Cancer in Nude Mice Using A Monoclonal Antibody Recognizing Blood Group-A Antigen

No AccessJournal of Urology1 Jun 1987Experimental Immunotherapy of Xenografted Bladder Cancer in Nude Mice Using A Monoclonal Antibody Recognizing Blood Group-A Antigen Dah-Shyong Yu, Ming-Yang Yeh, Sun-Yran Chang, Cheng-Ping Ma, Shou-Hwa Han, and T. Ming Chu Dah-Shyong YuDah-Shyong Yu More articles by this author , Ming-Yang YehMing-Yang Yeh More articles by this author , Sun-Yran ChangSun-Yran Chang More articles by this author , Cheng-Ping MaCheng-Ping Ma More articles by this author , Shou-Hwa HanShou-Hwa Han More articles by this author , and T. Ming ChuT. Ming Chu More articles by this author View All Author Informationhttps://doi.org/10.1016/S0022-5347(17)75327-XAboutPDF ToolsAdd to favoritesDownload CitationsTrack CitationsPermissionsReprints ShareFacebookLinked InTwitterEmail "Experimental Immunotherapy of Xenografted Bladder Cancer in Nude Mice Using A Monoclonal Antibody Recognizing Blood Group-A Antigen." The Journal of Urology, 137(6), p. 148A © 1987 by The American Urological Association Education and Research, Inc.FiguresReferencesRelatedDetailsCited byYu D, Chu T, Yeh M, Chang S, Ma C and Han S (2018) Antitumor Activity of Doxorubicin-Monoclonal Antibody Conjugate on Human Bladder CancerJournal of Urology, VOL. 140, NO. 2, (415-421), Online publication date: 1-Aug-1988. Volume 137Issue 6June 1987Page: 148A Advertisement Copyright & Permissions© 1987 by The American Urological Association Education and Research, Inc.MetricsAuthor Information Dah-Shyong Yu More articles by this author Ming-Yang Yeh More articles by this author Sun-Yran Chang More articles by this author Cheng-Ping Ma More articles by this author Shou-Hwa Han More articles by this author T. Ming Chu More articles by this author Expand All Advertisement PDF downloadLoading ...