Disease relevance of Erythrocyte T antigen

• Immunological studies from this population have shown that protection from amebiasis is associated with mucosal anti-E. histolytica Gal/GalNAc lectin antibodies, suggesting that a vaccine is an achievable goal [1].
• E. coli adhesins showed no blood group specificity, excepting 1 cancer isolate (HM44) with specificity for the Thomsen-Friedenreich antigen, but they could be blocked by soluble plantain fiber [2].
• Association of exposed Thomsen-Friedenreich antigen (T antigen) and acute renal failure in septic patients [3].
• For detection of a subpopulation of patients with Grade II carcinomas who were at high risk for development of subsequent invasion, combinations of markers, especially hyperdiploidy and abnormal expression of the Thomsen-Friedenreich antigen, were significantly more effective than any single marker system [4].
• To check the usefulness of this marker and technology in identifying cancers and precancers of other organs, we have assessed the differential expression of Gal-GalNAc in various adenocarcinomas and their corresponding normal tissues [5].

High impact information on Erythrocyte T antigen

• Gas-liquid chromatography-mass spectrometric analysis has shown that the purified LPS contained Gal, GalNAc, and NeuAc, which are sugar components of GM1 ganglioside [6].
• Flow cytometry revealed that a single treatment induced de novo expression of the Thomsen-Friedenreich antigen (Gal beta 1-3GalNAc-R), the product of beta 3Gal-T activity [7].
• Establishment of adherence by Entamoeba histolytica is mediated by a 170-kD Gal/GalNAc inhibitable lectin and is required for cytolysis and phagocytosis of mammalian target cells [8].
• The prespore vesicle (PSV) is an organelle which secretes spore coat proteins and gal/galNAc polysaccharides from prespore cells of Dictyostelium [9].
• By combining the techniques of protein A-gold immunocytochemistry and ricin-gold affinity cytochemistry we have demonstrated colocalization of the lysosomal enzyme alpha-mannosidase with gal/galNAc polysaccharides in prespore vesicles and the spore coat [9].

Chemical compound and disease context of Erythrocyte T antigen

• Jacalin, an alpha-O-glycoside of the disaccharide Thomsen-Friedenreich antigen (galactose beta1-3 N-acetylgalactosamine, T-antigen)-specific lectin from jackfruit seeds, has been shown to induce mitogenic responses and to block infection by HIV-1 in CD4(+) T lymphocytes [10].
• These cytoplasmic blebs were rich in Man, GlcNAc, Gal/GalNac, Fuc, NeuAc(alpha2,6)Gal, and oligosaccharides [11].
• Thomsen-Friedenreich antigen expression in gastric carcinomas is associated with MUC1 mucin VNTR polymorphism [12].
• Immunohistochemical examinations using these seven of eight antibodies except for TFA and routinely processed formalin-fixed and paraffin-embedded tissue specimens are beneficial in differentiating EOSC from other skin cancers [13].

Biological context of Erythrocyte T antigen

• The tumor-associated carbohydrate Thomsen-Friedenreich antigen (T antigen) and beta-galactoside binding lectins (galectins) have been implicated in tumor cell adhesion and tissue invasion [14].
• Imparting exquisite specificity to peanut agglutinin for the tumor-associated Thomsen-Friedenreich antigen by redesign of its combining site [15].
• To study transcriptional regulation in the lower branching eukaryote Entamoeba histolytica, we have identified two sequence-specific DNA-binding proteins that recognize the upstream regulatory element URE4, an enhancer that regulates expression of the Gal/GalNAc lectin heavy subunit gene hgl5 [16].
• These findings suggest that the 35 kDa subunit may have a specific function in the pathogenic pathway and provides a new insight into the role of this component of the Gal/GalNac lectin complex in amoebic virulence [17].
• These findings indicate that endocytosis of HAsTf-3 is mediated by the Gal/GalNAc-specific lectin and not by transferrin receptors [18].

Anatomical context of Erythrocyte T antigen

• These two ligands are recognized and internalized by the Gal/GalNAc receptor system of hepatocytes [19].
• The Thomsen-Friedenreich antigen (T-antigen) is a cryptic disaccharide structure on human erythrocytes and is supposed to be expressed in an unhidden form on carcinoma cells [20].
• Effects of Thomsen-Friedenreich antigen-specific peptide P-30 on beta-galactoside-mediated homotypic aggregation and adhesion to the endothelium of MDA-MB-435 human breast carcinoma cells [14].
• Leukocyte migration inhibition responses to MCF-7, murine mammary tumor virus, and Thomsen-Friedenreich antigen in a series of cancer patients [21].
• Specificity of reagents directed to the Thomsen-Friedenreich antigen and their capacity to bind to the surface of human carcinoma cell lines [20].

Associations of Erythrocyte T antigen with other chemical compounds

• A newly isolated lectin, Amaranthus caudatus agglutinin (also called amaranthin or ACA), which binds to the Thomsen-Friedenreich antigen (T-antigen) and its sialylated variants, was used as a histochemical probe for proliferating cells in sections of human colonic tissues [22].
• The monosaccharides present after hydrolysis were those typically found in animal glycoproteins (Fuc, Man, Gal, GalNAc, and GlcNAc) [23].
• In vitro studies of E. histolytica-Jurkat T-cell interactions demonstrated that apoptosis required contact via the amoebic Gal/GalNAc lectin, but was unaffected by 75% inhibition of the amoebic cysteine proteinases [24].
• The binding affinity of synthetic bi- and triantennary galactose ligands (Kichler, A. and Schuber, F. (1995) Glycoconj. Chem., 12, 275 281) has been determined for the Gal/GalNAc receptors of rat hepatocytes and macrophages [25].
• Fucosylated Thomsen-Friedenreich antigen in alpha-anomeric configuration in human gastric surface epithelia: an allogeneic carbohydrate antigen possibly controlled by the Se gene [26].

Gene context of Erythrocyte T antigen

• Therefore, we tried to evaluate the role of different glycosylated and non-glycoslyated MUC1 epitopes as well as other mucin-associated peptides (MUC2) and carbohydrates (Thomsen-Friedenreich antigen, sialyl-Lewisa, sialyl-Lewisx) as predictors of the clinical course and prognosis in mammary carcinomas [27].
• Activation of MAPK kinase pathway by Gal/GalNAc adherence lectin of E. histolytica: gateway to host response [28].
• Gal(beta1-3)GalNAc binding sites did not have an obligatory co-localization with voltage-gated sodium channels or the potassium ion channels Kv1.1 and Kv1.5 and are thus not likely carried by these ion channels [29].
• Myosin II and the Gal-GalNAc lectin play a crucial role in tissue invasion by Entamoeba histolytica [30].
• Furthermore, most of the hybrid-type sugar chains of CD36 with the Gal/GalNAc beta 1-->4GlcNAc beta 1-->2 outer chain on their Man alpha 1-->3 arm contained an unusual Man alpha 1-->2Man alpha 1-->3 group on their Man alpha 1-->6 arm [31].

Analytical, diagnostic and therapeutic context of Erythrocyte T antigen

• Lymphocyte activation markers CD69 and HLA-DR were studied in metastatic breast and ovarian cancer patients who received active specific immunotherapy (ASI) using cancer vaccines containing the synthetic tumor-associated antigen sialyl-Tn or the Thomsen-Friedenreich antigen conjugated to KLH plus DETOX adjuvant [32].
• Topography of the combining region of a Thomsen-Friedenreich-antigen-specific lectin jacalin (Artocarpus integrifolia agglutinin). A thermodynamic and circular-dichroism spectroscopic study [33].
• Using three disaccharide (Thomsen-Friedenreich antigen; Gal beta 1,3GalNAc alpha 1,R)-binding pentadecapeptides without internal disulfide bridges as role models, we successfully tested a combined strategy with different techniques of NMR spectroscopy, electrospray ionization mass spectrometry, and molecular modeling [34].
• Those derived from SW 948 xenografts showed an enrichment of round, non-adherent cells, strongly reactive with the NeuAc alpha 2,6 Gal/GalNAc-specific lectin from Sambucus nigra (SNA), thus indicating that a selection of these cells has occurred [35].
• A protocol for transfusion of infants with erythrocyte T-antigen activation was evaluated for safety and effectiveness in a prospective, 3-year, sequential series of 1672 infants admitted for intensive care [36].

References