Identification of erythrocyte Gal alpha 1-3Gal glycosphingolipids with a mouse monoclonal antibody, Gal-13.

Galili, Uri; Basbaum, Carol; Shohet, Stephen B.; Buehler, Joanne; Macher, Bruce A.

doi:10.1016/s0021-9258(18)61249-9

Cited by 90 publications

(10 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In view of our recent studies (Galili et al, 1988) on the expression of Galal-3Gal/S-4GlcNAc residues on mouse myeloma cells and the activity of the enzyme al-3 galactosyltransferasc in these cells, we hypothesized that the secretory product, i.e., IgG molecules synthesized by mouse myeloma cells, may also have Galal-3Galj31-4GlcNAc residues. To study this possibility, we used the mouse monoclonal IgG antibody designated (Galili et al, 1987c) as a representative mouse monoclonal IgG. As seen in Figure 6, anti-Gal bound to the heavy chain of mouse IgG.…”

Section: Resultsmentioning

confidence: 99%

Distribution of Gal.alpha.1.fwdarw.3Gal.beta.1.fwdarw.4GlcNAc residues on secreted mammalian glycoproteins (thyroglobulin, fibrinogen, and immunoglobulin G) as measured by a sensitive solid-phase radioimmunoassay

Thall¹,

Galili²

1990

Biochemistry

133

View full text Add to dashboard Cite

The study of the expression of Gal alpha 1----3Gal beta 1----4GlcNAc residues on mammalian glycoconjugates is of particular interest since as many as 1% of circulating IgG antibodies in man (the natural anti-Gal antibody) interact specifically with this carbohydrate residue. In recent studies, we have found that Gal alpha 1----3Gal beta 1----4GlcNAc residues are abundant on red cells and nucleated cells of nonprimate mammals, prosimians, and New World monkeys, but their expression is diminished in Old World monkeys, apes, and humans. In the present work, we have analyzed the expression of these residues on secreted mammalian glycoproteins. For this purpose, we have developed a radioimmunoassay (RIA) which enables the quantification of Gal alpha 1----3Gal beta 1----4GlcNAc residues on the secreted glycoproteins. Purified biotinylated anti-Gal was used as the antibody in the RIA, and bovine thyroglobulin enriched for Gal alpha 1----3Gal beta 1----4GlcNAc residues served as a solid-phase antigen. In this study, it is reported for the first time that the evolutionary pattern of Gal alpha 1----3Gal beta 1----4GlcNAc residue distribution in in vivo secreted glycoproteins is similar to that observed in membranes of cell lines and of red cells. Thyroglobulin, fibrinogen, or IgG molecules from nonprimate mammals and from New World monkeys express varying amounts of Gal alpha 1----3Gal beta 1----4GlcNAc residues ranging between 0.01 and 11 residues per molecule, whereas no such residues are present on any of these glycoproteins of human or Old World monkey origin.(ABSTRACT TRUNCATED AT 250 WORDS)

show abstract

Section: Resultsmentioning

confidence: 99%

Distribution of Gal.alpha.1.fwdarw.3Gal.beta.1.fwdarw.4GlcNAc residues on secreted mammalian glycoproteins (thyroglobulin, fibrinogen, and immunoglobulin G) as measured by a sensitive solid-phase radioimmunoassay

Thall¹,

Galili²

1990

Biochemistry

133

View full text Add to dashboard Cite

show abstract

“…Glycosphingolipids. Total neutral glycosphingolipids from human erythrocytes were purified by standard procedures (30) . Preparation of other glycosphingolipids has been described previously (30,31) .…”

Section: Methodsmentioning

confidence: 99%

Lipooligosaccharides (LOS) of Neisseria gonorrhoeae and Neisseria meningitidis have components that are immunochemically similar to precursors of human blood group antigens. Carbohydrate sequence specificity of the mouse monoclonal antibodies that recognize crossreacting antigens on LOS and human erythrocytes.

Mandrell

Griffiss

Macher

1988

The Journal of Experimental Medicine

252

167

View full text Add to dashboard Cite

We have used mouse mAbs, 3F11 and 06B4, that are specific for highly conserved epitopes of Neisseria gonorrhoeae lipooligosaccharides (LOS) to identify immunochemically similar structures on human erythrocytes. mAb 3F11 agglutinated erythrocytes from all randomly selected adult humans, while mAb 06B4 agglutinated only 80% of the same specimens. The antibodies had an activity with erythrocytes similar to human cold agglutinins in that agglutination occurred at 4 degrees C and decreased with increasing incubation temperature. Human infant erythrocytes were agglutinated less well, but enzymatic treatment of either infant or adult cells resulted in an increase in expression of the 3F11- and 06B4-defined epitopes. Both antibodies bound to a series of neutral glycosphingolipids from human erythrocytes and neutrophils that have a type 2 (Gal beta 1----4GlcNAc) or N-acetyllactosamine structure. Neither antibody bound to glycosphingolipids from human meconium, which have a type 1 (Gal beta 1----3GlcNAc) structure. The antibodies were unable to bind to N-acetyl-lactosamine glycosphingolipids with a nonreducing terminal sialic acid or a Gala1----3Gal disaccharide. Antibody binding also was blocked by the presence of fucose linked to the penultimate glucosamine residue of N-acetyllactosamine glycosphingolipids. Although both antibodies bound to linear and branched-chain N-acetyllactosamine glycosphingolipids, 3F11 had a higher affinity for branched structures than did 06B4. The activity of 3F11 with human adult and infant treated and untreated erythrocytes with N-acetyllactosamine glycosphingolipids, and with LOS was very similar, if not identical, in specificity to 1B2, an mAb prepared from mice inoculated with a linear N-acetyllactosamine glycosphingolipid.

show abstract

“…The binding of αGal-reactive Abs to glycosphingolipids depends on the avidity of Abs. For example, anti-αGal IgG with high avidity for B di -PG binds to rabbit erythrocyte glycosphingolipids, similar to monoclonal Abs Gal-13, while cross-reactive anti-A di IgG with lower avidity for B di -PG does not bind [40,44]. The range of IC 50 for PGs with isolated Abs was from 2 × 10 −8 to 7 × 10 −6 M. These results were obtained by affinity chromatography using a solution of 8 M urea for elution of Abs at lower temperatures (4-10 • C), with gradual removal of urea by dialysis, which may be preferable in order to restore the activity of AG Abs.…”

Section: Study Of the Ag Abs Specificitymentioning

confidence: 97%

Prospects and Challenges of the Study of Anti-Glycan Antibodies and Microbiota for the Monitoring of Gastrointestinal Cancer

Smorodin

2021

IJMS

View full text Add to dashboard Cite

Over the past decades, a large amount of data has been accumulated in various subfields of glycobiology. However, much clinically relevant data and many tools are still not widely used in medicine. Synthetic glycoconjugates with the known structure of glycans are an accurate tool for the study of glycan-binding proteins. We used polyacrylamide glycoconjugates (PGs) including PGs with tumour-associated glycans (TAGs) in immunoassays to assess the prognostic potential of the serum level of anti-glycan antibodies (AG Abs) in gastrointestinal cancer patients and found an association of AG Abs with survival. The specificity of affinity-isolated AG Abs was investigated using synthetic and natural glycoconjugates. AG Abs showed mainly a low specificity to tumour-associated and tumour-derived mucins; therefore, the protective role of the examined circulating AG Abs against cancer remains a challenge. In this review, our findings are analysed and discussed in the context of the contribution of bacteria to the AG Abs stimulus and cancer progression. Examples of the influence of pathogenic bacteria colonising tumours on cancer progression and patient survival through mechanisms of interaction with tumours and dysregulated immune response are considered. The possibilities and problems of the integrative study of AG Abs and the microbiome using high-performance technologies are discussed.

show abstract

Identification of erythrocyte Gal alpha 1-3Gal glycosphingolipids with a mouse monoclonal antibody, Gal-13.

Cited by 90 publications

References 28 publications

Distribution of Gal.alpha.1.fwdarw.3Gal.beta.1.fwdarw.4GlcNAc residues on secreted mammalian glycoproteins (thyroglobulin, fibrinogen, and immunoglobulin G) as measured by a sensitive solid-phase radioimmunoassay

Distribution of Gal.alpha.1.fwdarw.3Gal.beta.1.fwdarw.4GlcNAc residues on secreted mammalian glycoproteins (thyroglobulin, fibrinogen, and immunoglobulin G) as measured by a sensitive solid-phase radioimmunoassay

Prospects and Challenges of the Study of Anti-Glycan Antibodies and Microbiota for the Monitoring of Gastrointestinal Cancer

Contact Info

Product

Resources

About