A novel carbohydrate, differentiation antigen on fucogangliosides of human myeloid cells recognized by monoclonal antibody VIM-2.

Macher, Bruce A.; Buehler, Joanne; Scudder, Peter; Knapp, Walter; Feizi, Ten

doi:10.1016/s0021-9258(19)81495-3

Cited by 104 publications

(8 citation statements)

References 21 publications

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“…A ganglioside with the same structure was originally isolated from chronic myelogenous leukemia cells and characterized (Fukuda et al, 1986). The terminal structure, including 2f3 NeuAc and 1f3 Fuc linked to two LacNAc units, was identified as an epitope defined by mAb VIM-2 (Macher et al, 1988) and was thought to be the E-selectin binding epitope (Tiemeyer et al, 1991). This structure does not bind to E-selectin under static conditions, as shown in our previous (Stroud et al, 1996a) and present study.…”

Section: Discussionsupporting

confidence: 74%

Sialosyl-Fucosyl Poly-LacNAc without the Sialosyl-Le^xEpitope as the Physiological Myeloid Cell Ligand in E-Selectin-Dependent Adhesion: Studies under Static and Dynamic Flow Conditions^,

1997

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The majority of E- and P-selectin ligands in leukocytes and myelocytic or monocytic leukemia cells are carried by transmembrane glycoproteins having a tandem repeat mucin-like domain through which O-linked carbohydrate ligands are carried. However, determination of structure and adhesive function of carbohydrates in glycoproteins is extremely difficult because of the extensive structural heterogeneity and the scarcity of material for functional analysis. We have overcome this difficulty through use of poly-LacNAc gangliosides isolated from a large quantity of ( approximately 1.2 L packed) HL60 cells [Stroud, M. R., Handa, K., Salyan, M. E. K., Ito, K., Levery, S. B., Hakomori, S., Reinhold, B. B., & Reinhold, V. N. (1996) Biochemistry 35, 758-769, 770-778]. We identified two major types of poly-LacNAc gangliosides without the sialosyl-Lex epitope as being capable of binding to E-selectin: (i) those having a single alpha1-->3 fucosylation at internal GlcNAcs but not at the penultimate GlcNAc and (ii) those having double alpha1-->3 fucosylation at internal GlcNAcs, excluding the penultimate GlcNAc. Gangliosides from group i above did not show any adhesion under static conditions, but showed strong adhesion under dynamic flow conditions. Gangliosides from group ii above showed adhesion under both static and dynamic conditions, as did sialosyl-Lex (SLex)-containing structures in previous studies. However, SLex-containing poly-LacNAc gangliosides are virtually absent or present in only trace quantities in leukocytes and HL60 cells. Poly-LacNAc gangliosides from groups i and ii above, lacking SLex structure, are the major membrane components of leukocytes and HL60 cells. These carbohydrates, bound to lipid or to protein, may therefore be the physiological epitope for E-selectin-dependent binding of these cells, particularly under dynamic flow conditions.

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Section: Discussionsupporting

confidence: 74%

Sialosyl-Fucosyl Poly-LacNAc without the Sialosyl-Le^xEpitope as the Physiological Myeloid Cell Ligand in E-Selectin-Dependent Adhesion: Studies under Static and Dynamic Flow Conditions^,

1997

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“…A range of glycan determinants are shown from disaccharides to octasaccharides. The boxed determinants are recognized with relatively high affinity and specificity by the following: A. galectin-3 and galectin-9; 41,[190][191][192][193][194][195] 107,108,134 G. Ricinus communis agglutinin-I (RCA-I); 217,218 H. mAb CHO-131 to Core 2 SLe x ; 219 I. poly-Le x antibody to circulating cathodic antigen; 220 J. P-type lectins; 39 K. asialoglycoprotein receptor (Gal/GalNAc lectin) in hepatocytes; 221 L. mAb to VIM-2 antigen; 222 M. P-and L-selectin; 34,121 N. cholera toxin; 183 O. cysteine-rich domain of the mannose/GalNAc-4-SO4 receptor; 223 P. mAb 114-4D12 to multifucosylated O-glycan of Schistosoma mansoni; 224 Q. anti-GQ1b IgG; 225 R. H/HS binding domain for antithrombin. [226][227][228] poly-N-acetyllactosamine, and the lack of recognition for many compounds containing b-galactosyl residues.…”

Section: Minimal or Partial Determinants-''necessary But Not Sufficie...mentioning

confidence: 99%

The repertoire of glycan determinants in the human glycome

2009

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The number of glycan determinants that comprise the human glycome is not known. This uncertainty arises from limited knowledge of the total number of distinct glycans and glycan structures in the human glycome, as well as limited information about the glycan determinants recognized by glycan-binding proteins (GBPs), which include lectins, receptors, toxins, microbial adhesins, antibodies, and enzymes. Available evidence indicates that GBP binding sites may accommodate glycan determinants made up of 2 to 6 linear monosaccharides, together with their potential side chains containing other sugars and modifications, such as sulfation, phosphorylation, and acetylation. Glycosaminoglycans, including heparin and heparan sulfate, comprise repeating disaccharide motifs, where a linear sequence of 5 to 6 monosaccharides may be required for recognition. Based on our current knowledge of the composition of the glycome and the size of GBP binding sites, glycoproteins and glycolipids may contain approximately 3000 glycan determinants with an additional approximately 4000 theoretical pentasaccharide sequences in glycosaminoglycans. These numbers provide an achievable target for new chemical and/or enzymatic syntheses, and raise new challenges for defining the total glycome and the determinants recognized by GBPs.

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“…There has been almost no unambiguous characterization of the real carbohydrate target structure of selectins present in normal human neutrophils or monocytic leukemia HL60 cells, because of the extreme difficulty of isolating and characterizing the essential epitope expressed in these cells. Tiemeyer et al (1991) claimed that GSLs with VIM-2 epitope structure (Macher et al, 1988) (same as Str VII in Table 1) are the E-selectin binding site. GSL with the same structure was previously isolated from a large quantity of myelogenous leukemia cells (Fukuda et al, 1984).…”

mentioning

confidence: 99%

Monosialogangliosides of Human Myelogenous Leukemia HL60 Cells and Normal Human Leukocytes. 1. Separation of E-Selectin Binding from Nonbinding Gangliosides, and Absence of Sialosyl-Le^x Having Tetraosyl to Octaosyl Core

Stroud¹,

Handa²,

Salyan³

et al. 1996

Biochemistry

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Previous studies suggested that sialosyl-Le(x) (SLex) is a ligand expressed in human neutrophils and myelogenous leukemia HL60 cells which binds to E-selectin and possibly P-selectin. However, clear data on structures of carbohydrate epitopes in these cells were lacking. A systematic study was therefore initiated, employing a large quantity of HL60 cells (> or = 1200 mL packed) and human leukocytes (approximately 100 mL packed). Gangliosides were extracted, followed by extensive fractionation and examination of the E- and P-selectin binding ability of each fraction. The following results were of particular interest: (i) Only monosialogangliosides having a polylactosamine core with > 10 monosaccharide units (or > 4 N-acetyllactosamine units) showed E-selectin binding under static conditions with thin-layer chromatography overlay technique employing 32P-labeled E-selectin-expressing CHO cells. (ii) Sulfate groups were not detectable in the binding fractions, and di- and trisialoganglioside fractions did not show E-selectin binding under these conditions. (iii) None of the fractions showed P-selectin binding under a similar assay system using 32P-labeled P-selectin-expressing CHO cells. (iv) Major gangliosides of HL60 cells were structures I-XI (shown in Table 1 of text), none of which showed E-selectin binding under the above conditions. (v) SLex gangliosides having tetraosyl to octaosyl ceramide core, which are the major gangliosides of epithelial tumors (shown in Table 2), were completely absent from HL60 cells and neutrophils. Isolation and chemical characterization of ganglioside structures I-XI are described in this paper.

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A novel carbohydrate, differentiation antigen on fucogangliosides of human myeloid cells recognized by monoclonal antibody VIM-2.

Cited by 104 publications

References 21 publications

Sialosyl-Fucosyl Poly-LacNAc without the Sialosyl-Le^xEpitope as the Physiological Myeloid Cell Ligand in E-Selectin-Dependent Adhesion: Studies under Static and Dynamic Flow Conditions^,

Sialosyl-Fucosyl Poly-LacNAc without the Sialosyl-Le^xEpitope as the Physiological Myeloid Cell Ligand in E-Selectin-Dependent Adhesion: Studies under Static and Dynamic Flow Conditions^,

The repertoire of glycan determinants in the human glycome

Monosialogangliosides of Human Myelogenous Leukemia HL60 Cells and Normal Human Leukocytes. 1. Separation of E-Selectin Binding from Nonbinding Gangliosides, and Absence of Sialosyl-Le^x Having Tetraosyl to Octaosyl Core

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A novel carbohydrate, differentiation antigen on fucogangliosides of human myeloid cells recognized by monoclonal antibody VIM-2.

Cited by 104 publications

References 21 publications

Sialosyl-Fucosyl Poly-LacNAc without the Sialosyl-LexEpitope as the Physiological Myeloid Cell Ligand in E-Selectin-Dependent Adhesion: Studies under Static and Dynamic Flow Conditions,

Sialosyl-Fucosyl Poly-LacNAc without the Sialosyl-LexEpitope as the Physiological Myeloid Cell Ligand in E-Selectin-Dependent Adhesion: Studies under Static and Dynamic Flow Conditions,

The repertoire of glycan determinants in the human glycome

Monosialogangliosides of Human Myelogenous Leukemia HL60 Cells and Normal Human Leukocytes. 1. Separation of E-Selectin Binding from Nonbinding Gangliosides, and Absence of Sialosyl-Lex Having Tetraosyl to Octaosyl Core

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Sialosyl-Fucosyl Poly-LacNAc without the Sialosyl-Le^xEpitope as the Physiological Myeloid Cell Ligand in E-Selectin-Dependent Adhesion: Studies under Static and Dynamic Flow Conditions^,

Sialosyl-Fucosyl Poly-LacNAc without the Sialosyl-Le^xEpitope as the Physiological Myeloid Cell Ligand in E-Selectin-Dependent Adhesion: Studies under Static and Dynamic Flow Conditions^,

Monosialogangliosides of Human Myelogenous Leukemia HL60 Cells and Normal Human Leukocytes. 1. Separation of E-Selectin Binding from Nonbinding Gangliosides, and Absence of Sialosyl-Le^x Having Tetraosyl to Octaosyl Core