Carbohydrate-specific monoclonal antibodies bind to human granulocytes and stimulate antibody-dependent cellular cytotoxicity

Spitalnik, Patrice F.; Spitalnik, Steven L.; Danley, J. M.; Lopez, Angel F.; Vadas, Mathew A.; Civin, CI; Ginsburg, Victor

doi:10.1016/0003-9861(89)90267-1

Cited by 7 publications

(4 citation statements)

References 41 publications

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“…Therefore, the fucosyl-A-acetyllactosamine residues expressed on Leu-CAMs might be important for initial interaction with ligands such as ICAM-1 and 1CAM-2 (Rothlein et al, 1986;Patarroyo et al, 1987;Staunton et al, 1989). The presence of fucosyl-A-acetyllactosamine on CDlla/CD18 has previously been demonstrated by using a monoclonal antibody (Spitalnik et al, 1989).…”

Section: Discussionmentioning

confidence: 99%

Structural study of the sugar chains of human leukocyte cell adhesion molecules CD11/CD18

Asada¹,

Furukawa²,

Kantor³

et al. 1991

Biochemistry

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Leu-CAMs (CD11/CD18) consisting of LFA-1, Mac-1, and p150/95 are leukocyte cell surface glycoproteins that are involved in various leukocyte functions. The asparagine-linked sugar chains were released as oligosaccharides from Leu-CAMs by hydrazinolysis. About 12 mol of sugar chains was released from 1 mol of Leu-CAMs. These sugar chains were converted to radioactive oligosaccharides by reduction with sodium borotritide and separated into neutral and acidic fractions by paper electrophoresis. All of the acidic oligosaccharides were converted to neutral ones by digestion with sialidase, indicating that they are sialyl derivatives. The neutral and sialdase-treated acidic oligosaccharides were fractionated by chromatography on lectin columns followed by Bio-Gel P-4 column chromatography. Structural studies of each oligosaccharide by sequential exo- and endoglycosidase digestion and by methylation analysis revealed that Leu-CAMs contain mainly high mannose type and high molecular weight complex type sugar chains. The latter sugar chains were of bi-, tri-, and tetraantennary complex types with the Gal beta 1----4(Fuc alpha 1----3)GlcNAc beta 1----and/or the Gal beta 1----3GlcNAc beta 1----groups together with the Gal beta 1----4GlcNAc group in their outer-chain moieties. In addition to these sugar chains, a small amount of monoantennary complex type and hybrid type sugar chains was found in Leu-CAMs. Furthermore, analysis of the asparagine-linked sugar chains released from the beta-subunit of Leu-CAMs by a series of lectin chromatography showed that subunit-specific glycosylation is not observed between the alpha- and beta-subunits of Leu-CAMs.

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Section: Discussionmentioning

confidence: 99%

Structural study of the sugar chains of human leukocyte cell adhesion molecules CD11/CD18

Asada¹,

Furukawa²,

Kantor³

et al. 1991

Biochemistry

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“…Neutrophils (or G-MDSCs) are found to be CD14 neg/low and CD15 pos , whereas monocytes (or Mo-MDSCs) are CD14 high and CD15 neg/low [35]. Unfortunately, these two markers are not sufficient to identify neutrophils, as eosinophils have a similar CD15 expression [41]. We suggest CD16 as an additional marker, as mature neutrophils are CD16 high , eosinophils are CD16 neg , and monocytes either CD16 neg or CD16 int .…”

Section: Identification Of Neutrophils and G-mdscsmentioning

confidence: 99%

Immune suppression by neutrophils and granulocytic myeloid-derived suppressor cells: similarities and differences

Pillay

Tak

Kamp

et al. 2013

Cell. Mol. Life Sci.

333

339

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Neutrophils are essential effector cells in the host defense against invading pathogens. Recently, novel neutrophil functions have emerged in addition to their classical anti-microbial role. One of these functions is the suppression of T cell responses. In this respect, neutrophils share similarities with granulocytic myeloid-derived suppressor cells (G-MDSCs). In this review, we will discuss the similarities and differences between neutrophils and G-MDSCs. Various types of G-MDSCs have been described, ranging from immature to mature cells shaping the immune response by different immune suppressive mechanisms. However, all types of G-MDSCs share distinct features of neutrophils, such as surface markers and morphology. We propose that G-MDSCs are heterogeneous and represent novel phenotypes of neutrophils, capable of suppressing the immune response. In this review, we will attempt to clarify the differences and similarities between neutrophils and G-MDSCs and attempt to facilitate further research.

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“…The structures Gal/31-4(Fuced-3)GlcNAc (Le x or CD15), and Neu5Aca2-3Galf31-4(Fucod-3)GlcNAc (sialyl-Le ~) are present as nonreducing termini on polylactosaminoglycans isolated from human neutrophil glycopeptides (11,50). Le x, which is also present on neutrophil glycolipids (12), is recognized by a number of mAbs specific for neutrophils and monocytes (18,47,49,54,57). Our neuraminidase and protease studies indicate that Le x per se cannot constitute the recognition structure for GMP-140.…”

Section: Table II Effect Of Anti-le • Mab or Neoglycoproteins On [~2~i]gmp-140 Binding To Neutrophilsmentioning

confidence: 99%

GMP-140 binds to a glycoprotein receptor on human neutrophils: evidence for a lectin-like interaction.

Moore

Varki

McEver

1991

The Journal of Cell Biology

237

147

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Abstract. GMP-140 is a rapidly inducible receptor for neutrophils and monocytes expressed on activated platelets and endothelial cells. It is a member of the selectin family of lectin-like cell surface molecules that mediate leukocyte adhesion. We used a radioligand binding assay to characterize the interaction of purified GMP-140 with human neutrophils. Unstimulated neutrophils rapidly bound [12~I]GMP-140 at 4°C, reaching equilibrium in 10-15 min. Binding was Ca 2÷ dependent, reversible, and saturable at 3-6 nM free GMP-140 with half-maximal binding at =1.5 nM. Receptor density and apparent affinity were not altered when neutrophils were stimulated with 4/~-phorbol 12-myristate 13-acetate. Treatment of neutrophils with proteases abolished specific binding of [125I]GMP-140. Binding was also diminished when neutrophils were treated with neuraminidase from Vibrio cholerae, which cleaves ix2-3-, a2-6-, and ot2-8-1inked sialic acids, or from Newcastle disease virus, which cleaves only a2-3-and tx2-8-1inked sialic acids. Binding was not inhibited by an mAb to the abundant myeloid oligosaccharide, Le x (CD15), or by the neoglycoproteins Lex-BSA and sialyl-Le~-BSA. We conclude that neutrophils constitutively express a glycoprotein receptor for GMP-140, which contains sialic acid residues that are essential for function. These findings support the concept that GMP-140 interacts with leukocytes by a lectin-like mechanism.

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Carbohydrate-specific monoclonal antibodies bind to human granulocytes and stimulate antibody-dependent cellular cytotoxicity

Cited by 7 publications

References 41 publications

Structural study of the sugar chains of human leukocyte cell adhesion molecules CD11/CD18

Structural study of the sugar chains of human leukocyte cell adhesion molecules CD11/CD18

Immune suppression by neutrophils and granulocytic myeloid-derived suppressor cells: similarities and differences

GMP-140 binds to a glycoprotein receptor on human neutrophils: evidence for a lectin-like interaction.

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