A granulocyte reactive monoclonal antibody, 1G10, identifies the Gal beta 1-4 (Fuc alpha 1-3)GlcNAc (X determinant) expressed in HL-60 cells on both glycolipid and glycoprotein molecules

Urdal, D L; Brentnall, TA; Bernstein, ID; Hakomori, S

doi:10.1182/blood.v62.5.1022.bloodjournal6251022

Cited by 7 publications

(8 citation statements)

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“…We note here that in many cases, the abnormal glycosylation patterns in cancer cells are reminiscent of those expressed by cells of myeloid lineage. For example, expression of P1-6GlcNAc linked, polylactosamine antenna in N-linked structures is a common characteristic of malignant cells as well as normal granulocytes, and monocytes (Hakomori, 1996;Saitoh et al, 1992;Asada et al, 1997;Yoshimura et al, 1995;Yousefi et al, 1991;Shimodaira et al, 1997;F'ukuda, 1985fikuda et al, 1984;Gooi et al, 1983;Urdal et al, 1983;Skubitz et al, 1983;Feizi, 1985;fikushi et al, 1984;Dennis et al, 1987;Gorelik et al, 1997). The polylactosamine antennae are carriers of Lewis" (Le") and sialyl Le" structures, which are used by the above cell typea in aelectin binding interactions (Lowe et al, 1990;Phillips et al, 1990;Walz et al, 1990).…”

Section: Discussionmentioning

confidence: 99%

Melanoma × Macrophage Fusion Hybrids Acquire Increased Melanogenesis and Metastatic Potential: Altered N‐Glycosylation as an Underlying Mechanism

Sodi

Chakraborty

Platt

et al. 1998

Pigment Cell Research

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We recently reported that a majority of hybrids generated in vitro between weakly metastatic mouse Cloudman S91 melanoma cells and human or mouse macrophages showed enhanced metastatic potential. With few exceptions, hybrids with enhanced metastatic potential also had elevated basal melanin content and increased responsiveness to MSH compared to parental cells. Here we investigated the hybrid melanotic phenotype in more detail, comparing the pigmentary systems of hybrids and parental Cloudman S91 cells by several techniques. Cells were studied by electron microscopy, cell lysates were analyzed for tyrosinase (E.C.1.14.18.1) activity, and melanosomal proteins were analyzed by gel electrophoresis and immunoblotting. Melanosomes in parental Cloudman melanoma cells were few in number and relatively amorphous, whereas those in the hybrids were numerous and heavily pigmented, containing highly organized lattice structures. Both basal and MSH-inducible tyrosinase activities were elevated several fold in hybrids compared to parental cells. Tyrosinase, TRP-2, and LAMP-1 from hybrids migrated more slowly on gels compared to the same proteins from parental melanoma cells, consistent with increased glycosylation. Migration of LAMP-1 from hybrids was similar to that from peritoneal macrophages, which also appeared to be more heavily glycosylated than LAMP-1 from Cloudman cells. By using 3H-glucosamine as a marker of N-glycosylation, its incorporation into tyrosinase and LAMP-1 was found to be elevated in hybrids, suppressed by N-glycosylation inhibitors, and stimulated by MSH to a greater degree in hybrids compared to parental cells. These results indicate N-glycosylation as an important regulatory pathway for MSH-induced melanogenesis and further suggest that altered N-linked glycosylation may be an underlying mechanism for regulation of both melanogenesis and metastasis in macrophage x melanoma hybrids.

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Section: Discussionmentioning

confidence: 99%

Melanoma × Macrophage Fusion Hybrids Acquire Increased Melanogenesis and Metastatic Potential: Altered N‐Glycosylation as an Underlying Mechanism

Sodi

Chakraborty

Platt

et al. 1998

Pigment Cell Research

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“…The attached sulphate and sialic moieties are responsible for the strong negative charge on the mucin surface [14]. Presence of Lewis antigens is a modification of oligosaccharide chains [18,19,20,21].…”

Section: Introductionmentioning

confidence: 99%

Mucins: the Old, the New and the Promising Factors in Hepatobiliary Carcinogenesis

Kasprzak

Adamek

2019

IJMS

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Mucins are large O-glycoproteins with high carbohydrate content and marked diversity in both the apoprotein and the oligosaccharide moieties. All three mucin types, trans-membrane (e.g., MUC1, MUC4, MUC16), secreted (gel-forming) (e.g., MUC2, MUC5AC, MUC6) and soluble (non-gel-forming) (e.g., MUC7, MUC8, MUC9, MUC20), are critical in maintaining cellular functions, particularly those of epithelial surfaces. Their aberrant expression and/or altered subcellular localization is a factor of tumour growth and apoptosis induced by oxidative stress and several anti-cancer agents. Abnormal expression of mucins was observed in human carcinomas that arise in various gastrointestinal organs. It was widely believed that hepatocellular carcinoma (HCC) does not produce mucins, whereas cholangiocarcinoma (CC) or combined HCC-CC may produce these glycoproteins. However, a growing number of reports shows that mucins can be produced by HCC cells that do not exhibit or are yet to undergo, morphological differentiation to biliary phenotypes. Evaluation of mucin expression levels in precursors and early lesions of CC, as well as other types of primary liver cancer (PLC), conducted in in vitro and in vivo models, allowed to discover the mechanisms of their action, as well as their participation in the most important signalling pathways of liver cystogenesis and carcinogenesis. Analysis of mucin expression in PLC has both basic research and clinical value. Mucins may act as oncogenes and tumour-promoting (e.g., MUC1, MUC13), and/or tumour-suppressing factors (e.g., MUC15). Given their role in promoting PLC progression, both classic (MUC1, MUC2, MUC4, MUC5AC, MUC6) and currently tested mucins (e.g., MUC13, MUC15, MUC16) have been proposed to be important diagnostic and prognostic markers. The purpose of this review was to summarize and update the role of classic and currently tested mucins in pathogenesis of PLC, with explaining the mechanisms of their action in HCC carcinogenesis. It also focuses on determination of the diagnostic and prognostic role of these glycoproteins in PLC, especially focusing on HCC, CC and other hepatic tumours with- and without biliary differentiation.

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“…The accumulation of DimLe x on tumor tissues is a result of the enhanced activity of the β-(1→3)-Glc N Ac transferase and increased fucosylation [ 10 , 11 , 12 ]. Numerous monoclonal antibodies (mAbs) directed against various cancers (gastric cancer, colonic and small cell adenocarcinomas, lung squamous carcinoma) and cancer cell lines (leukemia HL-60, SCLC) were shown to react with the Lewis X (Le x ) determinant similarly to a mAb directed against the stage-specific embryonic antigen-1 (SSEA-1) [ 11 , 13 , 14 , 15 , 16 , 17 , 18 , 19 , 20 , 21 , 22 , 23 , 24 , 25 , 26 ]. Antibodies directed against the Le x determinant (anti-SSEA-1, FH3, etc.)…”

Section: Introductionmentioning

confidence: 99%

Recognition of Dimeric Lewis X by Anti-Dimeric Lex Antibody SH2

et al. 2020

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The carbohydrate antigen dimeric Lewis X (DimLex), which accumulates in colonic and liver adenocarcinomas, is a valuable target to develop anti-cancer therapeutics. Using the native DimLex antigen as a vaccine would elicit an autoimmune response against the Lex antigen found on normal, healthy cells. Thus, we aim to study the immunogenic potential of DimLex and search internal epitopes displayed by DimLex that remain to be recognized by anti-DimLex monoclonal antibodies (mAbs) but no longer possess epitopes recognized by anti-Lex mAbs. In this context, we attempted to map the epitope recognized by anti-DimLex mAb SH2 by titrations and competitive inhibition experiments using oligosaccharide fragments of DimLex as well as Lex analogues. We compare our results with that reported for anti-Lex mAb SH1 and anti-polymeric Lex mAbs 1G5F6 and 291-2G3-A. While SH1 recognizes an epitope localized to the non-reducing end Lex trisaccharide, SH2, 1G5F6, and 291-2G3-A have greater affinity for DimLex conjugates than for Lex conjugates. We show, however, that the Lex trisaccharide is still an important recognition element for SH2, which (like 1G5F6 and 291-2G3-A) makes contacts with all three sugar units of Lex. In contrast to mAb SH1, anti-polymeric Lex mAbs make contact with the GlcNAc acetamido group, suggesting that epitopes extend further from the non-reducing end Lex. Results with SH2 show that this epitope is only recognized when DimLex is presented by glycoconjugates. We have reported that DimLex adopts two conformations around the β-d-GlcNAc-(1→3)-d-Gal bond connecting the Lex trisaccharides. We propose that only one of these conformations is recognized by SH2 and that this conformation is favored when the hexasaccharide is presented as part of a glycoconjugate such as DimLex-bovine serum albumin (DimLex-BSA). Proper presentation of the oligosaccharide candidate via conjugation to a protein or lipid is essential for the design of an anti-cancer vaccine or immunotherapeutic based on DimLex.

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A granulocyte reactive monoclonal antibody, 1G10, identifies the Gal beta 1-4 (Fuc alpha 1-3)GlcNAc (X determinant) expressed in HL-60 cells on both glycolipid and glycoprotein molecules

Cited by 7 publications

References 0 publications

Melanoma × Macrophage Fusion Hybrids Acquire Increased Melanogenesis and Metastatic Potential: Altered N‐Glycosylation as an Underlying Mechanism

Melanoma × Macrophage Fusion Hybrids Acquire Increased Melanogenesis and Metastatic Potential: Altered N‐Glycosylation as an Underlying Mechanism

Mucins: the Old, the New and the Promising Factors in Hepatobiliary Carcinogenesis

Recognition of Dimeric Lewis X by Anti-Dimeric Lex Antibody SH2

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