Common tetrasaccharide epitope NeuAc alpha 2–&gt;3Gal beta 1–&gt;3(Neu-Ac alpha 2–&gt;6)GalNAc, presented by different carrier glycosylceramides or O-linked peptides, is recognized by different antibodies and ligands having distinct specificities.

Saitoh, Sei–Ichi; Levery, Steven B.; Salyan, Mary Ellen K.; Goldberg, R.; Hakomori, Sen‐itiroh

doi:10.1016/s0021-9258(17)37509-9

Cited by 64 publications

(15 citation statements)

References 46 publications

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“…Abs raised against GSLs that were used in this study were: mouse IgM MBr1 against globo-H, mouse IgM 1A4 (E10) against Gb3, mouse IgG 3 DH2 against GM3, mouse IgM MK1-8 against GM2, mouse IgM 9G7 against Gb4, mouse IgM SSEA-3 against Gb5 [14], mouse IgM RM1 against MSGb5 [15] and mouse IgM 5F3 against disialyl-Gb5 [16]. The mouse IgG 3 against MSGb5 was generated by Dr D. Solter (Department of Developmental Biology, Max-Planck Institute of Immunobiology, Freiburg, Germany) and was obtained from the Development Studies Hybridoma Bank [developed under the auspices of the NICHD (National Institute of Child Health and Human Development) and maintained by Abbreviations used: Ab, antibody; BCA, bicinchoninic acid; CMF-HBSS, calcium-and magnesium-free Hanks balanced salt solution; DMEM, Dulbecco's modified Eagle's medium; ECL, enhanced chemiluminescence; ERK, extracellular signal-regulated kinase; ET-18-OMe, 1-O-octadecyl-2-O-methyl-glycerophosphocholine; FAK, focal adhesion kinase; GD3, disialoganglioside 3; GEM, glycosphingolipid-enriched microdomain; GM3, monosialoganglioside 3; GSL, glycosphingolipid; HPTLC, high-performance TLC; mAb, monoclonal Ab; MAPK, mitogen-activated protein kinase; MEK, MAPK/ERK kinase; MMP, matrix metalloproteinase; MSGb5, monosialyl-globoside 5; MT, membrane type; PP1, 4-amino-1-tert-butyl-3-(1naphthyl)pyrazolo [3,4-d]pyrimidine; SSEA-4, stage-specific embryonic antigen-4.…”

Section: Antibodiesmentioning

confidence: 99%

Clustering of monosialyl-Gb5 initiates downstream signalling events leading to invasion of MCF-7 breast cancer cells

Slambrouck

Steelant

2007

Biochemical Journal

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Invasion is a complex process controlled by secretion and activation of proteases, alteration of integrin levels and GSL (glycosphingolipid) patterns. Differential organization of GSLs with specific membrane proteins and signal transducers in GEMs (GSL-enriched microdomains), initiates signalling events to modify cellular phenotype. Although the GSL monosialyl-Gb5 has been linked with invasion, its functional role in invasion is poorly described and understood. To investigate this problem, we induced the invasion of human breast cancer cells and subsequently explored the underlying mechanism. In the present study, the invasion of human MCF-7 breast cancer cells is highly dependent on clustering of monosialyl-Gb5, and the subsequent activation of monosialyl-Gb5-associated focal adhesion kinase and cSrc in GEM leading to the downstream activation of extracellular-signal-regulated kinase (ERK). As a result, we observed increased expression levels and activity of matrix metalloproteinases-2 and -9, which correlated with decreased expression of integrins alpha1 and beta1. Together these results suggest that the organization of crucial molecules in GEMs of MCF-7 cells is critical for their invasive properties.

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Section: Antibodiesmentioning

confidence: 99%

Clustering of monosialyl-Gb5 initiates downstream signalling events leading to invasion of MCF-7 breast cancer cells

Slambrouck

Steelant

2007

Biochemical Journal

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“…Binding of viral S-protein to the cell surface aminopeptidase N, the proteinaceous viral receptor, may be enhanced by bivalent interaction of the S-protein to the protein receptor and to glycans on the host. Expression of MSGG (Mono Sialosyl Galactosyl Globoside), the desialylated DSGG, and of DSGG is found in human erythrocytes and in kidney within the distal tubule and Henle's loop (45). GSL expression can vary in different tissues and MSGG has, for example, been characterized in embryonic stem cells, dorsal root ganglia and tumour tissues.…”

Section: Discussionmentioning

confidence: 99%

Concerns Raised on Blood Group Determinants in Plasma Membrane Interaction of the SARS-CoV-2

Fiedler¹

2021

Preprint

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The SARS-CoV-2 pandemic has resulted in the generation of evolutionary-related variants. The S-protein of the B.1.1.7 variant (deletion N-terminal domain (NTD) His69Val70Tyr144) may contribute to altered infectivity. These mutations may have been presaged by animal mutations in minks housed in mink farms that according to the present analysis by modelling of protein ligand docking altered a high affinity binding site in the S-protein NTD. These mutants likely occurred only sporadically in humans. Tissue-adaptations and the size of the mink relative to the infected human population size back then may have comparatively increased the relative mutation rate. Simple, multi-threaded automated docking that is widely available, assigns increased binding of the blood type II A antigen to the SARS-Cov-2 S-protein NTD of B.1.1.7 with an overall increased docking interaction of blood group A harbouring glycolipids relative to group B or H (H, p=0.04). The top scoring glycan is identified as a DSGG (also classified as sialosyl-MSGG or disialosyl-Gb5) that may compete with heparin, which is similar to heparan sulfate linked to proteinaceous receptors on the tissue surface. Other glycolipids are found to interact with lower affinity, except long ligands that have suitable ligand binding poses to match the curved binding pocket.

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“…Next, the disialosyl-galactosylgloboside was also found to be highly expressed in human renal cancer [18], and the expression of disialosyl-galactosylgloboside is associated with the potential of renal tumor cells metastasizing to the lung. Further study showed that expressing high levels of disialosyl-galactosylgloboside adhere strongly to perialveolar lung tissue sections, and it can be inhibited by a mAb (RMZ), which specifically direct to disialosyt-galactosylgloboside.…”

Section: Renal Cancermentioning

confidence: 97%

Functional Role of Glycosphingolipids in Cancer

Zheng

Terreni

Sollogoub

et al. 2020

CMC

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: Glycosphingolipids (GSLs) are ubiquitous components on animal cell membranes, and exposed on the outer surface. Various studies have demonstrated that they play key roles in cells proliferation, adhesion, motility and differentiation. Usually, the specific types of GSLs are expressed more highly in tumors than in normal tissues, which are known as tumorassociated antigens. It has been revealed that most tumor cells show altered GSLs patterns on their surface, abnormal GSLs signaling and biosynthesis, which together play a major role in tumor development. Tumor-associated GSL antigens have been used in the development of antitumor vaccines. It is no doubt that GSLs play a crucial role in tumor progression and would be a promising target for cancer treatment.

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Common tetrasaccharide epitope NeuAc alpha 2–>3Gal beta 1–>3(Neu-Ac alpha 2–>6)GalNAc, presented by different carrier glycosylceramides or O-linked peptides, is recognized by different antibodies and ligands having distinct specificities.

Cited by 64 publications

References 46 publications

Clustering of monosialyl-Gb5 initiates downstream signalling events leading to invasion of MCF-7 breast cancer cells

Clustering of monosialyl-Gb5 initiates downstream signalling events leading to invasion of MCF-7 breast cancer cells

Concerns Raised on Blood Group Determinants in Plasma Membrane Interaction of the SARS-CoV-2

Functional Role of Glycosphingolipids in Cancer

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