Recognition of Endogenous Ligands by C-Type Lectins:Interaction of Serum Mannan-binding Protein with Tumor-associated Oligosaccharide Epitopes

Kawasaki, Norioki; Kawasaki, Toshisuke

doi:10.4052/tigg.22.141

Cited by 10 publications

(12 citation statements)

References 46 publications

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“…MALDI mass spectrometry of the N-glycans released from CD26 by PNGase F suggested that complex-type N-glycans carrying a minimum of four Le a /Le b epitopes, arranged either as multimeric tandem repeats or terminal epitopes on multiantennary structures, are critically important for the high-affinity binding to MBP. On the basis of these observations, a hypothetical threedimensional model of the MBP-Le oligosaccharide complex was presented (26,27). In this study, we demonstrated that MBP recognizes human primary and metastatic colorectal carcinoma (Table II), and anti-CD3 staining (p = 0.0719) ( Table III), indicating that MBP stains colorectal carcinoma tissues, regardless of those factors.…”

Section: Discussionmentioning

confidence: 80%

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Mannan-Binding Protein, a C-Type Serum Lectin, Recognizes Primary Colorectal Carcinomas through Tumor-Associated Lewis Glycans

Nonaka

Imaeda

Matsumoto

et al. 2014

The Journal of Immunology

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Mannan (mannose)-binding protein (MBP) is a C-type serum lectin that plays a key role in innate immunity. MBP forms large multimers (200–600 kDa) and exhibits broad specificity for mannose, N-acetylglucosamine, and fucose. MBP exhibits high affinity for unique oligosaccharides that have been isolated from human colorectal carcinoma (SW1116) cells and characterized as highly fucosylated high m.w. type 1 Lewis glycans. In this study, we first demonstrated that MBP recognizes human primary colorectal carcinoma tissues through tumor-associated MBP ligands. We performed fluorescence-based histochemistry of MBP in human colorectal carcinoma tissues and showed that MBP clearly stained cancer mucosae in a Ca2+-dependent manner. Coincubation with plant (Aleuria aurantia) lectin, but not Con A, blocked MBP staining, indicating that fucose, rather than mannose, is involved in this interaction. The expression of MBP ligands was detected in 127 of 330 patients (38.5%), whereas, most significantly, there was no expression in 69 nonmalignant tissues. The MBP-staining pattern in cancer mucosae significantly overlapped with that of Lewis b [Fucα1-2Galβ1-3(Fucα1-4)GlcNAc] staining, but the Lewis b staining in normal tissues was not associated with MBP staining. In addition, the MBP staining correlated inversely with the expression of CA19-9 Ag, and MBP stained 11 of 25 (44%) CA19-9 (sialyl Lewis a [NeuAc(α2-3)Galβ1-3(Fucα1-4)GlcNAc])− colorectal carcinoma tissues. We found a favorable prognosis in patients with MBP ligand+ tumors. These results suggest that selective recognition of cancer cells by endogenous MBP seems to be associated with an antitumor effect and that tissue staining with MBP in combination with CA19-9 may serve as a novel indicator of colorectal carcinoma tissues.

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Section: Discussionmentioning

confidence: 80%

“…TO-PRO3 (blue, pseudo-color) was used for counter-staining. proposed structure of the MBP ligands isolated from SW1116 cells) (15,26,27).…”

Section: Mbp Recognizes Colorectal Tumor-derived Le B+ Glycansmentioning

confidence: 99%

Mannan-Binding Protein, a C-Type Serum Lectin, Recognizes Primary Colorectal Carcinomas through Tumor-Associated Lewis Glycans

Nonaka

Imaeda

Matsumoto

et al. 2014

The Journal of Immunology

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“…These glycans are involved in many biological processes including tumor metastasis ( 47 ). Recent studies indicated that Type-I LacNAc-tandem repeats were isolated from SW1116 human colorectal carcinoma cell line ( 28 , 48 , 49 ) and shown as the specific ligands of the tumor-associated human galectin 3 ( 22 , 50 ). Type-I LacNAc-containing glycans can be utilized to gain novel insights about their functional roles, such as interactions with carbohydrate-binding proteins (e.g., galectin 3), fertilization, pathogen adhesion, and inhibitory activity against tumor cells.…”

Section: Synthesis Of Type-i Lacnac Repeating Oligosaccharidesmentioning

confidence: 99%

“…TACA-based antitumor vaccines have shown great potential and high specificity in cancer immunotherapy. Initially, these carbohydrate antigens were isolated from tumor cells only, instead of normal cells ( 23 , 27 , 28 ). To explore the biological significance of tumor-associated antigens or any endogenous glycans, acquiring a sufficient quantity of desirable carbohydrates represents an important task.…”

Section: Introductionmentioning

confidence: 99%

Synthesis of Type-I and Type-II LacNAc-Repeating Oligosaccharides as the Backbones of Tumor-Associated Lewis Antigens

Phang

Lin

2022

Front. Immunol.

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Type-I and Type-II LacNAc are Gal-GlcNAc disaccharides bearing a β1,3- or β1,4-linkage respectively. They exist as the backbones of Lewis antigens that are highly expressed in several cancers. Owing to the promise of developing carbohydrate-based anti-cancer vaccines, glycan synthesis at a large scale is indeed an important task. Synthesis of Type-I and Type-II tandem repeat oligomers has been hampered by the presence of GlcNAc residues. Particularly, N-protecting group plays a determining role in affecting glycosyl donor’s reactivity and acceptor’s nucleophilicity. This review discusses several representative studies that assembled desirable glycans in an efficient manner, such as chemoselective one-pot synthesis and chemoenzymatic methods. Additionally, we also highlight solutions that have been offered to tackle long-lasting problems, e.g., prevention of the oxazoline formation and change of donor/acceptor reactivity. In retrospect of scientific achievements, we present the current restrictions and remaining challenges in this less explored frontier.

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“…Conversely, such characteristic clusters can also signal an aberration tied to malignancy to the innate host-defence system, a surveillance mechanism described in Table 4. In fact, the correspondingly glycosylated glycoproteins CD26/CD98hc are reactive with the collectin mannan-binding lectin, an activator of the complement cascade [41].…”

Section: Activitymentioning

confidence: 99%

Glycobiomarkers by glycoproteomics and glycan profiling (glycomics): emergence of functionality

Gabius

2011

Biochemical Society Transactions

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Glycans stand out from all classes of biomolecules because of their unsurpassed structural complexity. This is generated by variability in anomeric status of the glycosidic bond and its linkage points, ring size, potential for branching and introduction of diverse site-specific substitutions. What poses an enormous challenge for analytical processing is, at the same time, the basis for the fingerprint-like glycomic profiles of glycoconjugates and cells. What's more, the glycosylation machinery is sensitive to disease manifestations, earning glycan assembly a reputation as a promising candidate to identify new biomarkers. Backing this claim for a perspective in clinical practice are recent discoveries that even seemingly subtle changes in the glycan structure of glycoproteins, such as a N-glycan core substitution by a single sugar moiety, have far-reaching functional consequences. They are brought about by altering the interplay between the glycan and (i) its carrier protein and (ii) specific receptors (lectins). Glycan attachment thus endows the protein with a molecular switch and new recognition sites. Co-ordinated regulation of glycan display and presentation of the cognate lectin, e.g. in cancer growth regulation exerted by a tumour suppressor, further exemplifies the broad functional dimension inherent to the non-random shifts in glycosylation. Thus studies on glycobiomarkers converge with research on how distinct carbohydrate determinants are turned into bioactive signals.

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Recognition of Endogenous Ligands by C-Type Lectins:Interaction of Serum Mannan-binding Protein with Tumor-associated Oligosaccharide Epitopes

Cited by 10 publications

References 46 publications

Mannan-Binding Protein, a C-Type Serum Lectin, Recognizes Primary Colorectal Carcinomas through Tumor-Associated Lewis Glycans

Mannan-Binding Protein, a C-Type Serum Lectin, Recognizes Primary Colorectal Carcinomas through Tumor-Associated Lewis Glycans

Synthesis of Type-I and Type-II LacNAc-Repeating Oligosaccharides as the Backbones of Tumor-Associated Lewis Antigens

Glycobiomarkers by glycoproteomics and glycan profiling (glycomics): emergence of functionality

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