Accumulation of free Neu5Ac-containing complex-type N-glycans in human pancreatic cancers

Yabu, Masahiko; Korekane, Hiroaki; Takahashi, Hidenori; Ohigashi, Hajime; Ishikawa, Osamu; Miyamoto, Yasuhide

doi:10.1007/s10719-012-9435-9

Cited by 29 publications

(16 citation statements)

References 19 publications

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“…Most recent studies, however, have shown that similar sialyl-fOSs are accumulated in human pancreatic (33) or prostate cancers (34) but not in normal epithelial cells, thus suggesting that these glycans can serve as useful tumor markers. The mechanisms by which these glycans are accumulated in cancer cells are not understood.…”

Section: Discussionmentioning

confidence: 99%

Basal Autophagy Is Required for the Efficient Catabolism of Sialyloligosaccharides

Seino

Wang

Harada

et al. 2013

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

Basal Autophagy Is Required for the Efficient Catabolism of Sialyloligosaccharides

Seino

Wang

Harada

et al. 2013

Journal of Biological Chemistry

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“…Structural analyses of oligosaccharides associated with pancreatic cancers revealed, unlike colorectal cancer cells, the presence of a variety of free Neu5Ac-containing complex-type N -glycans from three out of the fi ve cases (Table 12.2 ) (Yabu et al 2013b ). The relative amounts of these free Neu5Ac-containing complex-type N -glycans were comparable to or much higher than those of GSLs in most, but not all, pancreatic cancers.…”

Section: Free Oligosaccharidesmentioning

confidence: 96%

Glycomic Analysis of Cancer

Miyamoto

2014

Sugar Chains

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Remarkable alterations in oligosaccharide structures are associated with many human diseases, including cancers. Numerous clinicopathological and biochemical studies have suggested the involvement of aberrant glycosylation in cancer malignancy, such as metastasis and invasion. Furthermore, altered carbohydrate determinants, including tumor-associated carbohydrate antigens such as SLe a (CA19-9), have been utilized as useful tumor markers for the diagnosis of cancer. Cancer glycomic analysis (i.e., precise and comprehensive analysis of altered oligosaccharides in cancer tissues and sera) is a widely used tool for (1) investigating the involvement of glycosylation in cancer malignancy and (2) discovering novel carbohydrate tumor marker candidates. Comprehensive clinico-glycomic studies of glycosphingolipids of colorectal cancers have revealed specifi c alterations related to malignant transformation, as well as characteristic alterations associated with clinical features. Glycomic analyses of colorectal cancers and pancreatic cancers revealed the presence of two kinds of novel fucogangliosides, sialylated type1H (Lewis-negative specifi c antigen) and sialylated type2H, both of which are isomers of sialyl Le x and sialyl Le a . The accumulation of free oligosaccharides in human cancers has been elucidated. Free Neu5Ac-containing complex-type N -glycans accumulated in pancreatic cancers. In addition to these free oligosaccharides, free KDN-containing complex-type N -glycans accumulated in prostate cancers. N -linked and O -linked glycans have also been targets for cancer glycomics. In particular, extensive studies of serum glycomic analyses have been performed to fi nd novel glycan cancer biomarker utilizing newly developed high-throughput platform technologies. It is anticipated that these cancer glycomic studies will lead to the discovery of glycan biomarker or therapy targets for cancers.

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“…This type of glycan is an effective biomarker for pancreatic cancer detection. 24 With these characteristics in mind, the key to constructing a complex-type glycan-targeted material is designing a molecular receptor capable of recognizing and discriminating the core glycan fragment composed of four monosaccharide residues, namely, Neu5Ac-Gal-GlcNAc-Man. In this respect, nature has inspiration for the saccharide receptor design, for example, Maackia amurensis leukoagglutinin displays a strong but A biomimetic design for a sialylated, glycan-specific smart polymer Z Chen et al specific binding with sialylated tri-saccharide (that is, Neu5Ac-α(2-3) Gal-β(1-4)GlcNAc).…”

Section: Introductionmentioning

confidence: 99%

A biomimetic design for a sialylated, glycan-specific smart polymer

Chen

Wang

et al. 2018

NPG Asia Mater

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Increasing evidence has indicated that glycans and their interactions with glycan-specific binding proteins have crucial roles in most physiological processes. One emerging topic in biomaterials is the construction of smart materials capable of recognizing and responding to these valuable glycans. However, because of the complicated compositions and structures as well as the low abundances and microheterogeneity of glycans, developing glycan-responsive materials with a high sensitivity and specificity is a long-term, challenging goal. Here, we report a biomimetic polymer capable of capturing and discriminating sialo-complex-type glycans with the core Neu5Ac-Gal-GlcNAc-Man sequence, which is one of the most effective biomarkers for cancer detection. As an optimized dipeptide, L-Asp-L-Phe has a strong but differential binding affinity for N-acetyl-neuraminic acid (Neu5Ac), N-acetyl-glucosamine (GlcNAc), galactose (Gal), and mannose (Man), which are the core construction units of sialylated glycans. In addition, the L-Asp-L-Phe-grafted polyethyleneimine film displays remarkable adsorption behavior for the model sialylated glycans and can discriminate their linkage isomers, which is accompanied by significant changes in the surface morphology and stiffness. These features facilitate the highly selective capture of sialylated glycopeptides from complex protein samples using PEI-g-L-Asp-L-Phe-modified mSiO 2 @SiO 2 @Fe 3 O 4 core-shell microspheres. The mechanism analysis demonstrates that the favorable polymeric spatial structures and multiple synergetic hydrogen-bonding interactions among the dipeptides and glycan are the main driving forces, indicating a clear direction for designing glycan-specific biomaterials.

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Accumulation of free Neu5Ac-containing complex-type N-glycans in human pancreatic cancers

Cited by 29 publications

References 19 publications

Basal Autophagy Is Required for the Efficient Catabolism of Sialyloligosaccharides

Basal Autophagy Is Required for the Efficient Catabolism of Sialyloligosaccharides

Glycomic Analysis of Cancer

A biomimetic design for a sialylated, glycan-specific smart polymer

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